Dehaloperoxidase

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{{STRUCTURE_1ewa| PDB=1ewa | SIZE=400| SCENE= |right|CAPTION=Dehaloperoxidase heme-containing dimer complex with iodophenol and sulfate ions, [[1ewa]] }}
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<StructureSection load='1ewa' size='350' side='right' caption='Dehaloperoxidase heme-containing dimer complex with iodophenol and sulfate ions (PDB entry [[1ewa]])' scene=''>
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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.
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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:11742345</ref>
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</StructureSection>
==3D structures of dehalperoxidase==
==3D structures of dehalperoxidase==
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**[[4kjt]] - AoDHP A (mutant) + O2<br />
**[[4kjt]] - AoDHP A (mutant) + O2<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 11:09, 22 December 2015


Dehaloperoxidase heme-containing dimer complex with iodophenol and sulfate ions (PDB entry 1ewa)

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3D structures of dehalperoxidase

Updated on 22-December-2015

References

  1. Larsen NA, Turner JM, Stevens J, Rosser SJ, Basran A, Lerner RA, Bruce NC, Wilson IA. Crystal structure of a bacterial cocaine esterase. Nat Struct Biol. 2002 Jan;9(1):17-21. PMID:11742345 doi:10.1038/nsb742

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Michal Harel, Alexander Berchansky

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