[Chemical modification of lysine residues in tyrosyl-tRNA-synthetase from cattle liver using pyridoxal-5'-phosphate].
Chemical modification of lysine residues of eukaryotic tyrosyl-tRNA synthetase was studied. It was shown that only four out of 22 lysine residues per enzyme dimer could be modified with pyridoxal-5'-phosphate. This modification led to the inactivation of tRNATyr aminoacylation by more than 90% but did not practically affect the rate of ATP-[32P]pyrophosphate exchange. Low molecular weight substrates (ATP, ATP-tyrosine) weakly protected the enzyme from inactivation, whereas tRNATyr afforded a much more effective protection. It was supposed that lysine residues of tyrosyl-tRNA synthetase can be involved in the interaction with tRNATyr.
Gnatenko
D V
DV
Korneliuk
A I
AI
Lavrik
O I
OI
D000818:Animals; D002417:Cattle; D006868:Hydrolysis; D007700:Kinetics; D008239:Lysine / Q000378:metabolism*; D008970:Molecular Weight; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D013379:Substrate Specificity; D014448:Tyrosine-tRNA Ligase / Q000378:metabolism*
D011732:Pyridoxal Phosphate; D014448:Tyrosine-tRNA Ligase; D008239:Lysine
Khimicheskaia modifikatsiia ostatkov lizina tirozil-tRNK-sintetazy iz pecheni byka s pomoshch'iu piridoksal'-5'-fosfata]