Structural investigation of the cofactor-free chloroperoxidases
| Autor: | Josef Altenbuchner, I. Pelletier, H.-J. Hecht, B. Hofmann, K.-H. Van Pee, Sabine Tölzer |
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| Rok vydání: | 1998 |
| Předmět: |
Protein Conformation
Stereochemistry Molecular Sequence Data Streptomyces aureofaciens Pseudomonas fluorescens Reaction intermediate Crystallography X-Ray Structure-Activity Relationship Bacterial Proteins Structural Biology Pseudomonas Haloperoxidase Amino Acid Sequence Binding site Molecular Biology chemistry.chemical_classification biology Chemistry Active site Halogenation biology.organism_classification Streptomyces Enzyme biology.protein Chloride Peroxidase Sequence Alignment Sequence Analysis |
| Zdroj: | Journal of Molecular Biology. 279:889-900 |
| ISSN: | 0022-2836 |
| DOI: | 10.1006/jmbi.1998.1802 |
| Popis: | The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens , Streptomyces lividans , and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites. |
| Databáze: | OpenAIRE |
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