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Literature summary for 6.1.1.10 extracted from

  • Al-Moubarak, E.; Simons, C.
    A homology model for Clostridium difficile methionyl tRNA synthetase: active site analysis and docking interactions (2010), J. Mol. Model., 17, 1679-1693.
    View publication on PubMed
Search for more literature for 6.1.1.10

Cloned(Commentary)

Cloned (Comment) Organism
MetRS DNA and amino acid sequence analysis, phylogenetic tree Clostridioides difficile

Inhibitors

Inhibitors Comment Organism Structure
additional information MetRS drug design and homology modelling, overview Clostridioides difficile
REP3123 a selective and potent competitive, versus methionine not ATP, MetRS inhibitor, that strongly binds at the active site, docking study Clostridioides difficile

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Clostridioides difficile
Zn2+ zinc is an absolute requirement for enzyme activity, binding site residues, overview Clostridioides difficile

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-methionine + tRNAMet Clostridioides difficile
-
 AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
ATP + L-methionine + tRNAMet Clostridioides difficile 630
-
 AMP + diphosphate + L-methionyl-tRNAMet
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q181D9
-
-
Clostridioides difficile 630 Q181D9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + tRNAMet
-
 Clostridioides difficile AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
ATP + L-methionine + tRNAMet active site analysis and docking study, overview. Key residues are His53, Asp51 and Lys56 consistently forming H-bonding interactions with the carboxylic acid moiety of methionine. Ile12 forms a hydrogen bond with this moiety in different dockings and the residues Ile224, Val226 and Ala230 form a hydrophobic pocket Clostridioides difficile AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
ATP + L-methionine + tRNAMet
-
 Clostridioides difficile 630 AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
ATP + L-methionine + tRNAMet active site analysis and docking study, overview. Key residues are His53, Asp51 and Lys56 consistently forming H-bonding interactions with the carboxylic acid moiety of methionine. Ile12 forms a hydrogen bond with this moiety in different dockings and the residues Ile224, Val226 and Ala230 form a hydrophobic pocket Clostridioides difficile 630 AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
additional information Met-tRNA anticodon interactions with the MetRS homology model, overview Clostridioides difficile ?
-
 ?
additional information Met-tRNA anticodon interactions with the MetRS homology model, overview Clostridioides difficile 630 ?
-
 ?

Subunits

Subunits Comment Organism
More secondary structure and three-dimensional structure molecular modeling, model validation, overview Clostridioides difficile

Synonyms

Synonyms Comment Organism
Methionyl tRNA synthetase
-
 Clostridioides difficile
MetRS
-
 Clostridioides difficile

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Clostridioides difficile