현재 위치
Home
Session 4: Life Science & Physical Science
Functional characterization of CYP105D17 from Streptomyces laurentii
-
- 발행기관
- 선문효정학술연구회 바로가기
-
- 간행물
- 선문효정학술연구회 학술대회 프로시딩 바로가기
-
- 통권
- Proceedings of THE 1st INTERNATIONAL CONFERENCE OF HYOJEONG ACADEMY 2023 (2023.01)바로가기
-
- 페이지
- pp.56-61
-
- 저자
-
- 언어
- 영어(ENG)
-
- URL
- https://www.earticle.net/Article/A488970
※ 기관로그인 시 무료 이용이 가능합니다.
4,000원
원문정보
초록
- 영어
- Streptomycetaceae family genomes contain a higher number of CYP genes as compared to other bacterial species. Especially, the CYP105 family is widely distributed and involved in biosynthetic pathways of secondary metabolites and modification of structurally associated xenobiotics. Here, we identified CYP105D17 associated with the predicted lanthipetide biosynthesis gene cluster from Streptomyces laurentii. The actual function of the gene cluster is still unknown, and CYP105D17 showed 81.8% identity with already characterized CYP105D18 from the same strain. The molecular weight of the protein was analyzed by SDS-PAGE to be ≈ 49 kDa. CYP105D17 also catalyzed the N-oxidation of papaverine in the presence of co-substrate (Hydrogen peroxide) H2O2 like CYP105D18. The optimum rate of papaverine N-oxide conversion by CYP105D17 was in the presence of 20 mM H2O2. Kinetic analysis for papaverine N-oxidation showed Km and Kcat values 302 ± 33 μM and 1.6 ± 0.08 min -1, respectively. The catalytic efficiency of CYP105D18 for papaverine N-oxidation was 0.31 sec- 1 μM-1. The structural model of CYP105D17 was generated using 7DLS as a template. Papaverine was buried in the complete hydrophobic core in CYP105D18. T239 was involved in the active site of CYP105D17 and Val231 was replaced with Ileu231 from CYP105D18. CYP105D18 was able to catalyze testosterone while CYP105D17 was unable despite the high structural similarity. Even with the high similarity with CYP105D18, CYP105D17 possesses low H2O2 tolerance and low catalytic efficiency towards papaverine N-oxidation. This provides insight into the biochemical properties, substrate preference, and detailed structural comparison of more closely related proteins.
목차
Abstract
1. Introduction
2. Materials and Methods
2.1 Cloning and overexpression of CYP105D17 and redox partners
2.2 Quantification of CYP105D17, and Redox Partners
2.3 Biochemical characterization of CYP105D17
2.4 Bioinformatics and molecular docking analysis
2.5 Product extraction, purification, and analysis
2.6 Determination of kinetic parameters
3. Results and Discussion
3.1 Characterization of CYP105D17
3.2 Kinetic analysis
3.3 Structural comparison of CYP105D17 with CYP105D18
4. Conclusions
Acknowledgement
References
저자
간행물 정보
발행기관
-
- 발행기관명
- 선문효정학술연구회 [Sun Moon Hyojeong Academy Society]
- 설립연도
- 2023
- 분야
- 복합학>학제간연구
- 소개
- Journal of Hyojeong Academia aims to serve as a global platform where researchers and scholars of various disciplines can contribute ideas for our sustainable global community of Co‐existence, Co‐prosperity, and Co‐righteousness. The journal is a multidisciplinary, open‐access, internationally peer‐reviewed academic journal, and it invites all areas of research conducted in the spirit of post materialism including studies centering on God, studies unifying religions and sciences, and studies on all aspects of Co‐existence, Co‐prosperity, and Co‐righteousness.
간행물
-
- 간행물명
- 선문효정학술연구회 학술대회 프로시딩
- 간기
- 반년간
- 수록기간
- 2023~2026
- 십진분류
- KDC 238 DDC 289
이 권호 내 다른 논문 / 선문효정학술연구회 학술대회 프로시딩 Proceedings of THE 1st INTERNATIONAL CONFERENCE OF HYOJEONG ACADEMY 2023
피인용수 : 0건 (자료제공 : 네이버학술정보)
함께 이용한 논문 이 논문을 다운로드한 분들이 이용한 다른 논문입니다.
출처 : 네이버학술정보
0개의 논문이 장바구니에 담겼습니다.