EC 5.1.3.3 - Aldose 1-epimerase

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IntEnz Enzyme Nomenclature
EC 5.1.3.3

Names

Accepted name:
aldose 1-epimerase
Other names:
aldose mutarotase
mutarotase
Systematic name:
aldose 1-epimerase

Reaction

Comments:

Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. This enzyme catalyses the first step in galactose metabolism by converting β-D-galactose into α-D-galactose, which is the substrate for EC 2.7.1.6, galactokinase [5,6].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00471
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004034
CAS Registry Number: 9031-76-9
UniProtKB/Swiss-Prot: (19) [show] [UniProt]

References

  1. Bentley, R. and Bhate, D.S.
    Mutarotase from Penicillium notatum. I. Purification, assay, and general properties of the enzyme.
    J. Biol. Chem. 235: 1219-1224 (1960). [PMID: 13799037]
  2. Bentley, R. and Bhate, D.S.
    Mutarotase from Penicillium notatum. II. The mechanism of the mutarotation reaction.
    J. Biol. Chem. 235: 1225-1233 (1960). [PMID: 13799038]
  3. Keilin, D. and Hartree, E.F.
    Biological catalysis of mutarotation of glucose.
    Biochem. J. 50: 341-348 (1952). [PMID: 14915955]
  4. Levy, G.B. and Cook, E.S.
    A rotographic study of mutarotase.
    Biochem. J. 57: 50-55 (1954). [PMID: 13159947]
  5. Beebe, J.A. and Frey, P.A.
    Galactose mutarotase: purification, characterization, and investigations of two important histidine residues.
    Biochemistry 37: 14989-14997 (1998). [PMID: 9778377]
  6. Thoden, J.B., Timson, D.J., Reece, R.J. and Holden, H.M.
    Molecular structure of human galactose mutarotase.
    J. Biol. Chem. 279: 23431-23437 (2004). [PMID: 15026423]
  7. Thoden, J.B., Kim, J., Raushel, F.M. and Holden, H.M.
    The catalytic mechanism of galactose mutarotase.
    Protein Sci. 12: 1051-1059 (2003). [PMID: 12717027]

[EC 5.1.3.3 created 1961]