Inactivation of the F1-ATPase from the thermophilic bacterium PS3 by 5'-p-fluorosulfonylbenzoylinosine at 65 degrees C is accompanied by modification of beta-tyrosine-364.
A major radioactive peptide, T1, was resolved by high-performance liquid chromatography from a tryptic digest prepared from the F1-ATPase from the thermophilic bacterium PS3 which had been inactivated with p-fluorosulfonylbenzoyl[3H]inosine. Two radioactive peptides, T1P1 and T1P2, were isolated from a peptic digest of T1 by high-performance liquid chromatography. The sequences of T1P1 and T1P2 were shown to be E-E-H-X-Q-V-A-R and E-E-H-X-Q, respectively, where X corresponds to derivatized Tyr-364 of the beta subunit.
D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D007288:Inosine / Q000031:analogs & derivatives* / Q000494:pharmacology; D008969:Molecular Sequence Data; D010434:Pepsin A; D010446:Peptide Fragments / Q000302:isolation & purification; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D014357:Trypsin; D014443:Tyrosine
D010446:Peptide Fragments; D014443:Tyrosine; D007288:Inosine; C050367:5'-(4-fluorosulfonylbenzoyl)inosine; D014357:Trypsin; D010434:Pepsin A; D006180:Proton-Translocating ATPases