Epoxidase

(Difference between revisions)

Revision as of 10:01, 12 March 2019

Hydroxypropylphosphonic acid epoxidase complex with fosfomycin, glycerol, NO and Fe+2 ion (PDB code 3scf)

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Updated on 12-March-2019

↑ 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

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 == Structural highlights ==
-The <scene name='75/752206/Cv/5'>active site of HppE contains fosfomycin and Fe+2</scene>. The enzyme uses an induced-fit mechanism to protect high-energy iron-oxygen species formed during catalysis by moving a <scene name='75/752206/Cv/4'>β-hairpin termed cantilever</scene> to seal off the top portion of the active site<ref>PMID:21682308</ref>. <scene name='75/752206/Cv/2'>Fe coordination site</scene>.
+The <scene name='75/752206/Cv/6'>active site of HppE contains fosfomycin and Fe+2</scene>. The enzyme uses an induced-fit mechanism to protect high-energy iron-oxygen species formed during catalysis by moving a <scene name='75/752206/Cv/7'>β-hairpin termed cantilever</scene> to seal off the top portion of the active site<ref>PMID:21682308</ref>. <scene name='75/752206/Cv/8'>Fe coordination site</scene>.
 </StructureSection>