ISSN:
1432-072X
Keywords:
Key wordsEnterobacter agglomerans
;
1
;
3-Propanediol dehydrogenase
;
Protein purification
;
Kinetic study
;
pH
;
Competitive inhibition
;
Mixed-type
;
inhibition
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme activity was optimal at pH 7.8. The enzyme was competitively inhibited by NAD+ (Ki of 0.29 mM), and 1,3-propanediol exerted a strong inhibitory effect according to a mixed-type inhibition with a Ki of 13.7 mM and an a-factor of 9.0. It is proposed that these dehydrogenase properties be extended to the dehydrogenases of Citrobacter freundii and Klebsiella pneumoniae, which exhibited numerous similar physical properties.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002030050482
Permalink