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

Lloyd, D ORCID: https://orcid.org/0000-0002-5656-0571, 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

Full text not available from this repository.

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:	26 Oct 2022 08:36
URI:	https://orca.cardiff.ac.uk/id/eprint/127880

Citation Data

Cited 11 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item