Characterization of Phosphoenolpyruvate Carboxylase from Oceanimonas smirnovii in Escherichia coli
- Authors
- Park, Soohyun; Lee, Wangjun; Kim, Hyeonsoo; Pack, Seung Pil; Lee, Jinwon
- Issue Date
- 9월-2015
- Publisher
- HUMANA PRESS INC
- Keywords
- Oceanimonas smirnovii; Phosphoenolpyruvate carboxylase; Characterization; Bicarbonate
- Citation
- APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, v.177, no.1, pp.217 - 225
- Indexed
- SCIE
SCOPUS
- Journal Title
- APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
- Volume
- 177
- Number
- 1
- Start Page
- 217
- End Page
- 225
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/92654
- DOI
- 10.1007/s12010-015-1739-3
- ISSN
- 0273-2289
- Abstract
- In this study, phosphoenolpyruvate carboxylase (PEPC) derived from Oceanimonas smirnovii (OS) was expressed as a soluble protein in Escherichia coli BL21(DE3). We isolated OS-PEPC (a recombinant PEPC protein) by his-tag purification. The purified protein showed a single band upon analysis with SDS-PAGE, and it had an apparent molecular mass of 98 kDa. Pufied OS-PEPC showed a specific activity value of 21.8 +/- A 0.495 U/mg protein. Especially, OS-PEPC showed the enzymatic activity between 40 and 50 A degrees C. It maintained enzymatic activity in basic pH conditions (pH value, 9-10). We also measured OS-PEPC PEP and HCO3 (-) saturation kinetics and confirmed the effect of divalent cation on OS-PEPC activity.
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Collections - Graduate School > Department of Biotechnology and Bioinformatics > 1. Journal Articles
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