PROSITE documentation PDOC00471Aldose 1-epimerase putative active site
Aldose 1-epimerase (EC 5.1.3.3) (mutarotase) is the enzyme responsible for the anomeric interconversion of D-glucose and other aldoses between their α- and β-forms.
The sequence of mutarotase from two bacteria, Acinetobacter calcoaceticus and Streptococcus thermophilus is available [1]. It has also been shown that, on the basis of extensive sequence similarities, a mutarotase domain seem to be present in the C-terminal half of the fungal GAL10 protein which encodes, in the N-terminal part, for UDP-glucose 4-epimerase.
The best conserved region in the sequence of mutarotase is centered around a conserved histidine residue which may be involved in the catalytic mechanism.
Last update:May 2004 / Text revised.
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| 1 | Authors | Poolman B. Royer T.J. Mainzer S.E. Schmidt B.F. |
| Title | Carbohydrate utilization in Streptococcus thermophilus: characterization of the genes for aldose 1-epimerase (mutarotase) and UDPglucose 4-epimerase. | |
| Source | J. Bacteriol. 172:4037-4047(1990). | |
| PubMed ID | 1694527 |
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