A natural heme-signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω-hydroxylation.

doi:10.1111/febs.13104

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Article

A natural heme-signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω-hydroxylation.

The FEBS journal - 1 Jan 2015

Khatri Yogan, Hannemann Frank, Girhard Marco, Kappl Reinhard, Hutter Michael, Urlacher Vlada B, Bernhardt Rita

Abstract excerpt

A novel naturally occurring heme-signature variant of CYP267A1 from myxobacterium Sorangium cellulosum So ce56 and its mutant L366F, the actual mimic of the 'conserved' heme-signature of cytochromes P450, were heterologously expressed in Escherichia coli in a soluble form and purified. The UV-visible characteristics of both variants were highly similar. Although leucine replaced the phenylalanine in the...

Topics

Amino Acid Sequence
Amino Acid Substitution
Animals
Bacterial Proteins
Catalytic Domain
Cattle
Conserved Sequence
Cytochrome P-450 Enzyme System
Electron Spin Resonance Spectroscopy
Fatty Acids
Gas Chromatography-Mass Spectrometry
Genetic Variation
Heme

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Hydroxylation

Models, Molecular

Molecular Sequence Data

Mutagenesis, Site-Directed

Myxococcales

Source

Open in PubMed

Identifiers

PMID: 25302415
DOI: 10.1111/febs.13104

Provenance

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