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Literature summary for 6.3.2.9 extracted from

  • Bertrand, J.A.; Auger, G.; Fanchon, E.; Martin, L.; Blanot, D.; van Heijenoort, J.; Dideberg, O.
    Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli (1997), EMBO J., 16, 3416-3425.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the enzyme in presence of its substrate UDP-N-acetylmuramoyl-L-Ala, at 1.9 A resolution Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu Escherichia coli key role in peptidoglycan biosynthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P14900
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
?
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu key role in peptidoglycan biosynthesis Escherichia coli ?
-
?