Essential arginine residues in isoprenylcysteine protein carboxyl methyltransferase

• Published in: Biochemistry and cell biology Vol. 75; no. 1; p. 63
• Main Authors: Boivin, D, Lin, W, Béliveau, R
• Format: Journal Article
• Language: English
• Published: Canada 1997
• Subjects: Adenosine - analogs & derivatives; Adenosine - pharmacology; Animals; Arginine - metabolism; Cell Membrane - enzymology; Enzyme Inhibitors - pharmacology; Hydrogen-Ion Concentration; Kidney - enzymology; Male; Methylation - drug effects; Phenylglyoxal - pharmacology; Protein Methyltransferases - antagonists & inhibitors; Protein Methyltransferases - metabolism; Rats; Rats, Sprague-Dawley; S-Adenosylhomocysteine - pharmacology; S-Adenosylmethionine - pharmacology; Structure-Activity Relationship

We used specific amino acid modifying reagents to characterize the isoprenylcysteine carboxyl methyltransferase in kidney membranes. The enzyme was inactivated by reagents specific for arginine, histidine, cysteine, and tryptophan residues. Protection by the product and inhibitor S-adenosyl-L-homocy...