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Literature summary for 6.3.2.9 extracted from

  • Vaganay, S.; Tanner, M.E.; van Heijenoort, J.; Blanot, D.
    Study of the reaction mechanism of the D-glutamic acid-adding enzyme from Escherichia coli (1996), Microb. Drug Resist., 2, 51-54.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2,4,6-Trinitrobenzenesulfonic acid
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Escherichia coli
Phosphinate an analogue of UDP-N-acetylmuramoyl-dipeptide, the N-acetylmuramoyl moiety being replaced by a hexanoyl chain and the peptide bond between L-Ala and D-Glu by a tetrahedral phosphinate bond Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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JM83(pMLD58), overproducing strain
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Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate a tetrahedral transition state follows the acyl phosphate in the reaction pathway Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramoyl-L-Ala + Glu
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Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
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