Epoxidase
From Proteopedia
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| - | <StructureSection load='3scf' size='340' side='right' caption=' | + | <StructureSection load='3scf' size='340' side='right' caption='Hydroxypropylphosphonic acid epoxidase complex with fosfomycin, glycerol, NO and Fe+2 ion (PDB code [[3scf]])' scene=''> |
== Function == | == Function == | ||
'''Hydroxypropylphosphonic acid epoxidase''' (HppE) is involved in the biosynthesis of the antibiotic fosfomycin<ref>PMID:16186494</ref>. 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<ref>PMID:26422370</ref>. | '''Hydroxypropylphosphonic acid epoxidase''' (HppE) is involved in the biosynthesis of the antibiotic fosfomycin<ref>PMID:16186494</ref>. 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<ref>PMID:26422370</ref>. | ||
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| - | == Disease == | ||
== Relevance == | == Relevance == | ||
| + | Fosfomycin is an antibiotic produced by some ''Streptomyces'' species. | ||
== Structural highlights == | == 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<ref>PMID:21682308</ref>.. | |
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</StructureSection> | </StructureSection> | ||
Revision as of 09:15, 6 February 2017
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3D structures of epoxidase
Updated on 06-February-2017
References
- ↑ 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
- ↑ 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
- ↑ 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
