ChemBio e-seminar by Prof. Ken Yokoyama
Event details
| Date | 25.10.2022 |
| Hour | 16:15 › 17:15 |
| Speaker | Prof. Ken Yokoyama Duke University, North Carolina, USA |
| Location | Online |
| Category | Conferences - Seminars |
| Event Language | English |
Title: Mechanism of radical-mediated C-C bond formation in molybdenum cofactor biosynthesis and human disease
Abstract:
Molybdenum cofactor (Moco) is a redox-active enzyme cofactor found in almost all organisms from all kingdoms of life. Unlike many cofactors, Moco cannot be taken up as a nutrient and requires de novo biosynthesis. Thus, Moco biosynthesis is an essential process for many organisms including humans and pathogenic bacteria. In humans, Moco is essential for the healthy development of the brain and genetic mutations in these biosynthetic enzymes cause a fatal metabolic disorder, Moco deficiency. During biosynthesis, the pterin backbone structure of Moco is constructed from guanosine 5’-triphosphate (GTP) via a unique rearrangement. In the past decade, we have discovered the functions of two enzymes (MoaA and MoaC) responsible for this transformation and have made significant progress toward understanding their catalytic mechanisms and how their mutations cause human disease. In this seminar, I will present some of the recent progress we have made in the past ~5 years.
Speaker's biography:
Prof. Yokoyama received Ph.D. from the Tokyo Institute of Technology by studying the mechanism of biosynthesis of aminoglycoside antibiotics and performed a postdoc study with Prof. JoAnne Stubbe at MIT, where he studied the mechanism of long-range radical propagation in ribonucleotide reductase (RNR) using unnatural tyrosine analogs to trap pathway radical species. As an independent researcher at Duke University, Prof. Yokoyama has been studying the biosynthesis of natural products and cofactors that involve unique metalloenzymes including radical SAM enzymes, as well as the mechanism of fungal cell wall biosynthesis.
Lab website: http://sites.duke.edu/yokoyamalab/
Abstract:
Molybdenum cofactor (Moco) is a redox-active enzyme cofactor found in almost all organisms from all kingdoms of life. Unlike many cofactors, Moco cannot be taken up as a nutrient and requires de novo biosynthesis. Thus, Moco biosynthesis is an essential process for many organisms including humans and pathogenic bacteria. In humans, Moco is essential for the healthy development of the brain and genetic mutations in these biosynthetic enzymes cause a fatal metabolic disorder, Moco deficiency. During biosynthesis, the pterin backbone structure of Moco is constructed from guanosine 5’-triphosphate (GTP) via a unique rearrangement. In the past decade, we have discovered the functions of two enzymes (MoaA and MoaC) responsible for this transformation and have made significant progress toward understanding their catalytic mechanisms and how their mutations cause human disease. In this seminar, I will present some of the recent progress we have made in the past ~5 years.
Speaker's biography:
Prof. Yokoyama received Ph.D. from the Tokyo Institute of Technology by studying the mechanism of biosynthesis of aminoglycoside antibiotics and performed a postdoc study with Prof. JoAnne Stubbe at MIT, where he studied the mechanism of long-range radical propagation in ribonucleotide reductase (RNR) using unnatural tyrosine analogs to trap pathway radical species. As an independent researcher at Duke University, Prof. Yokoyama has been studying the biosynthesis of natural products and cofactors that involve unique metalloenzymes including radical SAM enzymes, as well as the mechanism of fungal cell wall biosynthesis.
Lab website: http://sites.duke.edu/yokoyamalab/
Practical information
- Informed public
- Free