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 E-Mail IMAGE: (A) X-ray crystal structure of QhpG and schematic of crosslinked QhpC. The substrate QhpC is bound to the pocket formed by the catalytic domain, which includes the FAD cofactor and. view more  Credit: Osaka University Osaka, Japan - Investigators from the Institute of Scientific and Industrial Research at Osaka University, together with Hiroshima Institute of Technology, have announced the discovery of a new protein that allows an organism to conduct an initial and essential step in converting amino acid residues on a crosslinked polypeptide into an enzyme cofactor. This research may lead to a better understanding of the biochemistry underlying catalysis in cells.

Toshinori oozekiToshihide okajimaHiroshima institute of technologyNature communicationsIndustrial research at osaka universityOsaka universityDepartment of informationNational university corporationInstitute of scientificMinistry of educationIndustrial researchHiroshima instituteInnovative universitiesNature index innovationDesignated national university corporationWalk together