Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1965 Sep;96(3):766–770. doi: 10.1042/bj0960766

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

D Lloyd 1
PMCID: PMC1207214  PMID: 4285894

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.

Full text

PDF
766

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Callely A. G., Lloyd D. The metabolism of propionate in the colourless alga, Prototheca zopfii. Biochem J. 1964 Aug;92(2):338–345. doi: 10.1042/bj0920338. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. JAKOBY W. B. Aldehyde oxidation. II. Evidence for closely juxtaposed sulfhydryl groups on dehydrogenases. J Biol Chem. 1958 May;232(1):89–97. [PubMed] [Google Scholar]
  3. JAKOBY W. B. Arsenite inhibition; a property common to aldehyde dehydrogenases. Arch Biochem Biophys. 1957 Aug;70(2):625–627. doi: 10.1016/0003-9861(57)90153-4. [DOI] [PubMed] [Google Scholar]
  4. Nirenberg M. W., Jakoby W. B. ON THE SITES OF ATTACHMENT AND REACTION OF ALDEHYDE DEHYDROGEN ASES. Proc Natl Acad Sci U S A. 1960 Feb;46(2):206–212. doi: 10.1073/pnas.46.2.206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. YAMADA E. W., JAKOBY W. B. Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A. J Biol Chem. 1960 Mar;235:589–594. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES