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Literature summary for 2.5.1.7 extracted from

  • Schoenbrunn, E.; Sack, S.; Eschenburg, S.; Perrakis, A.; Krekel, F.; Amrhein, N.; Mandelkow, E.
    Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin (1996), Structure, 4, 1065-1075.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of substrate-free enzyme, two-domain structure with an unusual fold, inside out alpha/beta barrel, which is built up from the 6fold repetititon of one folding unit, structure analysis Enterobacter cloacae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine Enterobacter cloacae enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
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Organism

Organism UniProt Comment Textmining
Enterobacter cloacae
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Reaction

Reaction Comment Organism Reaction ID
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine Cys115 is the active site nucleophile Enterobacter cloacae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
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Enterobacter cloacae phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
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?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan Enterobacter cloacae phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
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?

Synonyms

Synonyms Comment Organism
EPT
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Enterobacter cloacae
UDP-N-acetylglucosamine enolpyruvyltransferase
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Enterobacter cloacae