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

Lloyd, D. 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: 11 Mar 2020 14:30
URI: http://orca.cf.ac.uk/id/eprint/127874

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