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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제26권 제12호
- 발행연도
- 2016.12
- 수록면
- 2,087 - 2,097 (11page)
- DOI
- 10.4014/jmb.1608.08049
이용수
초록· 키워드
오류제보하기
Most cold-adapted enzymes possess higher Km and kcat values than those of their mesophilic counterparts to maximize the reaction rate. This characteristic is often ascribed to a high structural flexibility and improved dynamics in the active site. However, this may be less convincing to cold-adapted metabolic enzymes, which work at substrate concentrations near Km. In this respect, cold adaptation of a shikimate kinase (SK) in the shikimate pathway from psychrophilic Colwellia psychrerythraea (CpSK) was characterized by comparing it with a mesophilic Escherichia coli homolog (EcSK). The optimum temperatures for CpSK and EcSK activity were approximately 30°C and 40°C, respectively. The melting points were 33°C and 45°C for CpSK and EcSK, respectively. The ΔGH2O (denaturation in the absence of denaturing agent) values were 3.94 and 5.74 kcal/mol for CpSK and EcSK, respectively. These results indicated that CpSK was a cold-adapted enzyme. However, contrary to typical kinetic data, CpSK had a lower Km for its substrate shikimate than most mesophilic SKs, and the kcat was not increased. This observation suggested that CpSK may have evolved to exhibit increased substrate affinity at low intracellular concentrations of shikimate in the cold environment. Sequence analysis and homology modeling also showed that some important salt bridges were lost in CpSK, and higher Arg residues around critical Arg 140 seemed to increase flexibility for catalysis. Taken together, these data demonstrate that CpSK exhibits characteristics of cold adaptation with unusual kinetic parameters, which may provide important insights into the cold adaptation of metabolic enzymes.
목차
등록된 정보가 없습니다.
참고문헌 (59)
참고문헌 신청
Ásgeirsson B / 2006 / Microscopic rate-constants for substrate binding and acylation in cold-adaptation of trypsin I from Atlantic cod / FEBS Lett 580:4639~4644
Bentahir M / 2000 / Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the antarctic Pseudomonas sp / TACII18. J. Biol. Chem 275:11147~11153
Cerasoli E / 2002 / The refolding of type II shikimate kinase from Erwinia chrysanthemi aft er denat urat ion in urea / Eur. J. Biochem 269:2124~2132
Cheng W-C / 2005 / Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase / J. Bacteriol :8156~8163
Cheng W-C / 2012 / Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism / PLoS One 7:e33481
Bentahir M / 2000 / Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the antarctic Pseudomonas sp / TACII18. J. Biol. Chem 275:11147~11153
Cerasoli E / 2002 / The refolding of type II shikimate kinase from Erwinia chrysanthemi aft er denat urat ion in urea / Eur. J. Biochem 269:2124~2132
Cheng W-C / 2005 / Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase / J. Bacteriol :8156~8163
Cheng W-C / 2012 / Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism / PLoS One 7:e33481
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