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Literature summary for 1.11.1.23 extracted from

  • Yan, F.; Li, T.; Lipscomb, J.D.; Liu, A.; Liu, H.W.
    Site-directed mutagenesis and spectroscopic studies of the iron-binding site of (S)-2-hydroxypropylphosphonic acid epoxidase (2005), Arch. Biochem. Biophys., 442, 82-91.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptomyces wedmorensis

Protein Variants

Protein Variants Comment Organism
E142A complete loss of enzymatic activity in vivo and in vitro, 2.1% of the active site iron as compared to wild-type enzyme, no self-hydroxylation at Tyr105 Streptomyces wedmorensis
H138A inactive in vivo, but in vitro it retains 27% of the active site iron and nearly 20% of the wild-type activity, limited self-hydroxylation (at Tyr105) Streptomyces wedmorensis
H180A complete loss of enzymatic activity in vivo and in vitro, 5.8% of the active site iron as compared to wild-type enzyme, no self-hydroxylation at Tyr105 Streptomyces wedmorensis

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Streptomyces wedmorensis Q56185
-
-

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 ?

Synonyms

Synonyms Comment Organism
fom4
-
Streptomyces wedmorensis

Cofactor

Cofactor Comment Organism Structure
FMN
-
Streptomyces wedmorensis
NADH
-
Streptomyces wedmorensis