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Reaction of uridine diphosphate galactose 4-epimerase with a suicide inactivator

Biochemistry, 1990
UDPgalactose 4-epimerase from Escherichia coli is rapidly inactivated by the compounds uridine 5'-diphosphate chloroacetol (UDC) and uridine 5'-diphosphate bromoacetol (UDB). Both UDC and UDB inactivate the enzyme in neutral solution concomitant with the appearance of chromophores absorbing maximally at 325 and 328 nm, respectively. The reaction of UDC
G R, Flentke, P A, Frey
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Myelodysplasia and deficiency of uridine diphosphate–galactose 4-epimerase

The Journal of Pediatrics, 1995
A 4-year-old girl known to have peripheral uridine diphosphate-galactose 4-epimerase deficiency was examined for bruising and thrombocytopenia. She had dysplastic peripheral blood and bone marrow changes, with a global platelet function defect. Uridine diphosphate-galactose-4-epimerase participates in a metabolic pathway that provides substrates for ...
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Inhibition of uridine diphosphate glucose dehydrogenase by metabolic intermediates of galactose

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
Abstract UDPG dehydrogenase (EC 1.1.1.22) from calf liver is competitively inhibited by UDPGal in vitro and “uncompetitive” inhibition of the enzyme is shown by UDP. The K i for UDPGal is 1.33 · 10 −4 M, the K m for UDPG is 0.9–1.2 · 10 −5 M at pH 8.3.
G. Salitis, I.T. Oliver
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Roots: Early explorations of the pathways of uridine diphosphate galactose in man and in microorganisms

BioEssays, 1985
AbstractThirty years ago, a number of human inborn errors in carbohydrate metabolism were explored with specific enzymatic tests on blood samples (hemolysates). Hereditary galactosemia was the first example. When the inoperative step in galactose metabolism was specified, the basis for the diet therapy used on the galactosemic infants, namely galactose‐
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Uridine diphosphate galactose 4-epimerase in human and other mammalian hemolysates

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract 1. 1. In contrast to the requirement for exogenous NAD+ in the assay of UDP-galactose 4-epimerase (UDPgalactose epimerase, EC 5.1.3.2), in hemolysates from adults, substantial epimerase activity can be demonstrated in hemolysates from newborn infants without addition of NAD+.
William R. Bergren   +2 more
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Efficient One-Pot Synthesis of Uridine Diphosphate Galactose Employing a Trienzyme System

Journal of Agricultural and Food Chemistry
The limited availability of high-cost nucleotide sugars is a significant constraint on the application of their downstream products (glycosides and prebiotics) in the food or pharmaceutical industry. To better solve the problem, this study presented a one-pot approach for the biosynthesis of UDP-Gal using a thermophilic multienzyme system consisting of
Yajing Li   +5 more
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A simple assay for uridine diphosphate galactose 4-epimerase activity.

Annales de genetique, 1980
A simple fluorescent test for the activity of blood uridine diphosphate galactose 4-epimerase which converts uridine diphosphate galactose to uridine diphosphate glucose is described. The enzyme activity is visually estimated by to reduction of NAD+ (non fluorescent) to NADH (fluorescent) in a coupled reaction with uridine diphosphate glucose ...
G, Vaca   +5 more
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Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli uridine diphosphate galactose 4-epimerase.

The Biochemical journal, 1973
UDP-6-deoxygalactose inhibits the UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli in a competitive manner with respect to the substrate UDP-galactose, giving K(i) 1.3x10(-3)m. As a substrate for the enzyme, it is transformed into UDP-6-deoxyglucose, although the reaction stops before equilibrium is attained.
M, Spencer   +3 more
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