type	Journal Article
authors	Manohar, R.; Appaji Rao, N.
title	Identification of active-site residues of sheep liver serine hydroxymethyltransferase
journal	Biochem J
Activity	2.1.2.1
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