Ontology highlight
ABSTRACT:
SUBMITTER: Daniel R
PROVIDER: S-EPMC176860 | biostudies-other | 1995 Apr
REPOSITORIES: biostudies-other
Journal of bacteriology 19950401 8
1,3-Propanediol dehydrogenase (EC 1.1.1.202) was purified to homogeneity from Citrobacter freundii grown anaerobically on glycerol in continuous culture. The enzyme is an octamer of a polypeptide of 43,400 Da. When tested as a dehydrogenase, the enzyme was most active with substrates containing two primary alcohol groups separated by one or two carbon atoms. In the physiological direction, 3-hydroxypropionaldehyde was the preferred substrate. The apparent Km values of the enzyme for 3-hydroxypro ...[more]