Modification of arginine residues in calf intestinal alkaline phosphatase.
Calf intestinal alkaline phosphatase is inactivated by 2,3-butanedione and phenylglyoxal. The reaction with either reagent results in a biphasic loss of enzymatic activity. Inactivation by 2,3-butanedione in borate buffer can be reversed after gel-filtration in Tris buffer but no enzyme reactivation is observed after phenylglyoxal treatment. Phosphate, ATP and NADH protect the enzyme from both compounds while no protection is displayed by L-phenylalanine. The selective chemical modification indicates that two differently reacting types of arginines are present in the active site domains of the dimeric enzyme.
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D001120:Arginine / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D002417:Cattle; D004852:Epoxy Compounds / Q000494:pharmacology; D007422:Intestines / Q000201:enzymology; D007700:Kinetics; D010658:Phenylglyoxal / Q000494:pharmacology; D013329:Structure-Activity Relationship
D004852:Epoxy Compounds; C007366:diepoxybutane; D001120:Arginine; D000469:Alkaline Phosphatase; D010658:Phenylglyoxal