Properties and sequence of the coenzyme B12-dependent glycerol dehydratase of Clostridium pasteurianum

FEMS Microbiol Lett. 1998 Jul 1;164(1):21-8. doi: 10.1111/j.1574-6968.1998.tb13062.x.

Abstract

The genes encoding coenzyme B12-dependent glycerol dehydratase of Clostridium pasteurianum were subcloned and expressed in Escherichia coli. The native molecular mass of the enzyme is 190,000 Da. The enzyme converts glycerol, 1,2-propanediol and 1,2-ethanediol to 3-hydroxypropionaldehyde, propionaldehyde and acetaldehyde, respectively, but glycerol is the preferred substrate. The nucleotide sequences of the dhaBCE genes encoding the three subunits of glycerol dehydratase and of orfZ whose function is unknown were determined. The deduced products of the dhaBCE genes with calculated molecular masses of 60,813, 19,549 and 16,722 Da, respectively, revealed high similarity to amino acid sequences of subunits of coenzyme B12-dependent glycerol and diol dehydratases from other organisms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Cloning, Molecular
  • Clostridium / enzymology*
  • DNA, Bacterial / genetics
  • Escherichia coli / enzymology
  • Glycerol / metabolism
  • Hydro-Lyases / chemistry*
  • Hydro-Lyases / genetics
  • Hydro-Lyases / metabolism
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Recombinant Proteins
  • Hydro-Lyases
  • glycerol dehydratase
  • Glycerol

Associated data

  • GENBANK/AF051373