Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP(.).

ABSTRACT: Coenzyme A (CoA) plays pivotal roles in a variety of metabolic pathways in all organisms. The biosynthetic pathway of CoA is strictly regulated by feedback inhibition. In the hyperthermophilic archaeon Thermococcus kodakarensis, ketopantoate reductase (KPR), which catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate, is a target of feedback inhibition by CoA. The crystal structure of KPR from T. kodakarensis (Tk-KPR) complexed with CoA and 2-oxopantoate has previously been reported. The structure provided an explanation for the competitive inhibition mechanism. Here, further biochemical analyses of Tk-KPR and the crystal structure of Tk-KPR in complex with NADP(+) are reported. A mutational analysis implies that the residues in the binding pocket cooperatively contribute to the recog

SUBMITTER: Aikawa Y 

PROVIDER: S-EPMC4854564 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature