Structural highlights
Publication Abstract from PubMed
The biosynthesis of thioviridamide-like compounds has not been elucidated. Herein, we report that TvaF from the thioviridamide biosynthetic gene cluster is an FMN-dependent cysteine decarboxylase that transforms the C-terminal cysteine of precursor peptides into a thioenol motif and exhibits high substrate flexibility. We resolved the crystal structure of TvaF bound with FMN at 2.24 A resolution. Key residues for FMN binding and catalytic activity of TvaF have been identified and evaluated by mutagenesis studies.
Characterization of the FMN-Dependent Cysteine Decarboxylase from Thioviridamide Biosynthesis.,Lu J, Li J, Wu Y, Fang X, Zhu J, Wang H Org Lett. 2019 Jun 3. doi: 10.1021/acs.orglett.9b01531. PMID:31184189[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu J, Li J, Wu Y, Fang X, Zhu J, Wang H. Characterization of the FMN-Dependent Cysteine Decarboxylase from Thioviridamide Biosynthesis. Org Lett. 2019 Jun 3. doi: 10.1021/acs.orglett.9b01531. PMID:31184189 doi:http://dx.doi.org/10.1021/acs.orglett.9b01531
