المؤلفون: Kohler, Amanda C, Mills, Matthew JL, Adams, Paul D, Simmons, Blake A, Sale, Kenneth L

المصدر: Proceedings of the National Academy of Sciences of the United States of America. 114(16)

مصطلحات موضوعية: Biochemistry and Cell Biology, Chemical Sciences, Biological Sciences, Catalysis, Crystallography, X-Ray, Kinetics, Metabolic Networks and Pathways, Oxidoreductases, O-Demethylating, Protein Conformation, Sphingomonas, Tyrosine, demethylase, biocatalysis, aryl metabolism, tetrahydrofolate, lignin

URL الوصول: https://escholarship.org/uc/item/231535vn

المؤلفون: Kenneth L. Sale, Matthew J. L. Mills, Paul D. Adams, Blake A. Simmons, Amanda C. Kohler

المصدر: Kohler, AC; Mills, MJL; Adams, PD; Simmons, BA; & Sale, KL. (2017). Structure of aryl O-demethylase offers molecular insight into a catalytic tyrosine-dependent mechanism. Proceedings of the National Academy of Sciences of the United States of America, 114(16), E3205-E3214. doi: 10.1073/pnas.1619263114. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/231535vn
Proceedings of the National Academy of Sciences of the United States of America, vol 114, iss 16

مصطلحات موضوعية: 0301 basic medicine, Sphingomonas paucimobilis, Oxidoreductases, O-Demethylating, biocatalysis, Stereochemistry, Protein Conformation, lignin, demethylase, Crystallography, X-Ray, Sphingomonas, Catalysis, 03 medical and health sciences, Synthetic biology, chemistry.chemical_compound, Transferase, Demethylation, Crystallography, Multidisciplinary, biology, Chemistry, Aryl, biology.organism_classification, tetrahydrofolate, O-Demethylating, Metabolic pathway, Kinetics, 030104 developmental biology, PNAS Plus, Biocatalysis, X-Ray, biology.protein, Demethylase, Tyrosine, Oxidoreductases, aryl metabolism, Metabolic Networks and Pathways

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13a9a558e6c038fd049fcc346a1f13b9
https://europepmc.org/articles/PMC5402402/