Description
The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.
Abbr
GALE, Native (Galactose-adapted Yeast)
Source
Galactose-adapted yeast
Form
Lyophilized powder containing approx. 40% buffer salts
Enzyme Commission Number
EC 5.1.3.2
Activity
10-20 units/mg protein (modified Warburg-Christian)
Unit Definition
One unit will convert 1.0 μmole UDP-galactose to Udp-glucose per min at pH 8.8 at 25°C. Contains approx. 0.4% galactokinase, and <0.2% UDPG-pyrophosphorylase, UDPG dehydrogenase and galactose-1-phosphate uridyl transferase.
Synonyms
UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-galactose-4-epimerase; UDP-glucose epimerase; UDP-galactose 4-epimerase; 4-epimerase; UDPG-4-epimerase; uridine diphosphoglucose 4-epimerase; uridine diphosphate glucose 4-epimerase; UDP-D-galactose 4-epimerase; EC 5.1.3.2; UDP-glucose 4-epimerase; GALE
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