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  Functional expression and characterization of cytochrome P450 52A21 from Candida albicans

Donghak, K., Cryle, M., De Voss, J. J., & Ortiz de Montellano, P. R. (2007). Functional expression and characterization of cytochrome P450 52A21 from Candida albicans. Archives of Biochemistry and Biophysics, 464(2), 213-220. doi:10.1016/j.abb.2007.02.032.

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Genre: Journal Article
Alternative Title : Functional expression and characterization of cytochrome P450 52A21 from Candida albicans

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ArchBiochemBiophys_464_2007_213.pdf (Any fulltext), 2MB
 
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Donghak, Kim, Author
Cryle, Max1, Author              
De Voss, James J., Author
Ortiz de Montellano, Paul R., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Cytochrome P450; Candida albicans; Fatty acid hydroxylase; Covalent heme binding; Halogen oxidation; Hydroxylation regiospecificity
 Abstract: Candida albicans contains 10 putative cytochrome P450 (CYP) genes coding for enzymes that appear to play important roles in fungal survival and virulence. Here, we report the characterization of CYP52A21, a putative alkane/fatty acid hydroxylase. The recombinant CYP52A21 protein containing a 6 × (His)-tag was expressed in Escherichia coli and was purified. The purified protein, reconstituted with rat NADPH-cytochrome P450 reductase, ω-hydroxylated dodecanoic acid to give 12-hydroxydodecanoic acid, but to a lesser extent also catalyzed (ω-1)-hydroxylation to give 11-hydroxydodecanoic acid. When 12,12,12-d3-dodecanoic acid was used as the substrate, there was a major shift in the oxidation from the ω- to the (ω-1)-hydroxylated product. The regioselectivity of fatty acid hydroxylation was examined with the 12-iodo-, 12-bromo-, and 12-chlorododecanoic acids. Although all three 12-halododecanoic acids bound to CYP52A21 with similar affinities, the production of 12-oxododecanoic acid decreased as the size of the terminal halide increased. The regioselectivity of CYP52A21 fatty acid oxidation is thus consistent with presentation of the terminal end of the fatty acid chain for oxidation via a narrow channel that limits access to other atoms of the fatty acid chain. This constricted access, in contrast to that proposed for the CYP4A family of enzymes, does not involve covalent binding of the heme to the protein.

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Language(s): eng - English
 Dates: 2007-01-182007-03-162007-08-15
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Archives of Biochemistry and Biophysics
Source Genre: Journal
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Publ. Info: New York : Academic Press
Pages: - Volume / Issue: 464 (2) Sequence Number: - Start / End Page: 213 - 220 Identifier: ISSN: 0003-9861
CoNE: https://pure.mpg.de/cone/journals/resource/991042745826956