Dehaloperoxidase
From Proteopedia
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| - | <StructureSection load='4fh6' size='350' side='right' caption='Dehaloperoxidase heme-containing dimer complex with tribromophenol, O2 and sulfate ions (PDB entry [[4fh6]])' scene=''> | + | <StructureSection load='4fh6' size='350' side='right' caption='Dehaloperoxidase heme-containing dimer complex with tribromophenol, O2 and sulfate ions (PDB entry [[4fh6]])' scene='48/484818/Cv/1'> |
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'''Dehaloperoxidase''' (DHP) is a heme-containing globin possessing peroxidase enzymatic activity. DHP catalyzes the peroxide-dependent dehalogenation of halophenol. DHP A and DHP B are isoenzymes of DHP.<ref>PMID:24791647</ref> | '''Dehaloperoxidase''' (DHP) is a heme-containing globin possessing peroxidase enzymatic activity. DHP catalyzes the peroxide-dependent dehalogenation of halophenol. DHP A and DHP B are isoenzymes of DHP.<ref>PMID:24791647</ref> | ||
Revision as of 11:27, 28 December 2015
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3D structures of dehaloperoxidase
Updated on 28-December-2015
References
- ↑ Barrios DA, D'Antonio J, McCombs NL, Zhao J, Franzen S, Schmidt AC, Sombers LA, Ghiladi RA. Peroxygenase and oxidase activities of dehaloperoxidase-hemoglobin from Amphitrite ornata. J Am Chem Soc. 2014 Jun 4;136(22):7914-25. doi: 10.1021/ja500293c. Epub 2014 May , 21. PMID:24791647 doi:http://dx.doi.org/10.1021/ja500293c
- ↑ Zhao J, de Serrano VS, Zhao J, Le PD, Franzen S. Structural and kinetic study of an internal substrate binding site of dehaloperoxidase-hemoglobin A from Amphitrite ornata. Biochemistry. 2013 Mar 12. PMID:23480178 doi:http://dx.doi.org/10.1021/bi301307f
