5Z9J

Identification of the functions of unusual cytochrome p450-like monooxygenases involved in microbial secondary metablism

Summary for 5Z9J

• Entry DOI: 10.2210/pdb5z9j/pdb
• Descriptor: Putative P450-like enzyme, PROTOPORPHYRIN IX CONTAINING FE, TRIS(HYDROXYETHYL)AMINOMETHANE, ... (4 entities in total)
• Functional Keywords: cytochrome p450, monooxygenase, oxidoreductase
• Biological source: Streptomyces himastatinicus ATCC 53653
• Total number of polymer chains: 4
• Total formula weight: 181735.27

Authors

Lu, M.,Lin, L.,Zhang, C.,Chen, Y. (deposition date: 2018-02-03, release date: 2019-02-06, Last modification date: 2024-03-27)

Primary citation

Zhang, C.,Lu, M.,Lin, L.,Huang, Z.,Zhang, R.,Wu, X.,Chen, Y.
Riboflavin Is Directly Involved in the N-Dealkylation Catalyzed by Bacterial Cytochrome P450 Monooxygenases.
Chembiochem, 2020

PubMed Abstract: Like a vast number of enzymes in nature, bacterial cytochrome P450 monooxygenases require an activated form of flavin as a cofactor for catalytic activity. Riboflavin is the precursor of FAD and FMN that serves as indispensable cofactor for flavoenzymes. In contrast to previous notions, herein we describe the identification of an electron-transfer process that is directly mediated by riboflavin for N-dealkylation by bacterial P450 monooxygenases. The electron relay from NADPH to riboflavin and then via activated oxygen to heme was proposed based on a combination of X-ray crystallography, molecular modeling and molecular dynamics simulation, site-directed mutagenesis and biochemical analysis of representative bacterial P450 monooxygenases. This study provides new insights into the electron transfer mechanism in bacterial P450 enzyme catalysis and likely in yeasts, fungi, plants and mammals.

PubMed: 32243060
DOI: 10.1002/cbic.202000071

Experimental method

X-RAY DIFFRACTION (2 Å)