Mechanistic Studies on the Single-Turnover Yeast Thiamin Pyrimidine Synthase: Characterization of the Inactive Enzyme. Academic Article

abstract

• The eukaryotic thiamin pyrimidine synthase, THI5p, has been identified as a suicidal/single-turnover enzyme that catalyzes the conversion of its active site histidine and lysine-bound pyridoxal phosphate (PLP) to the thiamin pyrimidine (HMP-P). Here we identify the histidine and PLP fragments using bottom-up proteomics and LC-MS analysis. We also identify the active form of the iron cofactor and quantitate the oxygen requirement of the THI5p reaction. This information is integrated into a mechanistic proposal for this remarkable reaction.

authors

• Begley, Tadhg

published proceedings

• J Am Chem Soc

altmetric score

• 13.45

author list (cited authors)

• Lai, R., Mondal, A., Fedoseyenko, D., & Begley, T. P.

citation count

• 1

complete list of authors

• Lai, Rung-Yi||Mondal, Anushree||Fedoseyenko, Dmytro||Begley, Tadhg P

publication date

• January 2022

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Histidine
• Humans
• Pyridoxal Phosphate
• Pyrimidines
• Saccharomyces Cerevisiae
• Thiamine

PubMed Central ID

• 35675507

Digital Object Identifier (DOI)

• 10.1021/jacs.2c03322

start page

• 10711

end page

• 10717

volume

• 144

issue

• 24

URL

• http://dx.doi.org/10.1021/jacs.2c03322