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Propionate assimilation in the flagellate Polytomella caeca. An inducible mitochondrial enzyme system

Lloyd, D, Evans, D A and Venables, S A 1968. Propionate assimilation in the flagellate Polytomella caeca. An inducible mitochondrial enzyme system. Biochemical Journal 109 (5) , pp. 897-907. 10.1042/bj1090897

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Abstract

1. The assimilation of propionate by Polytomella caeca involves the beta-oxidation of this fatty acid. 2. Propionate-grown cells immediately oxidize propionate, beta-hydroxypropionate, malonic semialdehyde and acetate; acetate-grown cells oxidize propionate rapidly only after a lag of 2hr., and this adaptation of resting cells to propionate involves the formation of the enzymes of beta-oxidation. 3. The beta-hydroxypropionate dehydrogenase and malonic semialdehyde dehydrogenase activities of both propionate-grown and propionate-adapted cells are partly located in mitochondrial fractions. 4. Mitochondria isolated from propionate-grown cells, and also those from acetate-grown cells fully adapted to propionate, oxidize succinate, alpha-oxoglutarate, beta-hydroxypropionate and malonic semialdehyde; oxidation of these substrates is tightly coupled to the phosphorylation of ADP. 5. Mitochondria from acetate-grown cells exhibit ADP-dependent oxidation of succinate and alpha-oxoglutarate, but do not oxidize beta-hydroxypropionate or malonic semialdehyde. Mitochondria isolated from acetate-grown cells adapted to propionate for 5hr. slowly oxidize beta-hydroxypropionate and malonic semialdehyde, but no tightly coupled phosphorylation is detectable. 6. Two of the inducible enzymes of propionate oxidation are located within the NAD-impermeable barrier and appear to be membrane-bound. 7. The formation of the inducible enzymes is inhibited by cycloheximide and actinomycin D, but not by chloramphenicol.

Item Type: Article
Date Type: Submission
Status: Published
Schools: Biosciences
Publisher: Portland Press
ISSN: 0264-6021
Last Modified: 17 Feb 2020 10:30
URI: http://orca-mwe.cf.ac.uk/id/eprint/127880

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