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Literature summary for 2.5.1.7 extracted from

  • Zemell, R.I.; Anwar, R.A.
    Mechanism of pyruvate-uridine diphospho-N-acetylglucosamine transferase. Evidence for an enzyme-enolpyruvate intermediate (1975), J. Biol. Chem., 250, 4959-4964.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thiol groups required for activity Enterobacter cloacae

Organism

Organism UniProt Comment Textmining
Enterobacter cloacae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Enterobacter cloacae

Reaction

Reaction Comment Organism Reaction ID
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine mechanism, formation of a covalent intermediate between enzyme and enolpyruvate moiety Enterobacter cloacae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Enterobacter cloacae
0.1 0.12 partially purified enzyme Enterobacter cloacae
1.9
-
purified enzyme Enterobacter cloacae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
-
Enterobacter cloacae phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate r