Dehalogenase
From Proteopedia
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<StructureSection load='2edc' size='340' side='right' caption='Structure of haloalkane dehalogenase complex with I- ion (purple) (PDB code [[2edc]]).' scene=''> | <StructureSection load='2edc' size='340' side='right' caption='Structure of haloalkane dehalogenase complex with I- ion (purple) (PDB code [[2edc]]).' scene=''> | ||
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== Function == | == Function == | ||
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• '''5-chloromuconolactone dehalogenase''' converts 5-chloromuconolactone to E-dienelactone.<br /> | • '''5-chloromuconolactone dehalogenase''' converts 5-chloromuconolactone to E-dienelactone.<br /> | ||
• '''Tetrachloroethene reductive dehalogenase''' catalyzes the conversion of trichloroethene, Cl- and acceptor to tetrachloroethene and reduced acceptor. | • '''Tetrachloroethene reductive dehalogenase''' catalyzes the conversion of trichloroethene, Cl- and acceptor to tetrachloroethene and reduced acceptor. | ||
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| - | == Disease == | ||
== Relevance == | == Relevance == | ||
| - | Haloalkane dehalogenase is tested for the biodegredation of toxic industrial by-products. | + | Haloalkane dehalogenase is tested for the biodegredation of toxic industrial by-products. Fluoroacetate dehalogenase is tested for the biodegredation of the poisonous fluroacetate which can kill livestock and is found in some plants in Australia, Africa and Central America. |
== Structural highlights == | == Structural highlights == | ||
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| + | In the fluoroacetate dehalogenase complex with halide, the iodide is seen in the active site cavity between two tryptophanes.<ref>PMID:8369276</ref> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:37, 22 December 2015
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3D structures of dehalogenase
Updated on 22-December-2015
References
- ↑ Koudelakova T, Chovancova E, Brezovsky J, Monincova M, Fortova A, Jarkovsky J, Damborsky J. Substrate specificity of haloalkane dehalogenases. Biochem J. 2011 Apr 15;435(2):345-54. doi: 10.1042/BJ20101405. PMID:21294712 doi:http://dx.doi.org/10.1042/BJ20101405
- ↑ Verschueren KH, Kingma J, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW. Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site. Biochemistry. 1993 Sep 7;32(35):9031-7. PMID:8369276
