Identification of amino acid residues essential for enzyme activity of sheep liver 5,10-methylenetetrahydrofolate reductase
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Sheep liver 5,10-methylenetetrahydrofolate reductase was subjected to specific chemical modification with phenylglyoxal, diethyl pyrocarbonate and N-bromosuccinimide. The second-order rate constants for inactivation were calculated to be 54 M-1 X min-1, 103 M-1 X min-1 and 154 M-1 X min-1 respectively. This inactivation could be prevented by incubation with substrates or products, suggesting that the residues modified, namely arginine, histidine and tryptophan, are essential for enzyme activity.
1999 ◽
Vol 69
(3)
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pp. 275
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2008 ◽
Vol 69
(3)
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pp. 275-281
2011 ◽
Vol 22
(7)
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pp. 1214-1223
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1997 ◽
Vol 1334
(1)
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pp. 57-64
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