Display options
Cite
Ohshiro K, Kakuta T, Nikaidou N, et al. Molecular cloning and nucleotide sequencing of organophosphorus insecticide hydrolase gene from Arthrobacter sp. strain B-5. J Biosci Bioeng. 1999;87(4):531-4doi: 10.1016/s1389-1723(99)80105-4.
Ohshiro, K., Kakuta, T., Nikaidou, N., Watanabe, T., & Uchiyama, T. (1999). Molecular cloning and nucleotide sequencing of organophosphorus insecticide hydrolase gene from Arthrobacter sp. strain B-5. Journal of bioscience and bioengineering, 87(4), 531-4. https://doi.org/10.1016/s1389-1723(99)80105-4
Ohshiro, K, et al. "Molecular cloning and nucleotide sequencing of organophosphorus insecticide hydrolase gene from Arthrobacter sp. strain B-5." Journal of bioscience and bioengineering vol. 87,4 (1999): 531-4. doi: https://doi.org/10.1016/s1389-1723(99)80105-4
Ohshiro K, Kakuta T, Nikaidou N, Watanabe T, Uchiyama T. Molecular cloning and nucleotide sequencing of organophosphorus insecticide hydrolase gene from Arthrobacter sp. strain B-5. J Biosci Bioeng. 1999;87(4):531-4. doi: 10.1016/s1389-1723(99)80105-4. PMID: 16232510.
Copy Download .nbib Format: NLM
Share it on

J Biosci Bioeng. 1999;87(4):531-4. doi: 10.1016/s1389-1723(99)80105-4.

Molecular cloning and nucleotide sequencing of organophosphorus insecticide hydrolase gene from Arthrobacter sp. strain B-5.

Journal of bioscience and bioengineering

K Ohshiro, T Kakuta, N Nikaidou, T Watanabe, T Uchiyama

Affiliations

  1. Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, 2-8050 Ikarashi, Niigata 950-2102, Japan.

PMID: 16232510 DOI: 10.1016/s1389-1723(99)80105-4

Abstract

The organophosphorus insecticide hydrolase (OPH) gene of Arthrobacter sp. strain B-5, isolated from turf green soil was cloned into Escherichia coli JM109. Three clones, termed EpB511, EpB521 and EpB531, exhibiting OPH activity were obtained. However, these three clones showed lower OP-degrading ability than strain B-5. A 7.7-kb inserted fragment of the plasmid pB521 harbored by EpB521 was subcloned, resulting in construction of a plasmid, pB526, carrying the 2.6-kb inserted fragment with OP-degrading ability. In this sequence, an open reading frame (ORF) that encodes a 43,607 Da polypeptide composed of 415 amino acids was identified. The N-terminal amino acid sequence deduced from the nucleotide sequence was identical to that of purified OPHs. The deduced amino acid sequence was compared with the sequences in the data bank and a 58.1% amino acid identity was found with the aryldialkylphosphatase from Nocardia sp. strain B-1, an enzyme that possesses catalytic functions similar to OPH.

Publication Types