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Galactose mutarotase (aldose 1-epimerase) (gene name GALM) is a human enzyme that reversibly converts α-aldose to the β-anomer. [5] This enzyme catalyzes the first step of the Leloir pathway, which is involved in galactose metabolism. [6] It belongs to family of aldose epimerases.
Intermediates and enzymes in the Leloir pathway of galactose metabolism [5] In the first step, galactose mutarotase facilitates the conversion of β-D-galactose to α-D-galactose since this is the active form in the pathway. Next, α-D-galactose is phosphorylated by galactokinase to galactose 1-phosphate.
The gal operon of E. coli consists of 4 structural genes: galE (epimerase), galT (galactose transferase), galK (galactokinase), and galM (mutarotase) which are transcribed from two overlapping promoters, PG1 (+1) and PG2 (-5), upstream from galE. [3] GalE encodes for an epimerase that
The initial stage is the conversion of β-D-galactose to α-D-galactose by the enzyme, mutarotase (GALM). The Leloir pathway then carries out the conversion of α-D-galactose to UDP-glucose via three principal enzymes: Galactokinase (GALK) phosphorylates α-D-galactose to galactose-1-phosphate, or Gal-1-P; Galactose-1-phosphate ...
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Galactose is therefore preferentially converted into glucose-1-phosphate, which may be shunted into glycolysis or the inositol synthesis pathway. [12] GALE functions as one of four enzymes in the Leloir pathway of galactose conversion of glucose-1-phosphate. First, galactose mutarotase converts β-D-galactose to α-D-galactose. [1]
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