Open AccessGlycerol conversion to 1,3‐propanediol by Clostridium pasteurianum : cloning and expression of the gene encoding 1,3‐propanediol dehydrogenase
Author(s) -
Luers Frauke,
Seyfried Markus,
Daniel Rolf,
Gottschalk Gerhard
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12665.x
Subject(s) - 1,3 propanediol , citrobacter freundii , gene , biochemistry , biology , microbiology and biotechnology , escherichia coli , glycerol kinase , glycerol , alcohol dehydrogenase , dehydrogenase , enzyme , chemistry , enterobacteriaceae
When grown on glycerol as sole carbon and energy source, cell extracts of Clostridium pasteurianum exhibited activities of glycerol dehydrogenase, dihydroxyacetone kinase, glycerol dehydratase and 1,3‐propanediol dehydrogenase. The genes encoding the latter two enzymes were cloned by colony hybridization using the dhaT gene of Citrobacter freundii as a heterologous DNA probe and expressed in Escherichia coli . The native molecular mass of 1,3‐propanediol dehydrogenase (DhaT) is 440 000 Da. The dhaT gene of C. pasteurianum was subcloned and its nucleotide sequence (1158 bp) was determined. The deduced gene product (41 776 Da) revealed high similarity to DhaT of C. freundii (80.5% identity; 89.8% similarity).