Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100

Appl Environ Microbiol. 2002 Mar;68(3):1220-7. doi: 10.1128/AEM.68.3.1220-1227.2002.


Rhizobium sp. strain AC100, which is capable of degrading carbaryl (1-naphthyl-N-methylcarbamate), was isolated from soil treated with carbaryl. This bacterium hydrolyzed carbaryl to 1-naphthol and methylamine. Carbaryl hydrolase from the strain was purified to homogeneity, and its N-terminal sequence, molecular mass (82 kDa), and enzymatic properties were determined. The purified enzyme hydrolyzed 1-naphthyl acetate and 4-nitrophenyl acetate indicating that the enzyme is an esterase. We then cloned the carbaryl hydrolase gene (cehA) from the plasmid DNA of the strain and determined the nucleotide sequence of the 10-kb region containing cehA. No homologous sequences were found by a database homology search using the nucleotide and deduced amino acid sequences of the cehA gene. Six open reading frames including the cehA gene were found in the 10-kb region, and sequencing analysis shows that the cehA gene is flanked by two copies of insertion sequence-like sequence, suggesting that it makes part of a composite transposon.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Base Sequence*
  • Biodegradation, Environmental
  • Carbaryl / metabolism*
  • Carboxylic Ester Hydrolases / genetics*
  • Carboxylic Ester Hydrolases / isolation & purification
  • Carboxylic Ester Hydrolases / metabolism
  • Cloning, Molecular
  • Insecticides / metabolism*
  • Molecular Sequence Data
  • Physical Chromosome Mapping
  • Plasmids
  • Polymerase Chain Reaction
  • Rhizobium / enzymology*
  • Rhizobium / genetics
  • Sequence Analysis, DNA


  • Bacterial Proteins
  • Insecticides
  • Carboxylic Ester Hydrolases
  • Carbaryl

Associated data

  • GENBANK/AB069723
  • GENBANK/AB069724