Modification of uridine phosphorylase from Escherichia coli by diethyl pyrocarbonate. Evidence for a histidine residue in the active site of the enzyme.

Uridine phosphorylase from Escherichia coli is inactivated by diethyl pyrocarbonate at pH 7.1 and 10 degrees C with a second-order rate constant of 840 M-1.min-1. The rate of inactivation increases with pH, suggesting participation of an amino acid residue with pK 6.6. Hydroxylamine added to the ina...

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Hlavní autoři: Drabikowska, A K, Woźniak, G
Médium: Artigo
Jazyk:Inglês
Vydáno: 1990
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1131723/
https://ncbi.nlm.nih.gov/pubmed/2205199
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