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PROSITE documentation PDOC00471

Aldose 1-epimerase putative active site





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

ALDOSE_1_EPIMERASE, PS00545; Aldose 1-epimerase putative active site  (PATTERN)


Reference

1AuthorsPoolman B. Royer T.J. Mainzer S.E. Schmidt B.F.
TitleCarbohydrate utilization in Streptococcus thermophilus: characterization of the genes for aldose 1-epimerase (mutarotase) and UDPglucose 4-epimerase.
SourceJ. Bacteriol. 172:4037-4047(1990).
PubMed ID1694527



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