Beta-phosphoglucomutase is an enzyme that transfers a phosphoryl group on a glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse. Specifically, it converts Beta-D-glucose-1-phosphate to Beta-D-glucose-6-phosphate. This enzyme participates in both the breakdown and synthesis of glucose. Maltose metabolism in Lactococcus lactis involves the conversion of beta-glucose 1-phosphate to glucose 6-phosphate, a reaction which is reversibly catalysed by a maltose-inducible and glucose-repressible beta-phosphoglucomutase (beta-PGM). Alpha-PGM is expressed constitutively. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. The enzyme from Lactococcus lactis has been extensively characterised including a remarkable crystal structure which traps the pentacoordinate transition state.
Function:
Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C1 anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.
Subcellular Location:
Cytoplasmic
Post-translational modifications:
Autophosphorylated.
Similarity:
Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.
SWISS:
P71447
Gene ID:
N/A
Database links:
Entrez Gene: 1114041 Lactococcus lacti
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