Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry (Q36893655)

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scientific article published on November 1997

Language	Label	Description	Also known as
English	Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry	scientific article published on November 1997

Statements

scholarly article

1 reference

Europe PubMed Central

16 August 2017

Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry (English)

1 reference

Europe PubMed Central

16 August 2017

matrix-assisted laser desorption/ionization

0 references

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

Gillet S

1

1 reference

Europe PubMed Central

16 August 2017

Hountondji C

2

1 reference

Europe PubMed Central

16 August 2017

Schmitter JM

3

1 reference

Europe PubMed Central

16 August 2017

Blanquet S

4

1 reference

Europe PubMed Central

16 August 2017

language of work or name

1 reference

based on heuristic

inferred from title

publication date

1 November 1997

1 reference

Europe PubMed Central

16 August 2017

Protein Science

1 reference

Europe PubMed Central

16 August 2017

6

1 reference

Europe PubMed Central

16 August 2017

2426-2435

1 reference

Europe PubMed Central

16 August 2017

11

1 reference

Europe PubMed Central

16 August 2017

Metal-binding site in a class I tRNA synthetase localized to a cysteine cluster inserted into nucleotide-binding fold

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

C-terminal peptide appendix in a class I tRNA synthetase needed for acceptor-helix contacts and microhelix aminoacylation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

Peptide Acceptors in the Leucine, Phenylalanine Transfer Reaction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

Fast purification of a functional elongator tRNAmetexpressed from a synthetic genein vivo

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

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Nonribosomal biosynthesis of peptide antibiotics

1 reference

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29 September 2017

Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

1 reference

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Selection of suppressor methionyl-tRNA synthetases: mapping the tRNA anticodon binding site

1 reference

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29 September 2017

Enzymatic aminoacylation of sequence-specific RNA minihelices and hybrid duplexes with methionine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

Interrelation between Transfer RNA and Amino-Acid-Activating Sites of Methionyl Transfer RNA Synthetase from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

29 September 2017

Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA synthetase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Enzymatic modification of proteins. V. Protein acceptor specificity in the arginine-transfer reaction.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Covalent aspartylation of aspartyl-tRNA synthetase from bakers' yeast by its cognate aspartyl adenylate: identification of the labeled residues

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

tRNA recognition site of Escherichia coli methionyl-tRNA synthetase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Sequence similarities among the family of aminoacyl-tRNA synthetases.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Activation of methionine by Escherichia coli methionyl-tRNA synthetase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNA(fMet) formyltransferase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

27 June 2018

Evidence that specificity of microhelix charging by a class I tRNA synthetase occurs in the transition state of catalysis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

4 September 2018

Modification of aminoacyl-tRNA synthetases with pyridoxal-5'-phosphate. Identification of the labeled amino acid residues.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143599

4 September 2018

The mechanism of action of methionyl-tRNA synthetase. 3. Ion requirements and kinetic parameters of the ATP-PPi exchange and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Covalent attachment of aspartic acid to yeast aspartyl-tRNA synthetase induced by the enzyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

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Incorporation of 3H-amino acids into proteins in a partially purified fraction of axoplasm: evidence for transfer RNA-mediated, post-translational protein modification in squid giant axons

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Posttranslational Protein Modification by Amino Acid Addition in Intact and Regenerating Axons of the Rat Sciatic Nerve

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Covalent modification of phenylalanyl-tRNA synthetase with phenylalanine during the amino acid activation reaction catalyzed by the enzyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification of peptide sequences at the tRNA binding site of Escherichia coli methionyl-tRNA synthetase

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/9385645

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/PRO.5560061116

1 reference

Europe PubMed Central

16 August 2017

1 reference

Europe PubMed Central

16 August 2017

1 reference

Europe PubMed Central

16 August 2017

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