Photoaffinity reagents for modification of aminoacyl‐tRNA synthetases

Budker, Vladimir G.; Knorre, D.G.; Kravchenko, Vladimir V.; Lavrik, Olga I.; Nevinsky, G.A.; Teplova, N.M.

doi:10.1016/0014-5793(74)80501-6

Cited by 31 publications

(15 citation statements)

References 16 publications

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“…The fulfdment of the first criterion was already demonstrated [5]. Azido-ATP: was found to be a strong competitive inhibitor of tRNA aminoacylation catalyzed by Phe-RSase, the K] value being only two times greater than K M for ATP.…”

Section: Resultsmentioning

confidence: 85%

“…Aliquots of irradiated and control samples were **In the previous paper [5] a significantly lower lamp intensity was used thus resulting in a longer reaction time.…”

Section: Methodsmentioning

confidence: 99%

“…The covalent attachment of [3H]azido-ATP to the enzyme was determined by measuring radioactivity retained with the protein on the nitrocellulose filters at pH 7.5 [5].…”

Section: Methodsmentioning

confidence: 99%

“…Recently ATP-7-p-azidoanilidate* was found to be competitive inhibitor of ATP for phenylalanyltRNA synthetase (EC 6.1.1.) and binding of the ATP moiety to the enzyme under irradiation of the mixture of the enzyme with azido-ATPx was demonstrated [5]. However these data were insufficient to prove that affinity labelling of the enzyme takes place.…”

Section: Introductionmentioning

confidence: 99%

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Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Ankilova¹,

Knorre²,

Kravchenko³

et al. 1975

FEBS Letters

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Section: Resultsmentioning

confidence: 85%

“…Aliquots of irradiated and control samples were **In the previous paper [5] a significantly lower lamp intensity was used thus resulting in a longer reaction time.…”

Section: Methodsmentioning

confidence: 99%

“…The covalent attachment of [3H]azido-ATP to the enzyme was determined by measuring radioactivity retained with the protein on the nitrocellulose filters at pH 7.5 [5].…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Ankilova¹,

Knorre²,

Kravchenko³

et al. 1975

FEBS Letters

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“…This derivative containing p-N3-C6H4-NHCHCH2-group was demonstrated earlier to inactivate Phe-RSase under UV-irradiation 2 …”

Section: Introductionmentioning

confidence: 85%

Affinity labeling of phenylalanyl-tRNA synthetase from E.coli MRE-600 by E.coli tRNAphe containing photoreactive group

Gorshkova¹,

Knorre²,

Lavrik³

et al. 1976

Nucleic Acids Research

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The photoinduced reaction of phenylalanyl-tRNA synthetase (B.C. 6.1.1.20) from E.coli MRE-600 with tRNAAPhe containing photoreative p-N3-C6H4-NJHCOCH2-group attached to 4-thiouridine sU8 (azido-tRNAAPhe) was investigated. inhibitio of the photoinduced reaction. Therefore, the reaction of [14c -Phe-azido-tRNA with the enzyme is significantly less sensitive to the presence of the ligands than the reaction of chlorambucilyl-tRNA with the reactive group attached to the acceptor end of the tRNA studied in 1. It has been concluded that the kinetics of the affinity labelling does permit to discriminate the influence of the low molecular weight ligands of the enzyme on the different sites of the tRNAenzyme interaction.

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Nitrenium Ions and Related Species in Photoaffinity Labeling

Wilson¹,

Voskresenska²

2013

Nitrenes and Nitrenium Ions

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Photoaffinity reagents for modification of aminoacyl‐tRNA synthetases

Cited by 31 publications

References 16 publications

Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Affinity labeling of phenylalanyl-tRNA synthetase from E.coli MRE-600 by E.coli tRNAphe containing photoreactive group

Nitrenium Ions and Related Species in Photoaffinity Labeling

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