Molecular cloning, sequencing and characterization of the genes for adenosylcobalamin-dependent diol dehydratase of Klebsiella pneumoniae.
Klebsiella pneumoniae and some of the other Enterobacteriaceae form both diol dehydratase and glycerol dehydratase in response to growth substrates. To compare these enzymes produced by the same bacterium, the pdd genes of K. pneumoniae encoding adenosylcobalamin-dependent diol dehydratase were cloned and sequenced. The sequential three open reading frames (pddA, pddB, and pddC genes) encoded polypeptides of 554, 228, and 174 amino acid residues with predicted molecular weights of 60,379(alpha), 24,401(beta), and 19,489(gamma), respectively. The deduced amino acid sequences of the subunits were 84-100% and 54-71% identical with those reported for diol dehydratases and glycerol dehydratases, respectively.
Tobimatsu
T
T
Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, Japan.
Azuma
M
M
Hayashi
S
S
Nishimoto
K
K
Toraya
T
T
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003038:Cobamides / Q000378:metabolism*; D005798:Genes, Bacterial; D007711:Klebsiella pneumoniae / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D011408:Propanediol Dehydratase / Q000235:genetics*; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D003038:Cobamides; D011408:Propanediol Dehydratase; C000913:cobamamide