|PROSITE documentation PDOC00471|
Aldose 1-epimerase (EC 126.96.36.199) (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 . 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.
May 2004 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|ALDOSE_1_EPIMERASE, PS00545; Aldose 1-epimerase putative active site (PATTERN)|
|Matching PDB structures: 1SNZ 1SO0 1YGA 1Z45 [ALL]|
|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).|