Literature summary for 1.11.1.23 extracted from

Liu, P.; Mehn, M.P.; Yan, F.; Zhao, Z.; Que, L. Jr.; Liu, H.W.
Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis (2004), J. Am. Chem. Soc., 126, 10306-10312.

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Protein Variants

Protein Variants	Comment	Organism
Y102F	mutant maintains 60% of the activity of the wild-type enzyme	Streptomyces wedmorensis
Y103F	mutant maintains 60% of the activity of the wild-type enzyme	Streptomyces wedmorensis
Y105F	mutant enzyme is inactive	Streptomyces wedmorensis

Organism

Organism	UniProt	Comment	Textmining
Streptomyces wedmorensis	Q56185	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
side-chain modification	DOPA formation, probably at Tyr105, is a self-hydroxylation reaction	Streptomyces wedmorensis

Reaction

Reaction	Comment	Organism	Reaction ID
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O	Tyr105 is a key residue, which plays a role in the activation of dioxygen required for the enzymatic activity of HppE	Streptomyces wedmorensis	a

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Release 2023.1 (January 2023)