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| Product | Description | |
|---|---|---|
| 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase | Binds 2 Mg2+ ions that are essential for activity. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase, the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities. Group: Enzymes. Synonyms: 2-amino-4-hydroxy-6-hydroxymethyldi. Enzyme Commission Number: EC 2.7.6.3. CAS No. 37278-23-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3222; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; EC 2.7.6.3; 37278-23-2; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; H2-pteridine-CH2OH pyrophosphokinase; 7,8-dihydroxymethylpterin-pyrophosphokinase; HPPK; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hydroxymethyldihydropteridine pyrophosphokinase; ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase. Cat No: EXWM-3222. |  |
| 3-hydroxypropionate dehydrogenase (NADP+) | Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference. Group: Enzymes. Synonyms: 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.298. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0207; 3-hydroxypropionate dehydrogenase (NADP+); EC 1.1.1.298; 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase. Cat No: EXWM-0207. | |
| 3-hydroxypropionyl-CoA dehydratase | Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea. The enzyme from Metallosphaera sedula acts nearly equally as well on (S)-3-hydroxybutanoyl-CoA but not (R)-3-hydroxybutanoyl-CoA. Group: Enzymes. Synonyms: 3-hydroxypropionyl-CoA hydro-lyase; 3-hydroxypropanoyl-CoA dehydratase. Enzyme Commission Number: EC 4.2.1.116. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4956; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116; 3-hydroxypropionyl-CoA hydro-lyase; 3-hydroxypropanoyl-CoA dehydratase. Cat No: EXWM-4956. | |
| 3-hydroxypropionyl-CoA synthase | Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea.The enzymes from Metallosphaera sedula and Sulfolobus tokodaii can also use propionate, acrylate, acetate, and butanoate as substrates, and are thus different from EC 6.2.1.17 (propionate-CoA ligase), which does not accept acetate or butanoate. Group: Enzymes. Synonyms: 3-hydroxypropionyl-CoA synthetase (AMP-forming); 3-hydroxypropionate-CoA ligase. Enzyme Commission Number: EC 6.2.1.36. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5694; 3-hydroxypropionyl-CoA synthase; EC 6.2.1.36; 3-hydroxypropionyl-CoA synthetase (AMP-forming); 3-hydroxypropionate-CoA ligase. Cat No: EXWM-5694. | |
| 4-hydroxybutanoyl-CoA dehydratase | Contains FAD and a [4Fe-4S] iron-sulfur cluster. The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation, Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation, and Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea. Group: Enzymes. Enzyme Commission Number: EC 4.2.1.120. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4961; 4-hydroxybutanoyl-CoA dehydratase; EC 4.2.1.120. Cat No: EXWM-4961. | |
| 5,10-methylenetetrahydromethanopterin reductase | Catalyses an intermediate step in methanogenesis from CO2 and H2 in methanogenic archaea. Group: Enzymes. Synonyms: 5,10-methylenetetrahydromethanopterin cyclohydrolase; N5,N10-methylenetetrahydromethanopterin reductase; methylene-H4MPT reductase; coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase; N5, N10-methylenetetrahydromethanopterin: coenzyme-F420 oxidoreductase. Enzyme Commission Number: EC 1.5.98.2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1565; 5,10-methylenetetrahydromethanopterin reductase; EC 1.5.98.2; 5,10-methylenetetrahydromethanopterin cyclohydrolase; N5,N10-methylenetetrahydromethanopterin reductase; methylene-H4MPT reductase; coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase; N5, N10-methylenetetrahydromethanopterin: coenzyme-F420 oxidoreductase. Cat No: EXWM-1565. | |
| 5-methyltetrahydrofolate: corrinoid/iron-sulfur protein Co-methyltransferase | Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea. Group: Enzymes. Synonyms: acsE (gene name). Enzyme Commission Number: EC 2.1.1.258. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1862; 5-methyltetrahydrofolate: corrinoid/iron-sulfur protein Co-methyltransferase; EC 2.1.1.258; acsE (gene name). Cat No: EXWM-1862. | |
| acrylyl-CoA reductase (NADPH) | Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea. The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA. Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16. Contains Zn2+. Group: Enzymes. Enzyme Commission Number: EC 1.3.1.84. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1353; acrylyl-CoA reductase (NADPH); EC 1.3.1.84. Cat No: EXWM-1353. | |
| α-D-ribose-1-phosphate 5-kinase (ADP) | The enzyme, characterized from the archaeon Thermococcus kodakarensis, participates in an archaeal pathway for nucleoside degradation. Group: Enzymes. Enzyme Commission Number: EC 2.7.1.212. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3048; α-D-ribose-1-phosphate 5-kinase (ADP); EC 2.7.1.212. Cat No: EXWM-3048. | |
| AMP phosphorylase | The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The activity with CMP and UMP requires activation by cAMP. Group: Enzymes. Synonyms: AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name). Enzyme Commission Number: EC 2.4.2.57. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2687; AMP phosphorylase; EC 2.4.2.57; AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name). Cat No: EXWM-2687. | |
| caldariellaquinol oxidase (H+-transporting) | A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane. Group: Enzymes. Synonyms: SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase caldariellaquinol:O2 oxidoreductase (H+-transporting). Enzyme Commission Number: EC 7.1.1.4 (Formerly EC 1.10.3.13). Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0479; caldariellaquinol oxidase (H+-transporting); EC 1.10.3.13; SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase caldariellaquinol:O2 oxidoreductase (H+-transporting). Cat No: EXWM-0479. | |
| chaperonin ATPase | Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 3.6.4.8 (proteasome ATPase). Group: Enzymes. Synonyms: chaperonin. Enzyme Commission Number: EC 3.6.4.9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4711; chaperonin ATPase; EC 3.6.4.9; chaperonin. Cat No: EXWM-4711. | |
| CTP-dependent riboflavin kinase | This archaeal enzyme differs from EC 2.7.1.26, riboflavin kinase, in using CTP as the donor nucleotide. UTP, but not ATP or GTP, can also act as a phosphate donor but it is at least an order of magnitude less efficient than CTP. Group: Enzymes. Synonyms: Methanocaldococcus jannaschii Mj0056; Mj0056. Enzyme Commission Number: EC 2.7.1.161. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2991; CTP-dependent riboflavin kinase; EC 2.7.1.161; Methanocaldococcus jannaschii Mj0056; Mj0056. Cat No: EXWM-2991. | |
| D-glyceraldehyde dehydrogenase (NADP+) | The enzyme from the archaea Thermoplasma acidophilum and Picrophilus torridus is involved in the non-phosphorylative Entner-Doudoroff pathway. cf. EC 1.2.99.8, glyceraldehyde dehydrogenase (FAD-containing). Group: Enzymes. Synonyms: glyceraldehyde dehydrogenase; GADH. Enzyme Commission Number: EC 1.2.1.89. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1192; D-glyceraldehyde dehydrogenase (NADP+); EC 1.2.1.89; glyceraldehyde dehydrogenase; GADH. Cat No: EXWM-1192. | |
| dihydromethanopterin reductase (acceptor) | This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+]. Group: Enzymes. Synonyms: DmrX. Enzyme Commission Number: EC 1.5.99.15. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1569; dihydromethanopterin reductase (acceptor); EC 1.5.99.15; DmrX. Cat No: EXWM-1569. | |
| dihydroneopterin aldolase | The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyse the epimerisation of the 2' hydroxy-group (EC 5.1.99.8, 7,8-dihydroneopterin epimerase). The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyses EC 5.1.99.8 and EC 1.13.11.81, 7,8-dihydroneopterin oxygenase. The enzyme from the yeast Saccharomyces cerevisiae also catalyses the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3, 2-amino-4-hydroxy-6-(hydroxymethyl)dihydropteridine diphosphokinase, and EC 2.5.1.15, dihydropteroate synthase. Group: Enzymes. Synonyms: 7,8-dihydroneopterin aldolase; 2-amino-. Enzyme Commission Number: EC 4.1.2.25. CAS No. 37290-59-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4864; dihydroneopterin aldolase; EC 4.1.2.25; 37290-59-8; 7,8-dihydroneopterin aldolase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming); DHNA; mptD (gene name); folB (gene name). Cat No: EXWM-4864. | |
| dihydropteroate synthase | The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25, dihydroneopterin aldolase. Group: Enzymes. Synonyms: dihydropteroate pyrophosphorylase; DHPS; 7,8-dihydropteroate synthase; 7,8-dihydr. Enzyme Commission Number: EC 2.5.1.15. CAS No. 9055-61-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2751; dihydropteroate synthase; EC 2.5.1.15; 9055-61-2; dihydropteroate pyrophosphorylase; DHPS; 7,8-dihydropteroate synthase; 7,8-dihydropteroate synthetase; 7,8-dihydropteroic acid synthetase; dihydropteroate synthetase; dihydropteroic synthetase; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase; (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase. Cat No: EXWM-2751. | |
| diphthine methyl ester synthase | This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98). The relevant histidine of elongation factor 2 is His715 in mammals and His699 in yeast. The order of the 4 methylations is not known. Group: Enzymes. Synonyms: S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Enzyme Commission Number: EC 2.1.1.314. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1922; diphthine methyl ester synthase; EC 2.1.1.314; S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Cat No: EXWM-1922. | |
| diphthine synthase | This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14, diphthine-ammonia ligase. Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314). In the archaeon Pyrococcus horikoshii the enzyme acts on His600 of elongation factor 2. Group: Enzymes. Synonyms: S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] methyltransferase; Dph5 (ambiguous). Enzyme Commission Number: EC 2.1.1.98. CAS No. 114514-25-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1998; diphthine synthase; EC 2.1.1.98; 114514-25-9; S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] methyltransferase; Dph5 (ambiguous). Cat No: EXWM-1998. | |
| DNA ligase (ATP, ADP or GTP) | The enzymes from the archaea Hyperthermus butylicus and Sulfophobococcus zilligii are active with ATP, ADP or GTP. They show no activity with NAD+. Different from EC 6.5.1.1, DNA ligase (ATP), which is specific for ATP, and EC 6.5.1.6, DNA ligase (ATP or NAD+) which can utilize either ATP or NAD+. Group: Enzymes. Enzyme Commission Number: EC 6.5.1.7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5826; DNA ligase (ATP, ADP or GTP); EC 6.5.1.7. Cat No: EXWM-5826. | |
| DNA ligase (ATP or NAD+) | The enzymes from the archaea Thermococcus fumicolans and Thermococcus onnurineus show high activity with either ATP or NAD+, and significantly lower activity with TTP, GTP, and CTP. Different from EC 6.5.1.1, DNA ligase (ATP), EC 6.5.1.2, DNA ligase (NAD+) and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP). Group: Enzymes. Enzyme Commission Number: EC 6.5.1.6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5825; DNA ligase (ATP or NAD+); EC 6.5.1.6. Cat No: EXWM-5825. | |
| dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase | The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, participates in the N-glycosylation of proteins. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain. Group: Enzymes. Synonyms: AglC; UDP-Glc-2,3-diNAcA glycosyltransferase. Enzyme Commission Number: EC 2.4.1.335. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2573; dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase; EC 2.4.1.335; AglC; UDP-Glc-2,3-diNAcA glycosyltransferase. Cat No: EXWM-2573. | |
| dolichyl-phosphooligosaccharide-protein glycotransferase | The enzyme, characterized from the archaea Methanococcus voltae and Haloferax volcanii, transfers a glycan component from dolichyl phosphooligosaccharide to external proteins. It is different from EC 2.4.99.18, dolichyl-diphosphooligosaccharide-protein glycotransferase, which uses dolichyl diphosphate as carrier compound in bacteria and eukaryotes. The enzyme participates in the N-glycosylation of proteins in some archaea. It requires Mn2+. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain. Group: Enzymes. Synonyms: AglB; archaeal oligosaccharyl transferase; dolichyl-monophosphooligosaccharide-protein glycotransferase. Enzyme Commission Number: EC 2.4.99.21. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2706; dolichyl-phosphooligosaccharide-protein glycotransferase; EC 2.4.99.21; AglB; archaeal oligosaccharyl transferase; dolichyl-monophosphooligosaccharide-protein glycotransferase. Cat No: EXWM-2706. | |
| formate dehydrogenase (coenzyme F420) | The enzyme from methanogenic archaea is a involved in formate-dependent H2 production. It contains noncovalently bound FAD. Group: Enzymes. Synonyms: coenzyme F420 reducing formate dehydrogenase; coenzyme F420-dependent formate dehydrogenase. Enzyme Commission Number: EC 1.2.99.9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1237; formate dehydrogenase (coenzyme F420); EC 1.2.99.9; coenzyme F420 reducing formate dehydrogenase; coenzyme F420-dependent formate dehydrogenase. Cat No: EXWM-1237. | |
| formate-phosphoribosyl aminoimidazolecarboxamide ligase | This archaeal enzyme, characterized from the methanogen Methanocaldococcus jannaschii, catalyses a step in the synthesis of purine nucleotides. It differs from the orthologous bacterial/eukaryotic enzymes, which utilize 10-formyltetrahydrofolate rather than formate and ATP. cf. EC 2.1.2.3, phosphoribosyl aminoimidazolecarboxamide formyltransferase. Group: Enzymes. Synonyms: 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase; 5-formaminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5'-monophosphate synthetase; purP (gene name). Enzyme Commission Number: EC 6.3.4.23. CAS No. 9032-3-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5793; formate-phosphoribosyl aminoimidazolecarboxamide ligase; EC 6.3.4.23; 9032-03-5; 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase; 5-formaminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5'-monophosphate synthetase; purP (gene name). Cat No: EXWM-5793. | |
| glucose-6-phosphate dehydrogenase (NAD+) | The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the archaeon Haloferax volcanii is specific for NAD+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+). Group: Enzymes. Synonyms: Glc6PDH; azf (gene name); archaeal zwischenferment. Enzyme Commission Number: EC 1.1.1.388. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0307; glucose-6-phosphate dehydrogenase (NAD+); EC 1.1.1.388; Glc6PDH; azf (gene name); archaeal zwischenferment. Cat No: EXWM-0307. | |
| ketol-acid reductoisomerase [NAD(P)+] | The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.382, ketol-acid reductoisomerase (NAD+)]. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.383. CAS No. 9075-2-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0302; ketol-acid reductoisomerase [NAD(P)+]; EC 1.1.1.383; 9075-02-9. Cat No: EXWM-0302. | |
| L-iditol 2-dehydrogenase | This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+. Group: Enzymes. Synonyms: polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. SDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0043; L-iditol 2-dehydrogenase; EC 1.1.1.14; 9028-21-1; polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Cat No: EXWM-0043. | |
| [lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase | The enzymes from the thermophilic bacterium Thermus thermophilus and the thermophilic archaea Sulfolobus acidocaldarius and Sulfolobus tokodaii protect the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW. This reaction is part of the lysine biosynthesis pathway in these organisms. Group: Enzymes. Synonyms: α-aminoadipate-lysW ligase lysX (gene name); LysX (ambiguous); AAA-LysW ligase. Enzyme Commission Number: EC 6.3.2.43. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5761; [lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase; EC 6.3.2.43; α-aminoadipate-lysW ligase lysX (gene name); LysX (ambiguous); AAA-LysW ligase. Cat No: EXWM-5761. | |
| malonyl-CoA reductase (malonate semialdehyde-forming) | Requires Mg2+. Catalyses the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and some thermoacidophilic archaea, respectively. The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the next reaction in the pathway, EC 1.1.1.298 [3-hydroxypropionate dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: NADP-dependent malonyl CoA reductase; malonyl CoA reductase (NADP); malonyl CoA reductase (malonate semialdehyde-forming). Enzyme Commission Number: EC 1.2.1.75. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1177; malonyl-CoA reductase (malonate semialdehyde-forming); EC 1.2.1.75; NADP-dependent malonyl CoA reductase; malonyl CoA reductase (NADP); malonyl CoA reductase (malonate semialdehyde-forming). Cat No: EXWM-1177. | |
| mevalonate 3-kinase | Mevalonate 3-kinase and mevalonate-3-phosphate-5-kinase (EC 2.7.1.186) act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum. Mevalonate 3-kinase is different from mevalonate kinase, EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea. Group: Enzymes. Synonyms: ATP:(R)-MVA 3-phosphotransferase. Enzyme Commission Number: EC 2.7.1.185. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3017; mevalonate 3-kinase; EC 2.7.1.185; ATP:(R)-MVA 3-phosphotransferase. Cat No: EXWM-3017. | |
| N1-aminopropylagmatine synthase | The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase. Group: Enzymes. Synonyms: agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE; agmatine aminopropyltransferase. Enzyme Commission Number: EC 2.5.1.104. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2720; N1-aminopropylagmatine synthase; EC 2.5.1.104; agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE; agmatine aminopropyltransferase. Cat No: EXWM-2720. | |
| NADH oxidase (H2O2-forming) | A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O2-forming enzyme and a H2O-forming enzyme (cf. EC 1.6.3.4, NADH oxidase (H2O-forming)). The enzymes from the anaerobic archaea Methanocaldococcus jannaschii and Pyrococcus furiosus also produce low amounts of H2O. Unlike EC 1.6.3.1 (NAD(P)H oxidase) it has no activity towards NADPH. Group: Enzymes. Synonyms: NOX-1; H2O2-forming NADH oxidase. Enzyme Commission Number: EC 1.6.3.3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1585; NADH oxidase (H2O2-forming); EC 1.6.3.3; NOX-1; H2O2-forming NADH oxidase. Cat No: EXWM-1585. | |
| NAD Kinase (Crude Enzyme) | NAD + kinase (EC 2. 7. 1. 23, NADK) is an enzyme that converts nicotinamide adenine dinucleotide (NAD + ) into NADP + through phosphorylating the NAD + coenzyme. NADP + is an essential coenzyme that is reduced to NADPH primarily by the pentose phosphate pathway to provide reducing power in biosynthetic processes such as fatty acid biosynthesis and nucleotide synthesis. The structure of the NADK from the archaean Archaeoglobus fulgidus has been determined. In humans, the genes NADK and MNADK encode NAD + kinases localized in cytosol and mitochondria,respectively. Similarly, yeast have both cytosolic and mitochondrial isoforms, and the yeast mitochondrial isoform accepts both NAD + and NADH as substrates for phosphorylation. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; agriculture; analysis. Group: Enzymes. Synonyms: DPN kinase; nicotinamide adenine dinucleotide kinase (phosphorylating); nicotinamide adenine dinucleotide kin. Enzyme Commission Number: EC 2.7.1.23. CAS No. 9032-66-0. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. DPN kinase; nicotinamide adenine dinucleotide kinase (phosphorylating); nicotinamide adenine dinucleotide kinase; NAD kinase; NADK. Pack: 100ml. Cat No: NATE-1824. | |
| Native Aspergillus melleus Proteinase | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Applications: Proteinase is an enzyme used to break down proteins by hydrolyzing peptide bonds. proteinase is used to degrade proteins, to study proteinase inhibitors and to study thermal inactivation kinetics. proteinase is used in nucleic acid isolation procedures in incubations. it is used to study proteinase-activated receptors, such as the transducers of proteinase-mediated signaling in inflammation and the immune response. it is from aspergillus melleus and has been used to non-specifically degraded xylanase from streptomyces halstedii. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Proteinase. Activity: > 3 units/mg solid. Storage: 2-8°C. Source: Aspergillus melleus. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0638. | |
| Native Bovine Protease | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Derived from new zealand-sourced pancreas. Applications: Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. this product is from bovine pancreas. protease from bovine pancrease (type i) has been used for the extraction of hemicellulose. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 5 units/mg solid. Storage: -20°C. Source: bovine pancreas. Species: Bovine. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0628. | |
| Native Rhizopus sp. Protease | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Acidic protease exhibits both proteolytic and lipolytic activities. stable in the acid range of ph 3-5. ph optimum is 3.0. Applications: Protease from rhizopus spp. has been used in a study to assess the amino acid sequences near the amino termini using automated edman degradation. it has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-dl-norleucine methyl ester in the presence of cupric acetate. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 0.2 unit/mg solid. Storage: 2-8°C. Form: Supplied as a powder containing dextrin as a stabilizer. Source: Rhizopus sp. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0629. | |
| nitric-oxide synthase [NAD(P)H] | Binds heme (iron protoporphyrin IX) and tetrahydrobiopterin. Most of the bacterial and archaeal enzymes consist of only an oxidase domain and function together with bacterial ferredoxins. The enzyme from the Δ-proteobacterium Sorangium cellulosum also includes a reductase domain that binds FAD, FMN and a [2Fe-2S] cluster. The similar enzymes from plants and animals use only NADPH as acceptor (cf. EC 1.14.13.39). Group: Enzymes. Synonyms: nitric oxide synthetase; NO synthase. Enzyme Commission Number: EC 1.14.13.165. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0764; nitric-oxide synthase [NAD(P)H]; EC 1.14.13.165; nitric oxide synthetase; NO synthase. Cat No: EXWM-0764. | |
| Phosphatase from Escherichia coli, Recombinant | A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase. Another large group of proteins present in archaea, bacteria, and eukaryote exhibits deoxyribonucleotide and ribonucleotide phosphatase or pyrophosphatase activities that catalyse the decomposition of dNTP/NTP into dNDP/NDP and a free phosphate ... phosphatase is collectively called as protein phosphatase, which removes a phosphate group from the phosphorylated amino acid residue of the substrate protein. Protein phosphorylation is a common posttranslational modification of protein catalyzed by protein kinases, and protein phosphatases reverse the effect. Group: Enzymes. Synonyms: HAD2. Enzyme Commission Number: EC 3.1.3.-. Purity: >95 % as judged by SDS-PAGE. Phosphatase. Mole weight: 26827.7 Da. Activity: 1.905 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. MG1655. Phosphatase; HAD2; EC 3.1.3.-. Cat No: NATE-1226. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-independent) | The enzymes from higher plants, algae, fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction. Group: Enzymes. Synonyms: cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); pho. Enzyme Commission Number: EC 5.4.2.12. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5523; phosphoglycerate mutase (2,3-diphosphoglycerate-independent); EC 5.4.2.12; cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); iPGM; iPGAM; PGAM-i. Cat No: EXWM-5523. | |
| porphobilinogen synthase | The enzyme catalyses the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. The enzymes from most organisms utilize metal ions (Zn2+, Mg2+, K+, and Na+) as cofactors that reside at multiple sites, including the active site and allosteric sites. Enzymes from archaea, yeast, and metazoa (including human) contain Zn2+ at the active site. In humans, the enzyme is a primary target for ...; 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing); hemB (gene name). Enzyme Commission Number: EC 4.2.1.24. CAS No. 9036-37-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5016; porphobilinogen synthase; EC 4.2.1.24; 9036-37-7; aminolevulinate dehydratase; Δ-aminolevulinate dehydratase; Δ-aminolevulinic acid dehydrase; Δ-aminolevulinic acid dehydratase; aminolevulinic dehydratase; Δ-aminolevulinic dehydratase; 5-levulinic acid dehydratase; 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing); hemB (gene name). Cat No: EXWM-5016. | |
| preflagellin peptidase | An aspartic peptidase from Archaea but not bacteria. In peptidase family A24 (type IV prepilin peptidase family). Group: Enzymes. Synonyms: FlaK. Enzyme Commission Number: EC 3.4.23.52. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4290; preflagellin peptidase; EC 3.4.23.52; FlaK. Cat No: EXWM-4290. | |
| rhomboid protease | These endopeptidases are multi-spanning membrane proteins. Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. A catalytic dyad is involved in proteolysis rather than a catalytic triad, as was thought previously. They are important for embryo development in Drosophila melanogaster. Rhomboid is a key regulator of EGF receptor signalling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. Belongs in peptidase family S54. Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. Rhomboids are widely conserved from bacteria to archaea to humans. Group: Enzymes. Enzyme Commission Number: EC 3.4.21.105. CAS No. 713145-02-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4100; rhomboid protease; EC 3.4.21.105; 713145-02-9. Cat No: EXWM-4100. | |
| Ribonuclease H from Escherichia coli, Recombinant | Ribonuclease H (RNase H) is a family of non-sequence-specific endonucleases that catalyze the cleavage of RNA via a hydrolytic mechanism. Members of the RNase H family can be found in nearly all organisms, from bacteria to archaea to eukaryotes. RNase Hs ribonuclease activity cleaves the 3-O-P bond of RNA in a DNA/RNA duplex substrate to produce 3-hydroxyl and 5-phosphate terminated products. In DNA replication, RNase H is responsible for removing the RNA primer, allowing completion of the newly synthesized DNA. Applications: Ribonuclease h from escherichia coli has been used in a study to assess metallobi ochemistry of the magnesium ion. ribonuclease h has also been used in a study to investigate selective inhibitors of hiv-1 reverse transcriptase ass ociated rnase h activity. Group: Enzymes. Synonyms: Ribonuclease H; RNase H; EC 3.1.4.34; 9050-76-4. Enzyme Commission Number: EC 3.1.4.34. CAS No. 9050-76-4. Rnase. Activity: 1,000-4,000 units/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 20 mM Tris-HCl, pH 7.5, 100 mM KCl, 10 mM MgCl2, 0.1 mM EDTA, 0.1 mM DTT and 0.05 mg BSA per ml. Source: E. coli. Species: Escherichia coli. Ribonuclease H; RNase H; EC 3.1.4.34; 9050-76-4. Pack: vial of ~30 units. Cat No: NATE-0657. | |
| secondary-alcohol dehydrogenase (coenzyme-F420) | The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones. Group: Enzymes. Synonyms: F420-dependent alcohol dehydrogenase; secondary alcohol:F420 oxidoreductase; F420-dependent secondary alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.98.5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0442; secondary-alcohol dehydrogenase (coenzyme-F420); EC 1.1.98.5; F420-dependent alcohol dehydrogenase; secondary alcohol:F420 oxidoreductase; F420-dependent secondary alcohol dehydrogenase. Cat No: EXWM-0442. | |
| succinate dehydrogenase | A flavoprotein (FAD) complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria and archaea. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. cf. EC 1.3.5.4, fumarate reductase (quinone). Group: Enzymes. Synonyms: succinate dehydrogenase (quinone); succinate dehydrogenase (ubiquinone); succinic dehydrogenase; complex II (ambiguous); succinate dehydrogenase complex; SDH; succinate:ubiquinone oxidoreductase. Enzyme Commission Number: EC 1.3.5.1. CAS No. 9028-11-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1385; succinate dehydrogenase; EC 1.3.5.1; 9028-11-9; succinate dehydrogenase (quinone); succinate dehydrogenase (ubiquinone); succinic dehydrogenase; complex II (ambiguous); succinate dehydrogenase complex; SDH; succinate:ubiquinone oxidoreductase. Cat No: EXWM-1385. | |
| sulfofructose kinase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihV (gene name). Enzyme Commission Number: EC 2.7.1.184. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3016; sulfofructose kinase; EC 2.7.1.184; yihV (gene name). Cat No: EXWM-3016. | |
| sulfofructosephosphate aldolase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihT (gene name). Enzyme Commission Number: EC 4.1.2.57. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4894; sulfofructosephosphate aldolase; EC 4.1.2.57; yihT (gene name). Cat No: EXWM-4894. | |
| sulfolactaldehyde 3-reductase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihU (gene name). Enzyme Commission Number: EC 1.1.1.373. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0291; sulfolactaldehyde 3-reductase; EC 1.1.1.373; yihU (gene name). Cat No: EXWM-0291. | |
| sulfoquinovose isomerase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihS (gene name). Enzyme Commission Number: EC 5.3.1.31. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5471; sulfoquinovose isomerase; EC 5.3.1.31; yihS (gene name). Cat No: EXWM-5471. | |
| tetrahydromethanopterin S-methyltransferase | Involved in the formation of methane from CO in Methanobacterium thermoautotrophicum. Methanopterin is a pterin analogue. The reaction involves the export of one or two sodium ions in Archaea. Group: Enzymes. Synonyms: tetrahydromethanopterin methyltransferase. Enzyme Commission Number: EC 2.1.1.86. CAS No. 103406-60-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1987; tetrahydromethanopterin S-methyltransferase; EC 2.1.1.86; 103406-60-6; tetrahydromethanopterin methyltransferase. Cat No: EXWM-1987. | |
| tRNA 4-demethylwyosine synthase (AdoMet-dependent) | This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine. The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine. Group: Enzymes. Synonyms: TYW1. Enzyme Commission Number: EC 4.1.3.44. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4921; tRNA 4-demethylwyosine synthase (AdoMet-dependent); EC 4.1.3.44; TYW1. Cat No: EXWM-4921. | |
| tRNA (guanine10-N2)-methyltransferase | In contrast to the archaeal enzyme tRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213), tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA. Group: Enzymes. Synonyms: (m2G10) methyltransferase; Trm11-Trm112 complex. Enzyme Commission Number: EC 2.1.1.214. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1816; tRNA (guanine10-N2)-methyltransferase; EC 2.1.1.214; (m2G10) methyltransferase; Trm11-Trm112 complex. Cat No: EXWM-1816. | |
| tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase | The enzyme from Aquifex aeolicus is similar to the TRM1 methyltransferases of archaea and eukarya (see EC 2.1.1.216, tRNA (guanine26-N2)-dimethyltransferase). However, it catalyses the double methylation of guanines at both positions 26 and 27 of tRNA. Group: Enzymes. Synonyms: Trm1 (ambiguous); tRNA (N2,N2-guanine)-dimethyltransferase; tRNA (m2(2G26) methyltransferase; Trm1[tRNA (m2(2)G26) methyltransferase]. Enzyme Commission Number: EC 2.1.1.215. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1817; tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase; EC 2.1.1.215; Trm1 (ambiguous); tRNA (N2,N2-guanine)-dimethyltransferase; tRNA (m2(2G26) methyltransferase; Trm1[tRNA (m2(2)G26) methyltransferase]. Cat No: EXWM-1817. | |
| tRNAIle2-agmatinylcytidine synthase | The enzyme from the archaeon Archaeoglobus fulgidus modifies the wobble base of the CAU anticodon of the archaeal tRNAIle2 at the oxo group in position 2 of cytidine34. This modification is crucial for accurate decoding of the genetic code. In bacteria EC 6.3.4.19, tRNAIle-lysidine synthase, catalyses the modification of [tRNAIle2]-cytidine34 to [tRNAIle2]-lysidine34. Group: Enzymes. Synonyms: TiaS; AF2259; tRNAIle-2-agmatinylcytidine synthetase; tRNAIle-agm2C synthetase; tRNAIle-agmatidine synthetase. Enzyme Commission Number: EC 6.3.4.22. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5792; tRNAIle2-agmatinylcytidine synthase; EC 6.3.4.22; TiaS; AF2259; tRNAIle-2-agmatinylcytidine synthetase; tRNAIle-agm2C synthetase; tRNAIle-agmatidine synthetase. Cat No: EXWM-5792. | |
| tRNA pseudouridine55 synthase | Pseudouridine synthase TruB from Escherichia coli specifically modifies uridine55 in tRNA molecules. The bifunctional archaeal enzyme also catalyses the pseudouridylation of uridine54. It is not known whether the enzyme from Escherichia coli can also act on position 54 in vitro, since this position is occupied in Escherichia coli tRNAs by thymine. Group: Enzymes. Synonyms: TruB; aCbf5; Pus4; YNL292w (gene name); ψ55 tRNA pseudouridine synthase; tRNA:ψ55-synthase; tRNA pseudouridine 55 synthase; tRNA:pseudouridine-55 synthase; ψ55 synthase; tRNA ψ55 synthase; tRNA:ψ55 synthase; tRNA-uridine55 uracil mutase; Pus10; tRNA-uridine54/55 uracil mutase. Enzyme Commission Number: EC 5.4.99.25. CAS No. 430429-15-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5565; tRNA pseudouridine55 synthase; EC 5.4.99.25; 430429-15-5; TruB; aCbf5; Pus4; YNL292w (gene name); ψ55 tRNA pseudouridine synthase; tRNA:ψ55-synthase; tRNA pseudouridine 55 synthase; tRNA:pseudouridine-55 synthase; ψ55 synthase; tRNA ψ55 synthase; tRNA:ψ55 synthase; tRNA-uridine55 uracil mutase; Pus10; tRNA-uridine54/55 uracil mutase. Cat No: EXWM-5565. | |
| tyramine-L-glutamate ligase | The enzyme, which has been characterized from the archaea Methanocaldococcus fervens, participates in the biosynthesis of the cofactor methanofuran. Requires a divalent cation for activity, with Mn2+ giving the highest activity, followed by Mg2+, Co2+, Zn2+, and Fe2+. Group: Enzymes. Synonyms: mfnD (gene name). Enzyme Commission Number: EC 6.3.4.24. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5794; tyramine-L-glutamate ligase; EC 6.3.4.24; mfnD (gene name). Cat No: EXWM-5794. | |
| UDP-N-acetylglucosamine diphosphorylase | Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Hemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase. The enzyme from plants and animals is also active toward N-acetyl-α-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase), while the bacterial enzyme shows low activity toward that substrate. Group: Enzymes. Synonyms: UDP-N-acetylglucosamine pyroph. Enzyme Commission Number: EC 2.7.7.23. CAS No. 9023-6-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3236; UDP-N-acetylglucosamine diphosphorylase; EC 2.7.7.23; 9023-06-7; UDP-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine pyrophosphorylase; UTP:2-acetamido-2-deoxy-α-D-glucose-1-phosphate uridylyltransferase; UDP-GlcNAc pyrophosphorylase; GlmU uridylyltransferase; Acetylglucosamine 1-phosphate uridylyltransferase; UDP-acetylglucosamine pyrophosphorylase; uridine diphosphate-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine phosphorylase; acetylglucosamine 1-phosphate uridylyltransferase. Cat No: EXWM-3236. | |
| XTP/dITP diphosphatase | The enzymes from the bacterium Escherichia coli and the archaea Methanococcus jannaschii and Archaeoglobus fulgidus are highly specific for XTP and dITP. The activity is dependent on divalent cations, Mg2+ is preferred. Group: Enzymes. Synonyms: hypoxanthine/xanthine dNTP pyrophosphatase; rdgB (gene name). Enzyme Commission Number: EC 3.6.1.66. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4639; XTP/dITP diphosphatase; EC 3.6.1.66; hypoxanthine/xanthine dNTP pyrophosphatase; rdgB (gene name). Cat No: EXWM-4639. | |
| 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase | A flavoprotein (FAD). The enzyme is involved in the biosynthesis of archaeal membrane lipids. It catalyses the reduction of all 8 double bonds in 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipids and all 4 double bonds in 3-O-geranylgeranyl-sn-glycerol phospholipids with comparable activity. Unlike EC 1.3.1.101, 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H], this enzyme shows no activity with NADPH, and requires a dedicated ferredoxin. Group: Enzymes. Synonyms: AF0464 (gene name); 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase (donor). Enzyme Commission Number: EC 1.3.7.11. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1392; 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase; EC 1.3.7.11; AF0464 (gene name); 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase (donor). Cat No: EXWM-1392. | |
| 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase | The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions. Group: Enzymes. Synonyms: ArfB. Enzyme Commission Number: EC 3.5.1.102. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4381; 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; EC 3.5.1.102; ArfB. Cat No: EXWM-4381. | |
| 2-phospho-L-lactate guanylyltransferase | This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria. Group: Enzymes. Synonyms: CofC; MJ0887. Enzyme Commission Number: EC 2.7.7.68. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3279; 2-phospho-L-lactate guanylyltransferase; EC 2.7.7.68; CofC; MJ0887. Cat No: EXWM-3279. | |
| 2-phospho-L-lactate transferase | This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria. Group: Enzymes. Synonyms: LPPG:Fo 2-phospho-L-lactate transferase; LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase; MJ1256; lactyl-2-diphospho-(5')guanosine:Fo 2-phospho-L-lactate transferase; CofD. Enzyme Commission Number: EC 2.7.8.28. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3327; 2-phospho-L-lactate transferase; EC 2.7.8.28; LPPG:Fo 2-phospho-L-lactate transferase; LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase; MJ1256; lactyl-2-diphospho-(5')guanosine:Fo 2-phospho-L-lactate transferase; CofD. Cat No: EXWM-3327. | |
| 4-phosphopantoate-β-alanine ligase | The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with β-alanine, followed by phosphorylation (EC 6.3.2.1 [pantoate-β-alanine ligase] and EC 2.7.1.33 [pantothenate kinase], respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with β-alanine. The two archaeal enzymes that catalyse this conversion are EC 2.7.1.169, pantoate kinase, and this enzyme. Group: Enzymes. Synonyms: phosphopantothenate synthetase; TK1686 protein. Enzyme Commission Number: EC 6.3.2.36. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5753; 4-phosphopantoate-β-alanine ligase; EC 6.3.2.36; phosphopantothenate synthetase; TK1686 protein. Cat No: EXWM-5753. | |
| 5,6,7,8-tetrahydromethanopterin hydro-lyase | Found in methylotrophic bacteria and methanogenic archaea. Group: Enzymes. Synonyms: formaldehyde-activating enzyme. Enzyme Commission Number: EC 4.2.1.147. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4988; 5,6,7,8-tetrahydromethanopterin hydro-lyase; EC 4.2.1.147; formaldehyde-activating enzyme. Cat No: EXWM-4988. | |
| (5-formylfuran-3-yl)methyl phosphate synthase | The enzyme catalyses the reaction in the direction of producing (5-formylfuran-3-yl)methyl phosphate, an intermediate in the biosynthesis of methanofuran. The sequence of events starts with the removal of a phosphate group, followed by aldol condensation and cyclization. Methanofuran is a carbon-carrier cofactor involved in the first step of the methanogenic reduction of carbon dioxide by methanogenic archaea. Group: Enzymes. Synonyms: mfnB (gene name); 4-HFC-P synthase; 4-(hydroxymethyl)-2-furaldehyde phosphate synthase. Enzyme Commission Number: EC 4.2.3.153. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5168; (5-formylfuran-3-yl)methyl phosphate synthase; EC 4.2.3.153; mfnB (gene name); 4-HFC-P synthase; 4-(hydroxymethyl)-2-furaldehyde phosphate synthase. Cat No: EXWM-5168. | |
| adenosylcobinamide hydrolase | Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB). Group: Enzymes. Synonyms: CbiZ; AdoCbi amidohydrolase. Enzyme Commission Number: EC 3.5.1.90. CAS No. 905988-16-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4482; adenosylcobinamide hydrolase; EC 3.5.1.90; 905988-16-1; CbiZ; AdoCbi amidohydrolase. Cat No: EXWM-4482. | |
| anaerobic carbon-monoxide dehydrogenase | This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [...-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Enzyme Commission Number: EC 1.2.7.4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1227; anaerobic carbon-monoxide dehydrogenase; EC 1.2.7.4; Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Cat No: EXWM-1227. | |
| archaetidylinositol phosphate synthase | Requires Mg2+ or Mn2+ for activity. The enzyme is involved in biosynthesis of archaetidyl-myo-inositol, a compound essential for glycolipid biosynthesis in archaea. Group: Enzymes. Synonyms: AIP synthase. Enzyme Commission Number: EC 2.7.8.39. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3338; archaetidylinositol phosphate synthase; EC 2.7.8.39; AIP synthase. Cat No: EXWM-3338. | |
| β-ribofuranosylphenol 5'-phosphate synthase | The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It was initially thought to use 4-aminobenzoate as a substrate, but was later shown to utilize 4-hydroxybenzoate. The activity is dependent on Mg2+ or Mn2+. Group: Enzymes. Synonyms: β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); β-ribofuranosylhydroxybenzene 5'-phosphate synthase; 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5'-phosphate synthase (incorrect); 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-rib. Enzyme Commission Number: EC 2.4.2.54. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2684; β-ribofuranosylphenol 5'-phosphate synthase; EC 2.4.2.54; β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); β-ribofuranosylhydroxybenzene 5'-phosphate synthase; 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5'-phosphate synthase (incorrect); 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) (incorrect). Cat No: EXWM-2684. | |
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