| 학회 |
한국공업화학회 |
| 학술대회 |
2015년 가을 (11/04 ~ 11/06, 제주국제컨벤션센터(ICCJEJU)) |
| 권호 |
19권 2호 |
| 발표분야 |
유용물질 자원화를 위한 이산화탄소의 생물학적 이용 (KCRC 특별세션) |
| 제목 |
Structural insight into the same substrate, same product, different chirality, and different bio-product by PaaH1 and PhaB from Ralstonia eutropha |
| 초록 |
Ralstonia eutropha can utilizes carbondioxide as a carbon source and produce various valuable bioproducts including polyhydroxyalkanoates (PAH). (S)-3-hydroxybutyryl-CoA dehydrogenase is an enzyme involved in n-butanol by catalyzing the conversion from acetoacetyl-CoA to (S)-3-hydroxylbutyryl-CoA. In order to elucidate the molecular mechanism of n-butanol biosynthesis, we determined a crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase from R. eutropha (RePaaH1). The enzyme functions as a homotetramer. Through the structure in complex with its substrate and cofactor, we revealed binding modes of NAD cofactor and acetoacetyl-CoA substrate. We measured kinetic parameters of the enzyme, and confirmed the key residues for enzyme catalysis by site-directed mutagenesis. (R)-3-hydroxybutyryl-CoA dehydrogenase is an enzyme involved in PHA by catalyzing the conversion from acetoacetyl-CoA to (R)-3-hydroxylbutyryl-CoA. We determined the crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase from R. eutropha (RePhaB). Unlike RePaaH1, RePhaB utilizes NADP as a cofactor, and functions as a homodimer. Through the structure in complex with its substrate and cofactor, we revealed binding modes of NADP cofactor and acetoacetyl-CoA substrate. In summary, by determining two 3-hydroxybutyryl-CoA dehydrogenases, we elucidated how these enzymes produce different chiral product using the same substrate. |
| 저자 |
김경진 |
| 소속 |
경북대 |
| 키워드 |
Ralstonia eutropha; PHA; structure
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| E-Mail |
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