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 | |
| 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