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Literature summary for 6.1.1.1 extracted from

  • Jarvest, R.L.; Berge, J.M.; Houge-Frydrych, C.S.; Janson, C.; Mensah, L.M.; O'Hanlon, P.J.; Pope, A.; Saldanha, A.; Qiu, X.
    Interaction of tyrosyl aryl dipeptides with S. aureus tyrosyl tRNA synthetase: inhibition and crystal structure of a complex (1999), Bioorg. Med. Chem. Lett., 9, 2859-2862.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme complexed to a tyrosyl aryl dipeptide inhibitor, structure analysis Staphylococcus aureus

Inhibitors

Inhibitors Comment Organism Structure
tyrosyl aryl dipeptides inhibitor interacts with and occupies the key catalytic residues in the tyrosyl binding pocket of the catalytic site Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + tyrosine + tRNATyr Staphylococcus aureus
-
AMP + Tyr-tRNATyr + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + tyrosine + tRNATyr
-
Staphylococcus aureus AMP + Tyr-tRNATyr + diphosphate
-
?

Synonyms

Synonyms Comment Organism
tyrosyl tRNA synthetase
-
Staphylococcus aureus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information
-
Staphylococcus aureus