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. 1973 May;133(1):183–187. doi: 10.1042/bj1330183

The reaction of a histidine residue in glutamate dehydrogenase with diethyl pyrocarbonate

Robert B Wallis 1,*, J John Holbrook 1
PMCID: PMC1177682  PMID: 4352838

Abstract

1. One mol of diethyl pyrocarbonate will react with one mol of glutamate dehydrogenase polypeptide chains to form one mol of N1-carbethoxyhistidine. Reaction is prevented by NADH. 2. The 1:1 complex has an increased specific activity (1.4–2.0-fold). 3. The reason for the activation is discussed. The results are not consistent with NADH dissociation from the enzyme–glutamate–NADH complex being rate-limiting in the steady state measured. 4. The effects of modification on the properties of the enzyme were investigated. The effects of GTP and NAD+ on the enzyme activity are unaltered by activation. NADH binding is unaltered and there is no apparent change in the molecular weight. However, the activated enzyme can still be further activated by ADP. Ks for ADP is decreased fivefold.

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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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