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Literature summary extracted from

  • Krekel, F.; Samland, A.K.; Macheroux, P.; Amrhein, N.; Evans, J.N.S.
    Determination of the pKa value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae (2000), Biochemistry, 39, 12671-12677.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.7 C115S
-
 Enterobacter cloacae
2.5.1.7 C251S site-directed mutagenesis, Cys251 is not involved in the catalysis, unaltered biochemical properties Enterobacter cloacae
2.5.1.7 C354S site-directed mutagenesis, Cys354 is not involved in the catalysis, unaltered biochemical properties Enterobacter cloacae
2.5.1.7 C381S site-directed mutagenesis, Cys381 is not involved in the catalysis, unaltered biochemical properties Enterobacter cloacae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.7 fosfomycin binds covalently to Cys115 Enterobacter cloacae
2.5.1.7 iodoacetamide inhibition by alkylation of the active site Cys155, pH-dependent, no alkylation below pH 7.0, maximum alkylation at pH 9.0 Enterobacter cloacae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.7 additional information
-
 additional information Km values of mutant enzymes for the substrates Enterobacter cloacae
2.5.1.7 0.008
-
 phosphoenolpyruvate wild-type enzyme Enterobacter cloacae
2.5.1.7 0.08
-
 UDP-GlcNAc wild-type enzyme 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
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.7 covalent adduct of enzyme and phosphoenolpyruvate Enterobacter cloacae

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 Cys115 in the active site can act as proton donor, necessary for activity, or as a nucleophile 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

Synonyms

EC Number Synonyms Comment Organism
2.5.1.7 UDP-N-acetylglucosamine enolpyruvyltransferase
-
 Enterobacter cloacae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.7 additional information
-
 additional information kcat values of mutant enzymes for the substrates Enterobacter cloacae
2.5.1.7 3
-
 phosphoenolpyruvate wild-type enzyme Enterobacter cloacae
2.5.1.7 3
-
 UDP-GlcNAc wild-type enzyme Enterobacter cloacae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.7 additional information
-
 determination of pKa value for Cys115: 8.3 Enterobacter cloacae