IDENTIFICATION OF AMINO-ACID RESIDUES AT THE ACTIVE-SITE OF HUMAN-LIVER SERINE HYDROXYMETHYLTRANSFERASE
- 1 September 1989
- journal article
- research article
- Vol. 19 (3) , 625-632
Abstract
Chemical modification of amino acid residues with phenylglyoxal, diethylpyrocarbonate, and N-bromosuccinimide indicated that at least one residue each of arginine, histidine, and tryptophan were necessary for the activity of human liver serine hydroxymethyltransferase. Protection by substrates suggested that these residues might occur at the active site of the enzyme.This publication has 10 references indexed in Scilit:
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