Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 410-414 |
| Number of pages | 5 |
| Journal | Journal of Bioscience and Bioengineering |
| Volume | 101 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2006 May 1 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
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Cloning and nucleotide sequence of carbaryl hydrolase gene (cahA) from Arthrobacter sp. RC100. / Hashimoto, Masayuki; Mizutani, Atsushi; Tago, Kanako; Ohnishi-Kameyama, Mayumi; Shimojo, Takahiro; Hayatsu, Masahito.
In: Journal of Bioscience and Bioengineering, Vol. 101, No. 5, 01.05.2006, p. 410-414.Research output: Contribution to journal › Article
TY - JOUR
T1 - Cloning and nucleotide sequence of carbaryl hydrolase gene (cahA) from Arthrobacter sp. RC100
AU - Hashimoto, Masayuki
AU - Mizutani, Atsushi
AU - Tago, Kanako
AU - Ohnishi-Kameyama, Mayumi
AU - Shimojo, Takahiro
AU - Hayatsu, Masahito
PY - 2006/5/1
Y1 - 2006/5/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33746712376&partnerID=8YFLogxK
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U2 - 10.1263/jbb.101.410
DO - 10.1263/jbb.101.410
M3 - Article
VL - 101
SP - 410
EP - 414
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 5
ER -