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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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.
| 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 |
| URI: | http://eprints.iisc.ernet.in/id/eprint/22400 |
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