Carbon-carbon bond cleavage by cytochrome P450Biol (CYP107H1)

Max J. Cryle; James J. De Voss

Carbon-carbon bond cleavage by cytochrome P450Biol (CYP107H1)

Max J. Cryle, James J. De Voss

Research output: Contribution to journal › Article › Research › peer-review

Abstract

Cytochrome P450_Biol (CYP107H1) is believed to supply pimelic acid equivalents for biotin biosynthesis in Bacillus subtilis: we report here that the mechanistic pathway adopted by this multifunctional P450 for the in-chain cleavage of fatty acids is via consecutive formation of alcohol and threo-diol intermediates, with the likely absolute configuration of the intermediates also reported.

Original language	English
Pages (from-to)	86-87
Number of pages	2
Journal	Chemical Communications
Volume	10
Issue number	1
Publication status	Published - 7 Jan 2004
Externally published	Yes

Cite this

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title = "Carbon-carbon bond cleavage by cytochrome P450Biol (CYP107H1)",

abstract = "Cytochrome P450Biol (CYP107H1) is believed to supply pimelic acid equivalents for biotin biosynthesis in Bacillus subtilis: we report here that the mechanistic pathway adopted by this multifunctional P450 for the in-chain cleavage of fatty acids is via consecutive formation of alcohol and threo-diol intermediates, with the likely absolute configuration of the intermediates also reported.",

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year = "2004",

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T1 - Carbon-carbon bond cleavage by cytochrome P450Biol (CYP107H1)

AU - Cryle, Max J.

AU - De Voss, James J.

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N2 - Cytochrome P450Biol (CYP107H1) is believed to supply pimelic acid equivalents for biotin biosynthesis in Bacillus subtilis: we report here that the mechanistic pathway adopted by this multifunctional P450 for the in-chain cleavage of fatty acids is via consecutive formation of alcohol and threo-diol intermediates, with the likely absolute configuration of the intermediates also reported.

AB - Cytochrome P450Biol (CYP107H1) is believed to supply pimelic acid equivalents for biotin biosynthesis in Bacillus subtilis: we report here that the mechanistic pathway adopted by this multifunctional P450 for the in-chain cleavage of fatty acids is via consecutive formation of alcohol and threo-diol intermediates, with the likely absolute configuration of the intermediates also reported.

UR - https://www.scopus.com/pages/publications/1642458263

M3 - Article

AN - SCOPUS:1642458263

SN - 1359-7345

VL - 10

SP - 86

EP - 87

JO - Chemical Communications

JF - Chemical Communications

IS - 1

ER -

Carbon-carbon bond cleavage by cytochrome P450Biol (CYP107H1)

Abstract

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