The Enzyme Database

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EC 5.1.3.3     
Accepted name: aldose 1-epimerase
Reaction: α-D-glucose = β-D-glucose
Other name(s): mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase
Systematic name: aldose 1-epimerase
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-76-9
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 (1960) 1219–1224. [PMID: 13799037]
2.  Bentley, R. and Bhate, D.S. Mutarotase from Penicillium notatum. II. The mechanism of the mutarotation reaction. J. Biol. Chem. 235 (1960) 1225–1233. [PMID: 13799038]
3.  Keilin, D. and Hartree, E.F. Biological catalysis of mutarotation of glucose. Biochem. J. 50 (1952) 341–348. [PMID: 14915955]
4.  Levy, G.B. and Cook, E.S. A rotographic study of mutarotase. Biochem. J. 57 (1954) 50–55. [PMID: 13159947]
5.  Beebe, J.A. and Frey, P.A. Galactose mutarotase: purification, characterization, and investigations of two important histidine residues. Biochemistry 37 (1998) 14989–14997. [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 (2004) 23431–23437. [PMID: 15026423]
7.  Thoden, J.B., Kim, J., Raushel, F.M. and Holden, H.M. The catalytic mechanism of galactose mutarotase. Protein Sci. 12 (2003) 1051–1059. [PMID: 12717027]
[EC 5.1.3.3 created 1961]
 
 


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