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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제30권 제12호
- 발행연도
- 2020.1
- 수록면
- 1,905 - 1,911 (7page)
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Homoserine dehydrogenase (HSD) catalyzes the reversible conversion of L-aspartate-4- semialdehyde to L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine. HSD has attracted great attention for medical and industrial purposes due to its recognized application in the development of pesticides and is being utilized in the large scale production of L-lysine. In this study, HSD from Bacillus subtilis (BsHSD) was overexpressed in Escherichia coli and purified to homogeneity for biochemical characterization. We examined the enzymatic activity of BsHSD for L-homoserine oxidation and found that BsHSD exclusively prefers NADP+ to NAD+ and that its activity was maximal at pH 9.0 and in the presence of 0.4 M NaCl. By kinetic analysis, Km values for L-homoserine and NADP+ were found to be 35.08 ± 2.91 mM and 0.39 ± 0.05 mM, respectively, and the Vmax values were 2.72 ± 0.06 μmol/min-1 mg-1 and 2.79 ± 0.11 μmol/ min-1 mg-1, respectively. The apparent molecular mass determined with size-exclusion chromatography indicated that BsHSD forms a tetramer, in contrast to the previously reported dimeric HSDs from other organisms. This novel oligomeric assembly can be attributed to the additional C-terminal ACT domain of BsHSD. Thermal denaturation monitoring by circular dichroism spectroscopy was used to determine its melting temperature, which was 54.8°C. The molecular and biochemical features of BsHSD revealed in this study may lay the foundation for future studies on amino acid metabolism and its application for industrial and medical purposes.
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참고문헌 (15)
참고문헌 신청
Jacques SL / 2001 / Characterization of yeast homoserine dehydrogenase, an antifungal target : the invariant histidine 309 is important for enzyme integrity / Biochim. Biophys. Acta 1544:28~41
Akai S / 2019 / The crystal structure of homoserine dehydrogenase complexed with l-homoserine and NADPH in a closed form / J. Biochem 165:185~195
DeLaBarre B / 2000 / Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases / Nat. Struct. Biol 7:238~244
Hayashi J / 2015 / Crystal structures of a hyperthermophilic archaeal homoserine dehydrogenase suggest a novel cofactor binding mode for oxidoreductases / Sci. Rep 5:11674
Navratna V / 2015 / Structural basis for the catalytic mechanism of homoserine dehydrogenase / Acta Crystallogr. D Biol. Crystallogr 71:1216~1225
Akai S / 2019 / The crystal structure of homoserine dehydrogenase complexed with l-homoserine and NADPH in a closed form / J. Biochem 165:185~195
DeLaBarre B / 2000 / Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases / Nat. Struct. Biol 7:238~244
Hayashi J / 2015 / Crystal structures of a hyperthermophilic archaeal homoserine dehydrogenase suggest a novel cofactor binding mode for oxidoreductases / Sci. Rep 5:11674
Navratna V / 2015 / Structural basis for the catalytic mechanism of homoserine dehydrogenase / Acta Crystallogr. D Biol. Crystallogr 71:1216~1225
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