2019年9月24日
Functional and Structural Analyses of trans C-Methyltransferase in Fungal Polyketide Biosynthesis.
Biochemistry
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- 巻
- 58
- 号
- 38
- 開始ページ
- 3933
- 終了ページ
- 3937
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1021/acs.biochem.9b00702
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.
- リンク情報
- ID情報
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- DOI : 10.1021/acs.biochem.9b00702
- ISSN : 0006-2960
- PubMed ID : 31486637