Manohar, R and Rao, NA (1984) Identification of active-site residues of sheep liver serine hydroxymethyltransferase. In: Biochemical Journal, 224 (3). pp. 703-707.
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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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Portland Press.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||20 Aug 2009 11:18|
|Last Modified:||19 Sep 2010 05:41|
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