X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate.

ABSTRACT: 1-Deoxy-d-xylulose 5-phosphate synthase (DXPS) uses thiamine diphosphate (ThDP) to convert pyruvate and d-glyceraldehyde 3-phosphate (d-GAP) into 1-deoxy-d-xylulose 5-phosphate (DXP), an essential bacterial metabolite. DXP is not utilized by humans; hence, DXPS has been an attractive antibacterial target. Here, we investigate DXPS from Deinococcus radiodurans (DrDXPS), showing that it has similar kinetic parameters K_m^d-GAP and K_m^pyruvate (54 ± 3 and 11 ± 1 μm, respectively) and comparable catalytic activity (k_cat = 45 ± 2 min^-1) with previously studied bacterial DXPS enzymes and employing it to obtain missing structural data on this enzyme family. In particular, we have determined crystallo

SUBMITTER: Chen PY 

PROVIDER: S-EPMC6699841 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature