Efrapeptin prevents modification by phenylglyoxal of an essential arginyl residue in mitochondrial adenosine triphosphatase.
Studies of phenylglyoxal incorporation by beef-heart mitochondrial ATPase reveal one fast-reacting arginyl residue/enzyme molecule. Modification of this group proceeds at a rate which parallels the loss of enzymatic activity. Efrapeptin protects the arginyl residue from reaction with phenylglyoxal. The data suggest that efrapeptin binds at the catalytic site and blocks accessibility of an essential arginine at the adenine nucleotide binding site. The detection of a single, fast-reacting, essential arginine on an enzyme with multiple copies of the catalytic subunit, provides further evidence in support of the alternating site mechanism for ATP synthesis proposed by Kayalar et al. (Kayalar, C., Rosing, J., and Boyer, P.D. (1977) J.Biol. Chem. 252, 2486--2491).
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000447:Aldehydes / Q000494:pharmacology*; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001120:Arginine; D002417:Cattle; D006037:Glyoxal / Q000031:analogs & derivatives / Q000494:pharmacology*; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology*; D010455:Peptides / Q000494:pharmacology; D011485:Protein Binding
D000447:Aldehydes; D000900:Anti-Bacterial Agents; D010455:Peptides; D006037:Glyoxal; C012953:efrapeptin; D001120:Arginine; D000251:Adenosine Triphosphatases