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Literature summary for 6.1.1.10 extracted from

  • Havrylenko, S.; Legouis, R.; Negrutskii, B.; Mirande, M.
    Methionyl-tRNA synthetase from Caenorhabditis elegans: a specific multidomain organization for convergent functional evolution (2010), Protein Sci., 19, 2475-2484.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information construction of truncated mutants lacking the tRNA-binding domain, deletion of the C-terminal tRBD of MetRS-Ce results in a 10fold increase in the kcat of Met-tRNAMet formation and a 15fold increase in KM for tRNAMe compared to the wild-type enzyme Caenorhabditis elegans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-methionine + tRNAMet Caenorhabditis elegans MetRS specifically binds tRNAMet and catalyzes the synthesis of methionyl-tRNAMet. The C-terminal appended domain causes a slow release of aminoacyl-tRNA and establishes a limiting step in the global aminoacylation reaction AMP + diphosphate + L-methionyl-tRNAMet
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?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + tRNAMet
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Caenorhabditis elegans AMP + diphosphate + L-methionyl-tRNAMet
-
?
ATP + L-methionine + tRNAMet MetRS specifically binds tRNAMet and catalyzes the synthesis of methionyl-tRNAMet. The C-terminal appended domain causes a slow release of aminoacyl-tRNA and establishes a limiting step in the global aminoacylation reaction Caenorhabditis elegans AMP + diphosphate + L-methionyl-tRNAMet
-
?

Subunits

Subunits Comment Organism
More MetRS is a multidomain protein, structural organization: the very C-terminal appended domain is related to the oligonucleotide binding-fold-based tRNA-binding domain recovered at the C-terminus of MetRS from plant, but, in the nematode enzyme, this domain is separated from the core enzyme by an insertion domain Caenorhabditis elegans

Synonyms

Synonyms Comment Organism
methionyl-tRNA synthetase
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Caenorhabditis elegans
MetRS
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Caenorhabditis elegans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Caenorhabditis elegans

Cofactor

Cofactor Comment Organism Structure
ATP
-
Caenorhabditis elegans

General Information

General Information Comment Organism
evolution MetRS from nematode is functionally related to human MetRS despite the fact that their appended tRNA-binding domains have distinct structural folds, and are not orthologues Caenorhabditis elegans