The Interaction of Phenylalanyl Transfer Ribonucleic Acid Synthetase and Phenylalanine Transfer Ribonucleic Acid
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چکیده
منابع مشابه
Interactions of Phenylalanyl Transfer Ribonucleic Acid Synthetase of Neurospora crassa with Valyl Transfer Ribonucleic Acid of Escherichia co&*
Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...
متن کاملInteractions of phenylalanyl transfer ribonucleic acid synthetase of Neurospora crassa with valyl transfer ribonucleic acid of Escherichia coli.
Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...
متن کاملInteractions of Phenylalanyl Transfer Ribonucleic Acid Synthetase of Neurospora crassa with Valyl Transfer Ribonucleic Acid of Escherichia co&*
Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...
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The arginine-activating enzyme of Escherichk coli requires transfer ribonucleic acid (tRNA) for catalysis of the ATP-pyrophosphate exchange reaction. Only the specific arginiie-accepting tRNA is effective5 and the terminal adenylic acid residue is essential for the reaction. A previously described isotope-trapping experiment led to the suggestion that an arginyl-tRNA ester was not formed during...
متن کاملTransfer Ribonucleic Acid Synthetase in Escherichia colil
The valyl-transfer ribonucleic acid (tRNA) synthetase of Escherichia coli strain NP2907, previously described as having an elevated Km for adenosine triphosphate and reduced stability in vitro compared to the wild type, was found to be conditionally thermolabile in vivo. The rate of inactivation of this enzyme at a particular temperature appears to be coordinated with the rate of growth; at 40 ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)76968-3