Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Samland, A.K.; Jelesarov, I.; Kuhn, R.; Amrhein, N.; Macheroux, P.
    Thermodynamic characterization of ligand-induced conformational changes in UDP-N-acetylglucosamine enolpyruvyl transferase (2001), Biochemistry, 40, 9950-9956.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.7 Enterobacter cloacae P33038 MurA
-
2.5.1.7 Enterobacter cloacae P33038 recombinant purified enzyme
-
2.5.1.7 Enterobacter cloacae DSM 30054 P33038 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 thermodynamical investigation of substrate binding and binding of inhibitory substrate analogue fosfomycin 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

Subunits

EC Number Subunits Comment Organism
2.5.1.7 additional information structure Enterobacter cloacae