Functional and Structural Analyses of trans C-Methyltransferase in Fungal Polyketide Biosynthesis

التفاصيل البيبلوغرافية
العنوان: Functional and Structural Analyses of trans C-Methyltransferase in Fungal Polyketide Biosynthesis
المؤلفون: Yuta Tsunematsu, Takuma Matsushita, Yi Tang, Shinji Kishimoto, Kodai Hara, Kenji Watanabe, Hiroshi Hashimoto
المصدر: Biochemistry. 58:3933-3937
بيانات النشر: American Chemical Society (ACS), 2019.
سنة النشر: 2019
مصطلحات موضوعية: chemistry.chemical_classification, 0303 health sciences, Chemistry, Stereochemistry, 030302 biochemistry & molecular biology, Mutant, Substrate (chemistry), Methylation, Biochemistry, 03 medical and health sciences, Polyketide, chemistry.chemical_compound, Enzyme, Biosynthesis, Oxidoreductase, Secondary metabolism
الوصف: Biosynthesis of certain fungal polyketide-peptide synthetases involves C-methyltransferase activity that adds one or more S-adenosyl-l-methionine-derived methyl groups to the carbon framework. The previously reported PsoF-MT, the stand-alone C-methyltransferase (MT) from the pseurotin biosynthetic pathway that exists as a domain within a trifunctional didomain enzyme PsoF, was characterized crystallographically and kinetically using mutants with substrate analogs to understand how a trans-acting C-MT works and compare it to known polyketide synthase-associated C-MTs. This study identified key active-site residues involved in catalysis and substrate recognition, which led us to propose the mechanism of C-methylation and substrate specificity determinants in PsoF-MT.
تدمد: 1520-4995
0006-2960
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::e7df32c61915ac49110a168018e13649
https://doi.org/10.1021/acs.biochem.9b00702
حقوق: CLOSED
رقم الأكسشن: edsair.doi...........e7df32c61915ac49110a168018e13649
قاعدة البيانات: OpenAIRE