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Literature summary extracted from

  • Samland, A.K.; Etezady-Esfarjani, T.; Amrhein, N.; Macheroux, P.
    Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae (2001), Biochemistry, 40, 1550-1559.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.7 expression of wild-type and mutants in Escherichia coli Enterobacter cloacae

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.7 D305A site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115 Enterobacter cloacae
2.5.1.7 D305C site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity Enterobacter cloacae
2.5.1.7 D305E site-directed mutagenesis, weaker binding of UDP-GlcNAc, 0.1% activity compared to the wild-type Enterobacter cloacae
2.5.1.7 D305H site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115 Enterobacter cloacae
2.5.1.7 N23A site-directed mutagenesis, reduced activity, 20fold higher apparent dissociation constant for fosfomycin compared to wild-type Enterobacter cloacae
2.5.1.7 N23S site-directed mutagenesis, reduced activity, 200fold higher apparent dissociation constant for fosfomycin compared to wild-type Enterobacter cloacae

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.7 Enterobacter cloacae
-
 MurA
-
2.5.1.7 Enterobacter cloacae
-
 recombinant purified enzyme
-
2.5.1.7 Enterobacter cloacae DSM 30054
-
 MurA
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine mechanism Enterobacter cloacae
a
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine D305 has a dual role as a general base and an essential binding partner to UDP-GlcNAc Enterobacter cloacae
a
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine N23 is responsible for stabilization of transition states Enterobacter cloacae
a
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine Asn23 and Asp305 are essential in the active site Enterobacter cloacae
a
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine enyme exhibits an open conformation when substrate-free, and a closed, tightly-packed conformation upon substrate binding Enterobacter cloacae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
-
 Enterobacter cloacae phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
 r
2.5.1.7 phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
-
 Enterobacter cloacae DSM 30054 phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
 r