| aldose 1-epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.1.3.3 | ||||||||
| CAS no. | 9031-76-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an aldose 1-epimerase ( EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction
- alpha-D-glucose beta-D-glucose
Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is aldose 1-epimerase. Other names in common use include mutarotase, and aldose mutarotase. This enzyme participates in glycolysis and gluconeogenesis.
As of late 2007, 23 structures have been solved for this class of enzymes, with PDB accession codes 1L7J, 1L7K, 1LUR, 1MMU, 1MMX, 1MMY, 1MMZ, 1MN0, 1NS0, 1NS2, 1NS4, 1NS7, 1NS8, 1NSM, 1NSR, 1NSS, 1NSU, 1NSV, 1NSX, 1NSZ, 1SNZ, 1SO0, and 1YGA.
- Bentley R; Bhate DS (1960). "Mutarotase from Penicillium notatum. I. Purification, assay, and general properties of the enzyme" (PDF). J. Biol. Chem. 235 (5): 1219–1224. doi: 10.1016/S0021-9258(18)69388-3. PMID 13799037.
- Bentley R; Bhate DS (1960). "Mutarotase from Penicillium notatum. II. The mechanism of the mutarotation reaction" (PDF). J. Biol. Chem. 235 (5): 1225–1233. doi: 10.1016/S0021-9258(18)69389-5. PMID 13799038.
- KEILIN D, HARTREE EF (1952). "Biological catalysis of mutarotation of glucose". Biochem. J. 50 (3): 341–8. doi: 10.1042/bj0500341. PMC 1197658. PMID 14915955.
- LEVY GB, COOK ES (1954). "A rotographic study of mutarotase". Biochem. J. 57 (1): 50–5. doi: 10.1042/bj0570050. PMC 1269703. PMID 13159947.
| aldose 1-epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.1.3.3 | ||||||||
| CAS no. | 9031-76-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an aldose 1-epimerase ( EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction
- alpha-D-glucose beta-D-glucose
Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is aldose 1-epimerase. Other names in common use include mutarotase, and aldose mutarotase. This enzyme participates in glycolysis and gluconeogenesis.
As of late 2007, 23 structures have been solved for this class of enzymes, with PDB accession codes 1L7J, 1L7K, 1LUR, 1MMU, 1MMX, 1MMY, 1MMZ, 1MN0, 1NS0, 1NS2, 1NS4, 1NS7, 1NS8, 1NSM, 1NSR, 1NSS, 1NSU, 1NSV, 1NSX, 1NSZ, 1SNZ, 1SO0, and 1YGA.
- Bentley R; Bhate DS (1960). "Mutarotase from Penicillium notatum. I. Purification, assay, and general properties of the enzyme" (PDF). J. Biol. Chem. 235 (5): 1219–1224. doi: 10.1016/S0021-9258(18)69388-3. PMID 13799037.
- Bentley R; Bhate DS (1960). "Mutarotase from Penicillium notatum. II. The mechanism of the mutarotation reaction" (PDF). J. Biol. Chem. 235 (5): 1225–1233. doi: 10.1016/S0021-9258(18)69389-5. PMID 13799038.
- KEILIN D, HARTREE EF (1952). "Biological catalysis of mutarotation of glucose". Biochem. J. 50 (3): 341–8. doi: 10.1042/bj0500341. PMC 1197658. PMID 14915955.
- LEVY GB, COOK ES (1954). "A rotographic study of mutarotase". Biochem. J. 57 (1): 50–5. doi: 10.1042/bj0570050. PMC 1269703. PMID 13159947.