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Literature summary for 5.1.1.3 extracted from

  • Doublet, P.; van Heijenoort, J.; Mengin-Lecreulx, D.
    Regulation of the glutamate racemase of Escherichia coli investigated by site-directed mutagenesis (1996), Microb. Drug Resist., 2, 43-49.
    View publication on PubMed
Search for more literature for 5.1.1.3

Activating Compound

Activating Compound Comment Organism Structure
UDP-N-acetylmuramyl-L-Ala absolutely required Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis experiments are described demonstrating the participation of Cys96 and Cys208 in the two-base reaction mechanism of the enzyme. The construction of N-terminal-truncated or C-terminal-truncated enzymes shows that the characteristic N-terminal amino acid extension of 20 residues is not involved in its activation by the nucleotide precursor Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Glu Escherichia coli the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glu
-
 Escherichia coli L-Glu
-
 ?
L-Glu the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase Escherichia coli ?
-
 ?