PMID: 6104953Feb 1, 1980Paper

Active-site amino acid residues in gamma-glutamyltransferase and the nature of the gamma-glutamyl-enzyme bond

The Biochemical Journal
J S Elce

Abstract

Active-site residues in rat kidney gamma-glutamyltransferase (EC 2.3.2.2) were investigated by means of chemical modification. 1. In the presence of maleate, the activity was inhibited by phenylmethanesulphonyl fluoride, and the inhibition was not reversed by beta-mercaptoethanol, suggesting that a serine residue is close to the active site, but is shielded except in the presence of maleate. 2. Treatment of the enzyme with N-acetylimidazole modified an amino group, exposed a previously inaccessible cysteine residue and inhibited hydrolysis of the gamma-glutamyl-enzyme intermediate, but not its formation. 3. After reaction of the enzyme successively with N-acetylimidazole and with non-radioactive iodoacetamide/serine/borate, two active-site residues reacted with iodo[(14)C]acetamide. One of these possessed a carboxy group, which formed a [(14)C]glycollamide ester, and the other was cysteine, shown by isolation of S-[(14)C]carboxymethylcysteine after acid hydrolysis. When N-acetylimidazole treatment was omitted, only the carboxy group reacted with iodo[(14)C]acetamide. 4. Isolation of the gamma-[(14)C]glutamyl-enzyme intermediate was made easier by prior treatment of the enzyme with N-acetylimidazole. The gamma-glutamyl-enzyme bo...Continue Reading

Citations

Feb 1, 1997·Infection and Immunity·P L Mäkinen, K K Mäkinen
Apr 14, 1981·Biochimica Et Biophysica Acta·D BagrelG Siest
Aug 21, 1987·Biochimica Et Biophysica Acta·N D CookT J Peters
Jan 1, 1985·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·B P Glynn, D B Johnson
Nov 27, 2007·Biochemical and Biophysical Research Communications·Ping-Lin OngLong-Liu Lin

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