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. 1973 Feb;131(2):421–423. doi: 10.1042/bj1310421

Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli uridine diphosphate galactose 4-epimerase (Short Communication)

M Spencer 1, P Blackburn 1, W Ferdinand 1, G M Blackburn 1
PMCID: PMC1177484  PMID: 4578944

Abstract

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 Ki 1.3×10−3m. As a substrate for the enzyme, it is transformed into UDP-6-deoxyglucose, although the reaction stops before equilibrium is attained. Possible causes of this behaviour are discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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