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.

Search for more literature for 1.11.1.23

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

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Release 2023.1 (January 2023)