[Dihydroxyacetone synthase from the methanol-utilizing yeast Candida boidinii].
A procedure for purification of dihydroxyacetone synthase catalyzing the formation of dihydroxyacetone and glyceraldehyde 3-phosphate from formaldehyde and xylulose 5-phosphate has been developed. Using ion-exchangers with increasing affinity for dihydroxyacetone synthase, a homogenous preparation of the enzyme with specific activity of 2 u./mg has been obtained. The enzyme is made up of 2 subunits with m. w. of 76,000, contains thiamine pyrophosphate, requires Mg2+ for its activity and differs from yeast transketolase by substrate specificity and some other properties. The role of dihydroxyacetone synthase in metabolism of methanol-utilizing yeasts is discussed.
D019880:Aldehyde-Ketone Transferases; D002175:Candida / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D000432:Methanol / Q000378:metabolism*; D008970:Molecular Weight; D014166:Transferases / Q000302:isolation & purification* / Q000378:metabolism
D046911:Macromolecular Substances; D014166:Transferases; D019880:Aldehyde-Ketone Transferases; C031222:formaldehyde transketolase; D000432:Methanol
Dioksiatsetonsintaza metilotrofnykh drozhzhei Candida boidinii.