지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2025.4
- 수록면
- 167 - 178 (12page)
이용수
초록· 키워드
오류제보하기
The enzyme MGG_00097 from rice blast fungus (Magnaporthe grisea) is a NADPH-dependent oxidoreductase, involved in synthesizing glycerol from dihydroxyacetone phosphate and dihydroxyacetone. The 35.5-kDa monomer belongs to the aldo-keto reductase superfamily, characterized by a highly conserved catalytic tetrad. This study, elucidates the expression, purification, and kinetic properties of recombinant MGG_00097. The ternary complex of MGG_00097 with NADP+ and glycerol was refined to a 2.9 Å resolution, revealing critical insights into substrate binding and catalysis. NADP+ binds within the active site, with residues Ser221, Leu223, Ser225, Lys271, Ser272, Ser273, Thr274, Arg277, and Asn281 forming the substrate and cofactor-binding pockets. A Y56A mutation reveals the open conformation of the cofactor-binding pocket, with Glu29 and Gln226 functioning as hinge residues for the conformational changes upon cofactor binding. These findings contribute to the understanding of MGG_00097’s catalytic mechanism and offer a basis for further biochemical and potential biotechnological applications.
목차
Materials and Methods
Results and Discussion
References
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