Crystal structure of AlpK: An essential monooxygenase involved in the biosynthesis of kinamycin

Autor:	Huanhuan Li, Keqing Fan, Jun Li, Yingfang Liu, Wenpeng Wang
Rok vydání:	2019
Předmět:	0301 basic medicine Models Molecular Stereochemistry Protein Conformation Biophysics Kinamycin Crystal structure Crystallography X-Ray Biochemistry Mixed Function Oxygenases 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Biosynthesis Bacterial Proteins Oxidoreductase Amino Acid Sequence Molecular Biology chemistry.chemical_classification Chemistry Quinones Cell Biology Monooxygenase Streptomyces 030104 developmental biology 030220 oncology & carcinogenesis Protein Multimerization Sequence Alignment
Zdroj:	Biochemical and biophysical research communications. 510(4)
ISSN:	1090-2104
Popis:	AlpK is an essential monooxygenase involved in the biosynthesis of kinamycin. It catalyzes the C5-hyfroxylattion of the crucial benzo[b]-fluorence intermediate in kinamycin synthesis. However, the structure and mechanism of AlpK is unclear. Here, we report the first structure of AlpK in complex with FAD. Our structure sheds light on the catalytic mechanism of AlpK.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c06e8ca6ce35fb53cbd9fb618ef7c25 https://pubmed.ncbi.nlm.nih.gov/30739782 Zobrazit plný text záznamu Full Text from ScienceDirect