Biophysical Characterization of a Novel Phosphopentomutase from the Hyperthermophilic Archaeon Thermococcus kodakarensis.

ABSTRACT: Phosphopentomutases catalyze the isomerization of ribose 1-phosphate and ribose 5-phosphate. Thermococcus kodakarensis, a hyperthermophilic archaeon, harbors a novel enzyme (PPM_Tk) that exhibits high homology with phosphohexomutases but has no significant phosphohexomutase activity. Instead, PPM_Tk catalyzes the interconversion of ribose 1-phosphate and ribose 5-phosphate. Here, we report biophysical analysis, crystallization, and three-dimensional structure determination of PPM_Tk by X-ray diffraction at 2.39 Å resolution. The solved structure revealed a novel catalytic motif, unique to PPM_Tk, which makes this enzyme distinct from the homologous counterparts. We postulate that this novel catalytic motif may enabl

SUBMITTER: Naz Z 

PROVIDER: S-EPMC11641776 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature