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


ABSTRACT: 1. 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.

SUBMITTER: Lloyd D 

PROVIDER: S-EPMC1207214 | BioStudies | 1965-01-01

SECONDARY ACCESSION(S): 10.1042/bj0960766

REPOSITORIES: biostudies

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