|
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 |
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