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. 1984 Dec 15;224(3):703–707. doi: 10.1042/bj2240703

Identification of active-site residues of sheep liver serine hydroxymethyltransferase.

R Manohar, N Appaji Rao
PMCID: PMC1144504  PMID: 6525172

Abstract

Chemical modification of amino acid residues with phenylglyoxal, N-ethylmaleimide and diethyl pyrocarbonate indicated that at least one residue each of arginine, cysteine and histidine were essential for the activity of sheep liver serine hydroxymethyltransferase. The second-order rate constants for inactivation were calculated to be 0.016 mM-1 X min-1 for phenylglyoxal, 0.52 mM-1 X min-1 for N-ethylmaleimide and 0.06 mM-1 X min-1 for diethyl pyrocarbonate. Different rates of modification of these residues in the presence and in the absence of substrates and the cofactor pyridoxal 5'-phosphate as well as the spectra of the modified protein suggested that these residues might occur at the active site of the enzyme.

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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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