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- * Aldose 1-epimerase putative active site *
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-
- 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
- alpha- and beta-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.
-
- -Consensus pattern: N-x-T-N-H-x-Y-F-N-L
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: December 1991 / First entry.
-
- [ 1] Poolman B., Royer T.J., Mainzer S.E., Schmidt B.F.
- J. Bacteriol. 172:4037-4047(1990).
-