Epoxidase

From Proteopedia

Revision as of 09:16, 6 February 2017

spinqualitylabelsall models Hydroxypropylphosphonic acid epoxidase complex with fosfomycin, glycerol, NO and Fe+2 ion (PDB code 3scf) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Hydroxypropylphosphonic acid epoxidase (HppE) is involved in the biosynthesis of the antibiotic fosfomycin[1]. HppE is a Zn+2/Fe+2-dependent enzyme. Halohydrin epoxidase (HHE) is involved in the degradation of halohydrins by the displacement of a halogen in halohydrins to produce the epoxide[2]. Relevance Fosfomycin is an antibiotic produced by some Streptomyces species. Structural highlights The active site of HppE contains fosfomycin and Fe+2. The enzyme uses an induced-fit mechanism to protect high-energy iron-oxygen species formed during catalysis by moving a β-hairpin termed cantilever to seal off the top portion of the active site[3].

3D structures of epoxidase

Updated on 06-February-2017

References

1. ↑ McLuskey K, Cameron S, Hammerschmidt F, Hunter WN. Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14221-6. Epub 2005 Sep 26. PMID:16186494
2. ↑ Watanabe F, Yu F, Ohtaki A, Yamanaka Y, Noguchi K, Yohda M, Odaka M. Crystal structures of halohydrin hydrogen-halide-lyases from Corynebacterium sp. N-1074. Proteins. 2015 Dec;83(12):2230-9. doi: 10.1002/prot.24938. Epub 2015 Oct 16. PMID:26422370 doi:http://dx.doi.org/10.1002/prot.24938
3. ↑ Yun D, Dey M, Higgins LJ, Yan F, Liu HW, Drennan CL. Structural Basis of Regiospecificity of a Mononuclear Iron Enzyme in Antibiotic Fosfomycin Biosynthesis. J Am Chem Soc. 2011 Jun 30. PMID:21682308 doi:10.1021/ja2025728