1a8u

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Streptomyces aureofaciens]]
[[Category: Streptomyces aureofaciens]]
[[Category: Altenbuchner, J.]]
[[Category: Altenbuchner, J.]]
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[[Category: Hecht, H.J.]]
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[[Category: Hecht, H J.]]
[[Category: Hofmann, B.]]
[[Category: Hofmann, B.]]
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[[Category: Pee, K.H.Van.]]
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[[Category: Pee, K H.Van.]]
[[Category: Pelletier, I.]]
[[Category: Pelletier, I.]]
[[Category: Toelzer, S.]]
[[Category: Toelzer, S.]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:29:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:09 2008''

Revision as of 09:42, 21 February 2008


1a8u, resolution 1.60Å

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CHLOROPEROXIDASE T/BENZOATE COMPLEX

Overview

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.

About this Structure

1A8U is a Single protein structure of sequence from Streptomyces aureofaciens with and as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

Structural investigation of the cofactor-free chloroperoxidases., Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ, J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069

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