Inactivation of histidine ammonia-lyase from Streptomyces griseus by dicarbonyl reagents.
Histidine ammonia-lyase from Streptomyces griseus was inactivated by methylglyoxal and phenylglyoxal, dicarbonyl reagents known to react specifically with arginyl residues in proteins. The inactivation showed pseudo-first-order kinetics and could be prevented by protection with histidinol phosphate, a competitive inhibitor of histidine ammonia-lyase. Analysis of the amino acid composition of histidine ammonia-lyase after treatment with phenylglyoxal, together with the kinetics of inactivation, suggested that inactivation was a consequence of specific reaction with one or more essential arginyl residues at or near the active site of the enzyme.
Department of Microbiology, Ohio State University, Columbus 43210.
P J
PJ
White
K E
KE
Kendrick
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001120:Arginine / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D006638:Histidine Ammonia-Lyase / Q000037:antagonists & inhibitors* / Q000187:drug effects / Q000378:metabolism*; D006641:Histidinol / Q000031:analogs & derivatives / Q000494:pharmacology; D008969:Molecular Sequence Data; D010658:Phenylglyoxal / Q000494:pharmacology; D011765:Pyruvaldehyde / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D013305:Streptomyces griseus / Q000201:enzymology*
D000596:Amino Acids; D006641:Histidinol; D011765:Pyruvaldehyde; D001120:Arginine; D006638:Histidine Ammonia-Lyase; D010658:Phenylglyoxal