The purification and properties of malonic semialdehyde oxidative decarboxylase from Prototheca zopfii.
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.
D001152:Arsenicals; D002262:Carboxy-Lyases / Q000378:metabolism*; D003065:Coenzyme A; D004798:Enzymes; D005033:Ethylmaleimide; D056890:Eukaryota / Q000201:enzymology*; D066298:In Vitro Techniques; D008314:Malonates; D009243:NAD; D014508:Urea
D001152:Arsenicals; D004798:Enzymes; D008314:Malonates; D009243:NAD; D014508:Urea; D002262:Carboxy-Lyases; D005033:Ethylmaleimide; D003065:Coenzyme A