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Literature summary for 1.11.1.23 extracted from

  • Zhao, Z.; Liu, P.; Murakami, K.; Kuzuyama, T.; Seto, H.; Liu, H.W.
    Mechanistic studies of HPP epoxidase: configuration of the substrate governs its enzymatic fate (2002), Angew. Chem. Int. Ed. Engl., 41, 4529-4532.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
[(2S)-1,1-difluoro-2-hydroxypropyl]phosphonic acid tight binding inhibitor Streptomyces wedmorensis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron mononuclear non-heme iron-dependent enzyme Streptomyces wedmorensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2 Streptomyces wedmorensis
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cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+ i.e. fosfomycin ?

Organism

Organism UniProt Comment Textmining
Streptomyces wedmorensis Q56185
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
-
Streptomyces wedmorensis cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+ i.e. fosfomycin ?
additional information the enzyme also forms 2-oxopropylphosphonic acid from (R)-2-hydroxypropylphosphonic acid. HPP epoxidase is not selective with regard to substrate recognition, but can stereospecifically convert each enantiomer into a unique product with similar efficiency Streptomyces wedmorensis ?
-
?

Synonyms

Synonyms Comment Organism
HPP epoxidase
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Streptomyces wedmorensis