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| {{STRUCTURE_1ewa| PDB=1ewa | SCENE= }} | | {{STRUCTURE_1ewa| PDB=1ewa | SCENE= }} |
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| '''Dehaloperoxidase and 4-iodophenol'''
| | ===Dehaloperoxidase and 4-iodophenol=== |
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| ==Overview==
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| The full-length, protein coding sequence for dehaloperoxidase was obtained using a reverse genetic approach and a cDNA library from marine worm Amphitrite ornata. The crystal structure of the dehaloperoxidase (DHP) was determined by the multiple isomorphous replacement method and was refined at 1.8-A resolution. The enzyme fold is that of the globin family and, together with the amino acid sequence information, indicates that the enzyme evolved from an ancient oxygen carrier. The peroxidase activity of DHP arose mainly through changes in the positions of the proximal and distal histidines relative to those seen in globins. The structure of a complex of DHP with 4-iodophenol is also reported, and it shows that in contrast to larger heme peroxidases DHP binds organic substrates in the distal cavity. The binding is facilitated by the histidine swinging in and out of the cavity. The modeled position of the oxygen atom bound to the heme suggests that the enzymatic reaction proceeds via direct attack of the oxygen atom on the carbon atom bound to the halogen atom. | | The line below this paragraph, {{ABSTRACT_PUBMED_10751397}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10751397 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10751397}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Globin]] | | [[Category: Globin]] |
| [[Category: Peroxidase]] | | [[Category: Peroxidase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:35:37 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:07:04 2008'' |