Cloning and nucleotide sequence of carbaryl hydrolase gene ( cahA) from Arthrobacter sp. RC100

A carbaryl hydrolase gene ( cahA) encoded on the plasmid pRC1 in Arthrobacter sp. RC100 was cloned and sequenced. The entire region of the deduced amino acid sequence was found to be homologous to that of an amidase family. Parts of the consensus sequences of the amidase gene have been identified in...

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Bibliographic Details
Published in:Journal of bioscience and bioengineering 2006-05, Vol.101 (5), p.410-414
Main Authors: Hashimoto, Masayuki, Mizutani, Atsushi, Tago, Kanako, Ohnishi-Kameyama, Mayumi, Shimojo, Takahiro, Hayatsu, Masahito
Format: Article
Language:English
Subjects:
amidase
Amidohydrolases - chemistry
Amidohydrolases - genetics
Amidohydrolases - isolation & purification
Amidohydrolases - metabolism
Amino Acid Sequence
ARTHROBACTER
Arthrobacter - enzymology
Arthrobacter - genetics
Base Sequence
Biological and medical sciences
Biotechnology
CARBAMATE
carbamate pesticides
CARBAMATES
CARBAMATOS
carbaryl degradation
CLONACION MOLECULAR
CLONAGE MOLECULAIRE
Cloning, Molecular - methods
Enzyme Activation
Enzyme Stability
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Fundamental and applied biological sciences. Psychology
HIDROLASAS
HYDROLASE
HYDROLASES
Hydrolysis
MOLECULAR CLONING
Molecular Sequence Data
Molecular Weight
NUCLEOTIDE SEQUENCE
PESTICIDE
PESTICIDES
PLAGUICIDAS
plasmid
Protein Engineering - methods
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
SECUENCIA NUCLEOTIDICA
SEQUENCE NUCLEOTIDIQUE
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Description
Summary:A carbaryl hydrolase gene ( cahA) encoded on the plasmid pRC1 in Arthrobacter sp. RC100 was cloned and sequenced. The entire region of the deduced amino acid sequence was found to be homologous to that of an amidase family. Parts of the consensus sequences of the amidase gene have been identified in CahA from strain RC100. CahA was overexpressed in Escherichia coli JM109, and the enzyme was purified to homogeneity by protamine sulfate treatment, ammonium sulfate precipitation, and hydrophobic and anion-exchange chromatographies. The purified enzyme showed hydrolase activity toward 1-naphthylacetamide and isobutyramide but showed no activity toward 1-naphthylacetate. This is the first report of an amidase that is able to hydrolyze N-methylcarbamate pesticides.
ISSN:1389-1723
1347-4421
DOI:10.1263/jbb.101.410