1a8s
CHLOROPEROXIDASE F/PROPIONATE COMPLEX
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OverviewOverview
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 StructureAbout this Structure
1A8S is a [Single protein] structure of sequence from [Pseudomonas fluorescens] with SO4 and PPI as [ligands]. Active as [[1]], with EC number [1.11.1.10]. Full crystallographic information is available from [OCA].
ReferenceReference
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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