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| Product | Description | |
|---|---|---|
| ADP-specific glucokinase | Requires Mg2+. The enzyme from Pyrococcus furiosus is highly specific for D-glucose; there is some activity with 2-deoxy-D-glucose, but no activity with D-fructose, D-mannose or D-galactose as the substrate. No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate. Group: Enzymes. Synonyms: ADP-dependent glucokinase. Enzyme Commission Number: EC 2.7.1.147. CAS No. 173585-07-4. Hexokinase (ADP-Dependent). 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-2977; ADP-specific glucokinase; EC 2.7.1.147; 173585-07-4; ADP-dependent glucokinase. Cat No: EXWM-2977. |  |
| α,α-trehalose synthase | Requires Mg2+ for maximal activity. The enzyme-catalysed reaction is reversible. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose. While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-α-D-glucose to the same extent, that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose. Group: Enzymes. Synonyms: trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.245. 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-2474; α,α-trehalose synthase; EC 2.4.1.245; trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase. Cat No: EXWM-2474. | |
| Amylomaltase 57A from Pyrococcus furiosus, Recombinant | Amylomaltase (4-α-glucanotransferase; EC 2.4.1.25) catalyzes glucan transfer from one α-1,4-glucan to another α-1,4-glucan or to glucose. Group: Enzymes. Synonyms: EC 2.4.1.25; Amylomaltase 57A; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Purity: >90% by SDS-PAGE. Amylomaltase. Mole weight: 33.5 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Pyrococcus furiosus. EC 2.4.1.25; Amylomaltase 57A; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Cat No: NATE-1295. | |
| D-aminoacyl-tRNA deacylase | The enzyme from Escherichia coli can cleave D-tyrosyl-tRNATyr, D-aspartyl-tRNAAsp and D-tryptophanyl-tRNATrp. Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc. Group: Enzymes. Synonyms: Dtd2; D-Tyr-tRNA(Tyr) deacylase; D-Tyr-tRNATyr deacylase; D-tyrosyl-tRNATyr aminoacylhydrolase; dtdA (gene name). Enzyme Commission Number: EC 3.1.1.96. 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-3525; D-aminoacyl-tRNA deacylase; EC 3.1.1.96; Dtd2; D-Tyr-tRNA(Tyr) deacylase; D-Tyr-tRNATyr deacylase; D-tyrosyl-tRNATyr aminoacylhydrolase; dtdA (gene name). Cat No: EXWM-3525. | |
| 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. | |
| hydrogen dehydrogenase (NADP+) | The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase, while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the α and Δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)+]. Group: Enzymes. Synonyms: NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous). Enzyme Commission Number: EC 1.12.1.3. CAS No. 9027-5-8. 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-0518; hydrogen dehydrogenase (NADP+); EC 1.12.1.3; 9027-05-8; NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous). Cat No: EXWM-0518. | |
| hydrogen dehydrogenase [NAD(P)+] | A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the α and Δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+). Group: Enzymes. Synonyms: hydrogenase II (ambiguous). Enzyme Commission Number: EC 1.12.1.5. 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-0520; hydrogen dehydrogenase [NAD(P)+]; EC 1.12.1.5; hydrogenase II (ambiguous). Cat No: EXWM-0520. | |
| isocitrate-homoisocitrate dehydrogenase | Requires Mn2+ and K+ or NH4+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+) and EC 1.1.1.87, homoisocitrate dehydrogenase, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrates. The enzyme may play a role in both the lysine and glutamate biosynthesis pathways. Group: Enzymes. Synonyms: homoisocitrate-isocitrate dehydrogenase; PH1722. Enzyme Commission Number: EC 1.1.1.286. 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-0194; isocitrate-homoisocitrate dehydrogenase; EC 1.1.1.286; homoisocitrate-isocitrate dehydrogenase; PH1722. Cat No: EXWM-0194. | |
| mannosyl-3-phosphoglycerate phosphatase | Requires Mg2+. The enzyme from Pyrococcus horikoshii is specific for α-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate. Group: Enzymes. Enzyme Commission Number: EC 3.1.3.70. CAS No. 393512-74-8. 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-3675; mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.70; 393512-74-8. Cat No: EXWM-3675. | |
| Methionine Aminopeptidase from Pyrococcus furiosus, Recombinant | Methionyl aminopeptidase (EC 3.4.11.18, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme. This enzyme catalyses the following chemical reaction:Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. This membrane-bound enzyme is present in both prokaryotes and eukaryotes. X-ray crystallography of the structure of methionine aminopeptidase from pyrococcus furiosus or pfmap was performed at a resolution of 1.75a and showed that the protein consists of a catalytic domain containing two cobalt ions in the active site and a unique insertion domain which is specific to the prokaryotic form of...o the methionyl aminopeptidases from escherichia coli and pyrococcus furiosus. it has also been used in a study to examine the binding of a new class of pseudopeptide analog inhibitors. Group: Enzymes. Synonyms: Methionyl aminopeptidase; EC 3.4.11.18; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Enzyme Commission Number: EC 3.4.11.18. CAS No. 9025-42-7. MAP. Storage: -20°C. Form: Solution containing 0.01% Tween 20, 0.1 mM CoCl2, and 10 mM Tris-HCl, pH 7.5. Source: E. coli. Species: Pyrococcus furiosus. Methionyl aminopeptidase; EC 3.4.11.18; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Cat No: NATE-0442. | |
| 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. | |
| N1-aminopropylagmatine ureohydrolase | The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine. Group: Enzymes. Enzyme Commission Number: EC 3.5.3.24. 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-4526; N1-aminopropylagmatine ureohydrolase; EC 3.5.3.24. Cat No: EXWM-4526. | |
| 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(P)H sulfur oxidoreductase (CoA-dependent) | This FAD-dependent enzyme, characterized from the archaeon Pyrococcus furiosus, is responsible for NAD(P)H-linked sulfur reduction. The activity with NADH is about half of that with NADPH. The reaction is dependent on CoA, although the nature of this dependency is not well understood. Group: Enzymes. Synonyms: NADPH NSR; S0 reductase; coenzyme A-dependent NADPH sulfur oxidoreductase. Enzyme Commission Number: EC 1.8.1.18. 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-1644; NAD(P)H sulfur oxidoreductase (CoA-dependent); EC 1.8.1.18; NADPH NSR; S0 reductase; coenzyme A-dependent NADPH sulfur oxidoreductase. Cat No: EXWM-1644. | |
| Protease S from Pyrococcus furiosus, Recombinant | Protease S is a serine endoprotease with broad specificity that will digest native and denatured proteins. Cleavage occurs mainly on the carboxy side of peptide bonds. The optimal temperature range is 85 to 95°C and the optimal pH range is 6.0 to 8.0. Protease S is inhibited by PMSF. Thermostable serine protease with broad specificity for native and denatured proteins. Applications: Protease s is from pyrococcus furiosus and is a recombinant protease that is expressed in bacillus sp. it is used for fragmentation of proteins and peptides required for primary structure analysis. Group: Enzymes. Synonyms: Protease S; peptidase S; proteinase S. Protease. Storage: 2-8°C. Form: Solution in 25 mM Tris-HCl, pH 7.6, containing 40% ethanol. Source: Bacillus sp. Species: Pyrococcus furiosus. Protease S; peptidase S; proteinase S. Cat No: NATE-0630. | |
| Pyroglutamate Aminopeptidase from Pyrococcus furiosus, Recombinant | Pyroglutamate aminopetidase is an enzyme that digests proteins. This enzyme is specific for N-terminal pyroglutamic acids. It cleaves the N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation. The optimal temperature range is 95 to 100°C and the optimal pH range is 6.0 to 9.0. Recombinant, expressed in e. coli, ~90% (sds-page). Applications: Thermostable aminopeptidase that liberates n-terminal pyroglutamic acid from proteins and peptides prior to edman degradation. pyroglutamate aminopeptidase, from pyrococcus furiosus is a recombinant, thermostable aminopeptidase that is expressed in escherichia coli. it is used to cleave pyrogl...5-21-2. Enzyme Commission Number: EC 3.4.19.3. CAS No. 9075-21-2. Pyrase. Mole weight: mol wt 24.072 kDa by amino acid sequence mol wt 28 kDa by SDS-PAGE. Activity: > 0.11 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium phosphate. Source: E. coli. Species: Pyrococcus furiosus. pyroglutamyl-peptidase I; Pyroglutamate aminopeptidase; EC 3.4.19.3; 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl p | |
| RNA 3'-terminal-phosphate cyclase (GTP) | The enzyme from the archaeon Pyrococcus furiosus is activated by Mg2+. cf. EC 6.5.1.4, RNA-3'-phosphate cyclase (ATP). Group: Enzymes. Synonyms: Pf-Rtc; RNA-3'-phosphate cyclase (GTP). Enzyme Commission Number: EC 6.5.1.5. 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-5824; RNA 3'-terminal-phosphate cyclase (GTP); EC 6.5.1.5; Pf-Rtc; RNA-3'-phosphate cyclase (GTP). Cat No: EXWM-5824. | |
| rubredoxin-NAD(P)+ reductase | The enzyme from Pyrococcus furiosus requires FAD. It reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. Ferredoxin is not utilized. Group: Enzymes. Synonyms: rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase; rubredoxin-nicotinamide adenine; dinucleotide phosphate reductase; NAD(P)+-rubredoxin oxidoreductase; NAD(P)H-rubredoxin oxidoreductase. Enzyme Commission Number: EC 1.18.1.4. CAS No. 80237-97-4. 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-1109; rubredoxin-NAD(P)+ reductase; EC 1.18.1.4; 80237-97-4; rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase; rubredoxin-nicotinamide adenine; dinucleotide phosphate reductase; NAD(P)+-rubredoxin oxidoreductase; NAD(P)H-rubredoxin oxidoreductase. Cat No: EXWM-1109. | |
| sulfhydrogenase | An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the β and γ subunits function as sulfur reductase and the α and Δ subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate. Group: Enzymes. Synonyms: sulfur reductase. Enzyme Commission Number: EC 1.12.98.4. 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-0527; sulfhydrogenase; EC 1.12.98.4; sulfur reductase. Cat No: EXWM-0527. | |
| tungstate-importing ATPase | An ABC-type (ATP-binding cassette-type) ATPase. The enzymes from the archaeon Pyrococcus furiosus, the Gram-positive bacterium Eubacterium acidaminophilum and the Gram-negative bacterium Campylobacter jejuni transport tungsten into the cell for incorporation into tungsten-dependent enzymes. Group: Enzymes. Synonyms: tungstate transporter; WtpABC; TupABC; tungstate-specific ABC transporter. Enzyme Commission Number: EC 3.6.3.55. 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-4694; tungstate-importing ATPase; EC 3.6.3.55; tungstate transporter; WtpABC; TupABC; tungstate-specific ABC transporter. Cat No: EXWM-4694. | |
| 2-(3-amino-3-carboxypropyl)histidine synthase | A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis. Group: Enzymes. Synonyms: Dph2. Enzyme Commission Number: EC 2.5.1.108. 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-2724; 2-(3-amino-3-carboxypropyl)histidine synthase; EC 2.5.1.108; Dph2. Cat No: EXWM-2724. | |
| 3-hexulose-6-phosphate synthase | Requires Mg2+ or Mn2+ for maximal activity. The enzyme is specific for D-ribulose 5-phosphate as substrate as ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate. In addition to formaldehyde, the enzyme can also use glycolaldehyde and methylglyoxal. This enzyme, along with EC 5.3.1.27, 6-phospho-3-hexuloisomerase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of this enzyme and EC 5.3.1.27, 6-phospho-3-hexuloisomerase. This enzyme is a member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily. Group: Enzymes. Synonyms: D-arabino-3-hexulose 6-phosphate formaldehyde-lyase; 3-hexulosephosphate synthase; 3-hexulose phosphate synthase; HPS. Enzyme Commission Number: EC 4.1.2.43. 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-4879; 3-hexulose-6-phosphate synthase; EC 4.1.2.43; D-arabino-3-hexulose 6-phosphate formaldehyde-lyase; 3-hexulosephosphate synthase; 3-hexulose phosphate synthase; HPS. Cat No: EXWM-4879. | |
| 6-phospho-3-hexuloisomerase | This enzyme, along with EC 4.1.2.43, 3-hexulose-6-phosphate synthase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of EC 4.1.2.43 (3-hexulose-6-phosphate synthase) and this enzyme. Group: Enzymes. Synonyms: 3-hexulose-6-phosphate isomerase; phospho-3-hexuloisomerase; PHI; 6-phospho-3-hexulose isomerase; YckF. Enzyme Commission Number: EC 5.3.1.27. 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-5466; 6-phospho-3-hexuloisomerase; EC 5.3.1.27; 3-hexulose-6-phosphate isomerase; phospho-3-hexuloisomerase; PHI; 6-phospho-3-hexulose isomerase; YckF. Cat No: EXWM-5466. | |
| β-Glucosidase 1A from Pyrococcus furiosus, Recombinant | Beta-glucosidase is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Group: Enzymes. Synonyms: EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; am. Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-22-3. Purity: >90% by SDS-PAGE. β-Glucosidase. Mole weight: 56.7 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Pyrococcus furiosus. EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-glucosidase; β-Glucosidase 1A. Cat No: NATE-1436. | |
| β-Mannosidase 1A from Pyrococcus furiosus, Recombinant | Beta-mannosidase is an enzyme with system name beta-D-mannoside mannohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement. Group: Enzymes. Synonyms: β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Enzyme Commission Number: EC 3.2.1.25. CAS No. 37288-54-3. Purity: >90% by SDS-PAGE. β-Mannosidase. Mole weight: 61.1 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Pyrococcus furiosus. β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8; β-Mannosidase 1A. Cat No: NATE-1470. | |
| GDP-Mannose pyrophosphorylase from Pyrococcus furiosus, Recombinant | In enzymology, a mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) is an enzyme that catalyzes the chemical reaction: GTP + alpha-D-mannose 1-phosphate ? diphosphate + GDP-mannose. Thus, the two substrates of this enzyme are GTP and alpha-D-mannose 1-phosphate, whereas its two products are diphosphate and GDP-mannose. Group: Enzymes. Synonyms: GTP-mannose-1-phosphate guanylyltransferase; PIM-GMP; GDP-mannose pyrophosphorylase; guanosine 5'-diphospho-D-mannose pyrophosphorylase; guanosine diphosphomannose pyrophosphorylase; guanosine triphosphate-mannose 1-phosphate guanylyltransferase; mannose 1-phosphate guanylyltransferase (guanosine triphosphate); mannose-1-phosphate guanylyltransferase; EC 2.7.7.13. Enzyme Commission Number: EC 2.7.7.13. CAS No. 37278-24-3. Purity: min 95% by SDS-PAGE. GDP-Mannose pyrophosphorylase. Source: E. coli. Species: Pyrococcus furiosus. GTP-mannose-1-phosphate guanylyltransferase; PIM-GMP; GDP-mannose pyrophosphorylase; guanosine 5'-diphospho-D-mannose pyrophosphorylase; guanosine diphosphomannose pyrophosphorylase; guanosine triphosphate-mannose 1-phosphate guanylyltransferase; mannose 1-phosphate guanylyltransferase (guanosine triphosphate); mannose-1-phosphate guanylyltransferase; EC 2.7.7.13. Cat No: NATE-1504. | |
| glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) | Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus. It is specific for glyceraldehyde-3-phosphate. Group: Enzymes. Synonyms: GAPOR; glyceraldehyde-3-phosphate Fd oxidoreductase; glyceraldehyde-3-phosphate ferredoxin reductase. Enzyme Commission Number: EC 1.2.7.6. CAS No. 162995-20-2. 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-1229; glyceraldehyde-3-phosphate dehydrogenase (ferredoxin); EC 1.2.7.6; 162995-20-2; GAPOR; glyceraldehyde-3-phosphate Fd oxidoreductase; glyceraldehyde-3-phosphate ferredoxin reductase. Cat No: EXWM-1229. | |
| Laminarinase 16A from Pyrococcus furiosus, Recombinant | Glucan endo-1,3-beta-D-glucosidase is an enzyme with system name 3-beta-D-glucan glucanohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. This enzyme is marginally active on mixed-link (1->3,1->4)-beta-D-glucans. Group: Enzymes. Synonyms: endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1?3)-β-g. Enzyme Commission Number: EC 3.2.1.39. CAS No. 9025-37-0. Purity: >90% by SDS-PAGE. Glucanase. Mole weight: 30.8 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Pyrococcus furiosus. endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1?3)-β-glucan 3-glucanohydrolase; endo-1,3-β-D-glucanase; endo-1,3-β-glucosidase; 1,3-β-D-glucan glucanohydrolase; EC 3.2.1.39; 9044-93-3; Laminarinase 16A. Cat No: NATE-1418. | |
| mannosyl-3-phosphoglycerate synthase | Requires Mg2+. The enzyme is absolutely specific for GDPmannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase), producing mannosylglycerate. Group: Enzymes. Synonyms: MPG synthase; GDP-mannose:3-phosphoglycerate 3-α-D-mannosyltransferase. Enzyme Commission Number: EC 2.4.1.217. CAS No. 393512-63-5. 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-2445; mannosyl-3-phosphoglycerate synthase; EC 2.4.1.217; 393512-63-5; MPG synthase; GDP-mannose:3-phosphoglycerate 3-α-D-mannosyltransferase. Cat No: EXWM-2445. | |
| NAD+-diphthamide ADP-ribosyltransferase | Diphtheria toxin and some other bacterial toxins catalyse this reaction, which inactivates translation elongation factor 2 (EF2). The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. cf. EC 2.4.2.31 NAD(P)+-protein-arginine ADP-ribosyltransferase. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Group: Enzymes. Synonyms: ADP-ribosyltransferase; mono(ADPribosyl)transferase; NAD-diphthamide ADP-ribosyltransferase; NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase. Enzyme Commission Number: EC 2.4.2.36. CAS No. 52933-21-8. 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-2664; NAD+-diphthamide ADP-ribosyltransferase; EC 2.4.2.36; 52933-21-8; ADP-ribosyltransferase; mono(ADPribosyl)transferase; NAD-diphthamide ADP-ribosyltransferase; NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase. Cat No: EXWM-2664. | |
| Native Hexokinase (ADP-Dependent) from Pyrococcus furiosus | In enzymology, a ADP-Dependent Hexokinase (EC 2.7.1.147) is an enzyme that catalyzes the chemical reaction: D-Glucose + ADP ? D-Glucose-6-phosphate + AMP. Applications: Useful for the enzymatic determination of adp. Group: Enzymes. Synonyms: ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Enzyme Commission Number: EC 2.7.1.147. CAS No. 173585-07-4. Hexokinase (ADP-Dependent). Mole weight: 100 kDa (gel filtration) 51 kDa (SDS-PAGE). Activity: More than 30 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Source: Pyrococcus furiosus. ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Cat No: NATE-1135. | |
| NiFe-type cytoplasmic hydrogenase from Pyrococcus furiosus, recombinant | The [NiFe] hydrogenases contain a minimum of two subunits known as the small (S) and large (L) subunits. The small subunit contains three iron-sulfur clusters while the large subunit contains the active site, a nickel-iron center which is connected to the solvent by a molecular tunnel. To date, periplasmic, cytoplasmic, and membrane-bound hydrogenases have been found. [NiFe] hydrogenases are known to be deactivated by molecular oxygen (O2). The [NiFe] hydrogenase of Pyrococcus furiosus is heterotetrameric wherein the additional two subunits allow the enzyme to use NAD(P)(H) as an electron carrier. Group: Enzymes. Synonyms: Cytoplasmic [NiFe]-Hydrogenase; OE-SHI; Cytoplasmic Hydrogenase; NiFe-type cytoplas. Purity: > 90% by SDS-PAGE. Cytoplasmic hydrogenase. Mole weight: Predicted: 155 kDa, Size Exclusion: 149 kDa +/- 5 kDa. Activity: >100 U/mL. Storage: This item is oxygen sensitive. Stable when stored sealed in strictly anaerobic environment (<10 ppm O2) at room temperature for up to 6 months. For long-term storage, protein can be flash frozen in nitrogen and stored at -80°C. Form: Liquid. Source: Pyrococcus furiosus. Cytoplasmic [NiFe]-Hydrogenase; OE-SHI; Cytoplasmic Hydrogenase; NiFe-type cytoplasmic hydrogenase; SHI; [NiFe] hydrogenase; NADP-specific NiFe-type cytoplasmic hydrogenase. Cat No: NATE-1691. | |
| sulfide dehydrogenase | A iron-sulfur flavoprotein. In the archaeon Pyrococcus furiosus the enzyme is involved in the oxidation of NADPH which is produced in peptide degradation. The enzyme also catalyses the reduction of sulfur with lower activity. Group: Enzymes. Synonyms: SuDH. Enzyme Commission Number: EC 1.8.1.19. 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-1645; sulfide dehydrogenase; EC 1.8.1.19; SuDH. Cat No: EXWM-1645. | |
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