Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
Search for products or services, then visit the American suppliers website for prices, SDS or more information. You can also view suppliers in Australia, NZ or the UK.
| Product | Description | |
|---|---|---|
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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-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. | |
| IMP cyclohydrolase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is IMP 1,2-hydrolase (decyclizing). Other names in common use include inosinicase, and inosinate cyclohydrolase. This enzyme catalyses the cyclisation of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP, a reaction which is important in de novo purine biosynthesis in archaeal species. Group: Enzymes. Synonyms: inosinicase; inosinate cyclohydrolase; IMP 1,2-hydrolase (decyclizing). Enzyme Commission Number: EC 3.5.4.10. CAS No. 9013-81-4. 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-4537; IMP cyclohydrolase; EC 3.5.4.10; 9013-81-4; inosinicase; inosinate cyclohydrolase; IMP 1,2-hydrolase (decyclizing). Cat No: EXWM-4537. | |
| methylornithine synthase | The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases. Group: Enzymes. Synonyms: PylB. Enzyme Commission Number: EC 5.4.99.58. 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-5601; methylornithine synthase; EC 5.4.99.58; PylB. Cat No: EXWM-5601. | |
| 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. | |
| (R)-citramalate synthase | One of the enzymes involved in a novel pyruvate pathway for isoleucine biosynthesis that is found in some, mainly archaeal, bacteria. The enzyme can be inhibited by isoleucine, the end-product of the pathway, but not by leucine. The enzyme is highly specific for pyruvate as substrate, as the 2-oxo acids 3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate, 2-oxohexanoate and 2-oxoglutarate cannot act as substrate. Group: Enzymes. Synonyms: CimA. Enzyme Commission Number: EC 2.3.1.182. 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-2124; (R)-citramalate synthase; EC 2.3.1.182; CimA. Cat No: EXWM-2124. | |
| ribose 1,5-bisphosphate isomerase | This archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The enzyme is activated by cAMP. Group: Enzymes. Synonyms: R15P isomerase; ribulose 1,5-bisphosphate synthase; RuBP synthase. Enzyme Commission Number: EC 5.3.1.29. 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-5468; ribose 1,5-bisphosphate isomerase; EC 5.3.1.29; R15P isomerase; ribulose 1,5-bisphosphate synthase; RuBP synthase. Cat No: EXWM-5468. | |
| 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 (adenine57-N1/adenine58-N1)-methyltransferase | The enzyme catalyses the formation of N1-methyladenine at two adjacent positions (57 and 58) in the T-loop of certain tRNAs (e.g. tRNAAsp). Methyladenosine at position 57 is an obligatory intermediate for the synthesis of methylinosine, which is commonly found at position 57 of archaeal tRNAs. Group: Enzymes. Synonyms: TrmI; PabTrmI; AqTrmI; MtTrmI. Enzyme Commission Number: EC 2.1.1.219. 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-1821; tRNA (adenine57-N1/adenine58-N1)-methyltransferase; EC 2.1.1.219; TrmI; PabTrmI; AqTrmI; MtTrmI. Cat No: EXWM-1821. | |
| tRNA (cytidine56-2'-O)-methyltransferase | The archaeal enzyme specifically catalyses the S-adenosyl-L-methionine dependent 2'-O-ribose methylation of cytidine at position 56 in tRNA transcripts. Group: Enzymes. Synonyms: aTrm56; tRNA ribose 2'-O-methyltransferase aTrm56; PAB1040 (gene name). Enzyme Commission Number: EC 2.1.1.206. 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-1807; tRNA (cytidine56-2'-O)-methyltransferase; EC 2.1.1.206; aTrm56; tRNA ribose 2'-O-methyltransferase aTrm56; PAB1040 (gene name). Cat No: EXWM-1807. | |
| 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-guanine15 transglycosylase | Archaeal tRNAs contain the modified nucleoside archaeosine at position 15. This archaeal enzyme catalyses the exchange of guanine at position 15 of tRNA with the base preQ0, which is ultimately modified to form the nucleoside archaeosine (cf. EC 2.6.1.97). Group: Enzymes. Synonyms: tRNA transglycosylase (ambiguous); transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine15 transglycosidase; TGT (ambiguous); transfer ribonucleic acid guanine15 transglycosylase. Enzyme Commission Number: EC 2.4.2.48. 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-2677; tRNA-guanine15 transglycosylase; EC 2.4.2.48; tRNA transglycosylase (ambiguous); transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine15 transglycosidase; TGT (ambiguous); transfer ribonucleic acid guanine15 transglycosylase. Cat No: EXWM-2677. | |
| 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 (pseudouridine54-N1)-methyltransferase | While this archaeal enzyme is specific for the 54 position and does not methylate pseudouridine at position 55, the presence of pseudouridine at position 55 is necessary for the efficient methylation of pseudouridine at position 54. Group: Enzymes. Synonyms: TrmY; m1ψ methyltransferase. Enzyme Commission Number: EC 2.1.1.257. 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-1861; tRNA (pseudouridine54-N1)-methyltransferase; EC 2.1.1.257; TrmY; m1ψ methyltransferase. Cat No: EXWM-1861. | |
| 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. | |
Our database is helping our users find suppliers everyday.
