Identification of amino acid residues at the active site of human liver serine hydroxymethyltransferase.
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.
Vijayalakshmi
D
D
Department of Biochemistry, Indian Institute of Science, Bangalore.
Rao
N A
NA
D000596:Amino Acids / Q000032:analysis*; D001120:Arginine / Q000032:analysis; D001665:Binding Sites; D001974:Bromosuccinimide / Q000494:pharmacology; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D012696:Glycine Hydroxymethyltransferase / Q000302:isolation & purification; D006639:Histidine / Q000032:analysis; D006801:Humans; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D010658:Phenylglyoxal / Q000494:pharmacology; D014166:Transferases; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D006898:Hydroxylamines; D019811:Hydroxylamine; D006639:Histidine; D014364:Tryptophan; D001120:Arginine; D014166:Transferases; D012696:Glycine Hydroxymethyltransferase; D001974:Bromosuccinimide; D004047:Diethyl Pyrocarbonate; D010658:Phenylglyoxal