The purification and properties of malonic semialdehyde oxidative decarboxylase from Prototheca zopfii.

Lloyd, D. ORCID: https://orcid.org/0000-0002-5656-0571 1965. The purification and properties of malonic semialdehyde oxidative decarboxylase from Prototheca zopfii. Biochemical Journal 3 , IMPORTED. 10.1042/bj0960766

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Abstract

An enzyme, which in the presence of NAD(+) and CoA oxidizes malonic semialdehyde to acetyl-CoA, has been purified from an extract of the colourless alga Prototheca zopfii. 2. The purified enzyme has optimum pH7.5, is specific for NAD(+) and requires a thiol compound for maximum activity. 3. The enzyme is inhibited by arsenite, N-ethylmaleimide and urea. 4. The results are discussed in relation to those obtained by other workers with a similar bacterial enzyme, and a possible reaction sequence is proposed.

Item Type:	Article
Date Type:	Publication
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/127874

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