Methionyl-tRNA synthetase needs an intact and mobile 332KMSKS336 motif in catalysis of methionyl adenylate formation.

doi:10.1006/jmbi.1994.1601

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Article

Methionyl-tRNA synthetase needs an intact and mobile 332KMSKS336 motif in catalysis of methionyl adenylate formation.

Journal of molecular biology - 30 Sept 1994

Schmitt E, Meinnel T, Blanquet S, Mechulam Y

Abstract excerpt

The family of aminoacyl-tRNA synthetases may be split into two classes according to the occurrence of specific combinations of peptide motifs. This study deals with the functional role of the KMSKS motif, which, in association with the HIGH motif, defines class 1 aminoacyl-tRNA synthetases. Each residue in the 332KMSKS336 sequence of Escherichia coli methionyl-tRNA synthetase, as well as R337 and the two...

Topics

Adenosine
Adenosine Monophosphate
Adenosine Triphosphate
Amino Acid Sequence
Animals
Catalysis
Conserved Sequence
Diphosphates
Humans
Hydrolysis
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Magnesium

Methionine

Methionine-tRNA Ligase

Molecular Sequence Data

Mutation

Sequence Alignment

Source

Open in PubMed

Identifiers

PMID: 7932711
DOI: 10.1006/jmbi.1994.1601

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7932711-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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