Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a particulate preparation from Pisum sativum.

Abstract:

:Mechanism of enzymatic conversion of a fatty acid to the corresponding alkane by the loss of the carboxyl carbon was investigated with particulate preparations from Pisum sativum. A heavy particulate preparation (sp. gr., 1.30 g/cm3) isolated by two density-gradient centrifugation steps catalyzed conversion of octadecanal to heptadecane and CO. Experiments with [1-3H,1-14C]octadecanal showed the stoichiometry of the reaction and retention of the aldehydic hydrogen in the alkane during this enzymatic decarbonylation. This decarbonylase showed an optimal pH of 7.0 and a Km of 35 microM for the aldehyde. This enzyme was severely inhibited by metal ion chelators and showed no requirement for any cofactors. Microsomal preparations and the particulate fractions from the first density-gradient step catalyzed acyl-CoA reduction to the corresponding aldehyde. Electron microscopic examination showed the presence of fragments of cell wall/cuticle but no vesicles in the decarbonylase preparation. It is concluded that the aldehydes produced by the acyl-CoA reductase located in the endomembranes of the epidermal cells are converted to alkanes by the decarbonylase located in the cell wall/cuticle region.

authors

Cheesbrough TM,Kolattukudy PE

doi

10.1073/pnas.81.21.6613

subject

Has Abstract

pub_date

1984-11-01 00:00:00

pages

6613-7

issue

21

eissn

0027-8424

issn

1091-6490

journal_volume

81

pub_type

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