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B6db references: 85121794

type Journal Article
authors Manohar, R.; Appaji Rao, N.
title Identification of active-site residues of sheep liver serine hydroxymethyltransferase
journal Biochem J
ui 85121794
year (1984)
volume 224
number 3
pages 703-7.
keywords Animal
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.
last changed 2002/11/04 17:41

B6db references