(Q67913142)

English

Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalysed by the methionyl-tRNA synthetase from Escherichia coli

scientific article published on 01 February 1991

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scholarly article

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19 September 2019

Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalysed by the methionyl-tRNA synthetase from Escherichia coli (English)

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Europe PubMed Central

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19 September 2019

Escherichia coli

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based on heuristic

inferred from title

transfer RNA aminoacylation

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8 December 2022

structural biology

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10.1016/0022-2836(91)90750-Z

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8 December 2022

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Y. Mechulam

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8 December 2022

Frédéric Dardel

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F. Dardel

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8 December 2022

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D. Le Corre

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8 December 2022

S. Blanquet

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8 December 2022

G. Fayat

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8 December 2022

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8 December 2022

publication date

1 February 1991

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19 September 2019

5 February 1991

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National Center for Biotechnology Information

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1847216

8 December 2022

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https://api.elsevier.com/content/article/PII:002228369190750Z?httpAccept=text/xml

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10.1016/0022-2836(91)90750-Z

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8 December 2022

https://api.elsevier.com/content/article/PII:002228369190750Z?httpAccept=text/plain

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10.1016/0022-2836(91)90750-Z

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8 December 2022

Journal of Molecular Biology

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19 September 2019

217

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19 September 2019

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19 September 2019

465-475

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19 September 2019

The mechanism of reaction of methionyl-tRNA synthetase from Escherichia coli. Interaction of the enzyme with ligands of the amino-acid-activation reaction

1

1 reference

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8 December 2022

The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. 1. Fluorescence Studies on tRNAMet Binding as a Function of Ligands, Ions and pH

2

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The Mechanism of Action of Methionyl-tRNA Synthetase. 2. Interaction of the Enzyme with Specific and Unspecific tRNAs

3

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8 December 2022

The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Mechanism of the amino-acid activation reaction catalyzed by the native and the trypsin-modified enzymes.

4

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8 December 2022

The amino acid activation reaction catalyzed by methionyl-transfer RNA synthetase: Evidence for synergistic coupling between the sites for methionine adenosine and pyrophosphate

5

1 reference

10.1016/0022-2836(91)90750-Z

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8 December 2022

The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. Inhibition by Adenosine and 8-Aminoadenosine of the Amino-Acid Activation Reaction

6

1 reference

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8 December 2022

Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme.

8

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8 December 2022

Couplings between the sites for methionine and adenosine 5'-triphosphate in the amino acid activation reaction catalyzed by trypsin-modified methionyl-transfer RNA synthetase from Escherichia coli

9

1 reference

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8 December 2022

Methionyl-tRNA Synthetase from Escherichia coli. Inactivation and Labeling by Periodate-Treated Initiator tRNA

10

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8 December 2022

Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis

11

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8 December 2022

Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism

12

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8 December 2022

Genetic engineering of methionyl-tRNA synthetase: in vitro regeneration of an active synthetase by proteolytic cleavage of a methionyl-tRNA synthetase--beta-galactosidase chimeric protein

13

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Complete Inactivation and Labeling of Methionyl-tRNA Synthetase by Periodate-Treated Initiator tRNA in the Presence of Sodium Cyanohydridoborate

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8 December 2022

Methionyl-tRNA synthetase from Escherichia coli: primary structure at the binding site for the 3'-end of tRNAfMet

15

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8 December 2022

Sequence similarities among the family of aminoacyl-tRNA synthetases.

16

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8 December 2022

Escherichia coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3'-end of tRNA.

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Affinity labeling of Escherichia coli phenylalanyl-tRNA synthetase at the binding site for tRNAPhe.

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Methionyl-tRNA synthetase from Escherichia coli: active stoichiometry and stopped-flow analysis of methionyl adenylate formation

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An Algorithm for Least-Squares Estimation of Nonlinear Parameters

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Identification of an amino acid region supporting specific methionyl-tRNA synthetase: tRNA recognition.

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Identifiers

10.1016/0022-2836(91)90750-Z

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1847216%20AND%20SRC:MED&resulttype=core&format=json

19 September 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1847216%20AND%20SRC:MED&resulttype=core&format=json

19 September 2019

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