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| Product | Description | |
|---|---|---|
| D-Psicose | D-Psicose is a biochemical reagent that can be used as a biological material or organic compound for life science related research. Uses: Scientific research. Group: Natural products. CAS No. 551-68-8. Pack Sizes: 500 g. Product ID: HY-N9914. |  |
| D-psicose 3-epimerase | The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose (cf. EC 5.1.3.31, D-tagatose 3-epimerase). The enzyme from the bacterium Clostridium scindens requires Mn2+, whereas the enzymes from the bacteria Clostridium cellulolyticum, Clostridium sp. BNL1100, and Clostridium bolteae require Co2+ as optimum cofactor. The enzyme from Ruminococcus sp. is not dependent on the presence of metal ions, but its activity is enhanced by Mn2+. Group: Enzymes. Synonyms: DPEase (ambiguous). Enzyme Commission Number: EC 5.1.3.30. 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-5417; D-psicose 3-epimerase; EC 5.1.3.30; DPEase (ambiguous). Cat No: EXWM-5417. |  |
| D-Psicose (Standard) | D-Psicose (Standard) is the analytical standard of D-Psicose. This product is intended for research and analytical applications. D-Psicose is a biochemical reagent that can be used as a biological material or organic compound for life science related research. Uses: Scientific research. Group: Natural products. CAS No. 551-68-8. Pack Sizes: 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-N9914R. | |
| D-Allulose (D-Psicose) | A C3 epimer of L-Fructose. Synonyms: D-Allulose; D-Ribo-2-hexulose. Grades: > 95%. CAS No. 551-68-8. Molecular formula: C6H12O6. Mole weight: 180.16. |  |
| D-arabinose isomerase | Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism. The enzyme catalyses the aldose-ketose isomerization of several sugars. Most enzymes also catalyse the reaction of EC 5.3.1.25, L-fucose isomerase. The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose. cf. EC 5.3.1.4, L-arabinose isomerase. Group: Enzymes. Synonyms: D-arabinose(L-fucose) isomerase; L-fucose isomerase; D-arabinose ketol-isomerase; arabinose isomerase (misleading). Enzyme Commission Number: EC 5.3.1.3. CAS No. 9023-81-8. 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-5469; D-arabinose isomerase; EC 5.3.1.3; 9023-81-8; D-arabinose(L-fucose) isomerase; L-fucose isomerase; D-arabinose ketol-isomerase; arabinose isomerase (misleading). Cat No: EXWM-5469. | |
| D-tagatose 3-epimerase | The enzymes isolated from the bacteria Pseudomonas cichorii, Pseudomonas sp. ST-24, Rhodobacter sphaeroides and Mesorhizobium loti catalyse the epimerization of various ketoses at the C-3 position, interconverting D-fructose and D-psicose, D-tagatose and D-sorbose, D-ribulose and D-xylulose, and L-ribulose and L-xylulose. The specificity depends on the species. The enzymes from Pseudomonas cichorii and Rhodobacter sphaeroides require Mn2+. Group: Enzymes. Synonyms: L-ribulose 3-epimerase; ketose 3-epimerase. Enzyme Commission Number: EC 5.1.3.31. 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-5418; D-tagatose 3-epimerase; EC 5.1.3.31; L-ribulose 3-epimerase; ketose 3-epimerase. Cat No: EXWM-5418. | |
| L-fucose isomerase | Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism. The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose. The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose. Group: Enzymes. Enzyme Commission Number: EC 5.3.1.25. CAS No. 60063-83-4. 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-5464; L-fucose isomerase; EC 5.3.1.25; 60063-83-4. Cat No: EXWM-5464. | |
| L-rhamnose isomerase | Contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose. Group: Enzymes. Synonyms: rhamnose isomerase; L-rhamnose ketol-isomerase. Enzyme Commission Number: EC 5.3.1.14. CAS No. 9023-84-1. 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-5455; L-rhamnose isomerase; EC 5.3.1.14; 9023-84-1; rhamnose isomerase; L-rhamnose ketol-isomerase. Cat No: EXWM-5455. | |
| L-Tagatose | L-Tagatose, derived from d-tagatose, is a low-calorie natural sweetener used in studying diseases related to high blood sugar levels, such as diabetes. Synonyms: L-Tagatose; 17598-82-2; L-LYXO-2-hexulose; Tagatose, L-; (3R,4R,5S)-1,3,4,5,6-Pentahydroxyhexan-2-one; L-Tagatose [MI]; keto-L-tagatose; 41IX5VHE3I; 551-68-8; 41847-60-3; UNII-41IX5VHE3I; L - tagatose; D-Psicose, >=95%; SCHEMBL9710274; BJHIKXHVCXFQLS-LFRDXLMFSA-N; CHEBI:134275; DTXSID901318451; MFCD00083478; HY-W145570; CS-0214560; T2535; C21523; D92607; Q27258441. CAS No. 17598-82-2. Molecular formula: C6H12O6. Mole weight: 180.16. | |
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