Cloning and expression of an ether-bond-cleaving enzyme involved in the metabolism of polyethylene glycol

Manabu Yamashita; Akio Tani; Fusako Kawai

doi:10.1263/jbb.98.313

Cloning and expression of an ether-bond-cleaving enzyme involved in the metabolism of polyethylene glycol

Manabu Yamashita, Akio Tani, Fusako Kawai

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

A gene encoding an ether-bond-cleaving enzyme, diglycolic acid dehydrogenase (DGADH) from polyethylene glycol-utilizing Pseudonocardia sp. strain K1, was cloned and expressed in Escherichia coli. The deduced amino acid sequence had a high homology with superoxide dismutases (SODs) from various bacteria. The recombinant protein showed the same activities as those of DGADH from Pseudonocardia sp. strain K1, namely, SOD activity and ether-bond-cleaving activity.

Original language	English
Pages (from-to)	313-315
Number of pages	3
Journal	Journal of Bioscience and Bioengineering
Volume	98
Issue number	4
DOIs	https://doi.org/10.1263/jbb.98.313
Publication status	Published - Oct 2004

Keywords

Ether-bond-cleaving enzyme
Metabolism of polyethylene glycol
Pseudonocardia sp. strain K1
Superoxide dismutase

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1263/jbb.98.313

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abstract = "A gene encoding an ether-bond-cleaving enzyme, diglycolic acid dehydrogenase (DGADH) from polyethylene glycol-utilizing Pseudonocardia sp. strain K1, was cloned and expressed in Escherichia coli. The deduced amino acid sequence had a high homology with superoxide dismutases (SODs) from various bacteria. The recombinant protein showed the same activities as those of DGADH from Pseudonocardia sp. strain K1, namely, SOD activity and ether-bond-cleaving activity.",

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author = "Manabu Yamashita and Akio Tani and Fusako Kawai",

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AU - Tani, Akio

AU - Kawai, Fusako

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AB - A gene encoding an ether-bond-cleaving enzyme, diglycolic acid dehydrogenase (DGADH) from polyethylene glycol-utilizing Pseudonocardia sp. strain K1, was cloned and expressed in Escherichia coli. The deduced amino acid sequence had a high homology with superoxide dismutases (SODs) from various bacteria. The recombinant protein showed the same activities as those of DGADH from Pseudonocardia sp. strain K1, namely, SOD activity and ether-bond-cleaving activity.

KW - Ether-bond-cleaving enzyme

KW - Metabolism of polyethylene glycol

KW - Pseudonocardia sp. strain K1

KW - Superoxide dismutase

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Cloning and expression of an ether-bond-cleaving enzyme involved in the metabolism of polyethylene glycol

Abstract

Keywords

ASJC Scopus subject areas

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