IUBMB Enzyme Nomenclature

EC 1.14.19.7

Accepted name: (S)-2-hydroxypropylphosphonic acid epoxidase

Reaction: (S)-2-hydroxypropylphosphonate + 2 NADH + O2 = (1R,2S)-epoxypropylphosphonate + 2 H2O + 2 NAD+

Glossary: (1R,2S)-epoxypropylphosphonate = fosfomycin

Other name(s): HPP epoxidase; HppE; 2-hydroxypropylphosphonic acid epoxidase; Fom4; (S)-2-hydroxypropylphosphonate epoxidase

Systematic name: (S)-2-hydroxypropylphosphonate,NADH:oxygen epoxidase

Comments: Contains one non-heme iron centre per monomer [1,5]. FMN is required to mediate the transfer of reducing equivalents from NADH to the active site iron [1]. This is the last enzyme in the biosynthetic pathway of fosfomycin, a broad-spectrum antibiotic produced by certain Streptomyces species.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:

References:

1. Munos, J.W., Moon, S.J., Mansoorabadi, S.O., Chang, W., Hong, L., Yan, F., Liu, A. and Liu, H.W. Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae. Biochemistry 47 (2008) 8726-8735. [PMID: 18656958]

2. Yan, F., Moon, S.J., Liu, P., Zhao, Z., Lipscomb, J.D., Liu, A. and Liu, H.W. Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues. Biochemistry 46 (2007) 12628-12638. [PMID: 17927218]

3. Hidaka, T., Goda, M., Kuzuyama, T., Takei, N., Hidaka, M. and Seto, H. Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis. Mol. Gen. Genet. 249 (1995) 274-280. [PMID: 7500951]

4. Liu, P., Mehn, M.P., Yan, F., Zhao, Z., Que, L., Jr. and Liu, H.W. Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis. J. Am. Chem. Soc. 126 (2004) 10306-10312. [PMID: 15315444]

5. Higgins, L.J., Yan, F., Liu, P., Liu, H.W. and Drennan, C.L. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 437 (2005) 838-844. [PMID: 16015285]

[EC 1.14.19.7 created 2011]


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