2-dehydropantoate 2-reductase

2-dehydropantoate 2-reductase is an enzyme classified under EC 1.1.1.169 that catalyzes the NADPH-dependent reduction of 2-dehydropantoate (ketopantoic acid) to (R)-pantoate, a crucial step in the biosynthetic pathway for pantothenate (vitamin B5) and subsequently coenzyme A[1][4][7][9]. This enzyme belongs to the oxidoreductase family, acting on the CH-OH group of donors with NADP+ as acceptor. It is essential for the growth and survival of many bacteria, making it a validated pharmacological target for the development of new antimicrobial therapies[3][5]. The enzyme is found in a variety of organisms, including pathogens like Mycobacterium tuberculosis, and is absent or substantially different in mammals, making it an attractive drug target for selective antibacterial action[3][5][7]. Multiple crystal structures have been solved, providing insight for rational inhibitor design[1][3]. Its systematic name is (R)-pantoate:NADP+ 2-oxidoreductase, and it is known by several alternative names referring to its substrate or the product of the reaction[1][4][8]. There are no clinically used inhibitors or drugs specifically documented for this enzyme in current databases.

Other names

2-oxopantoate reductase2-ketopantoate reductase2-ketopantoic acid reductaseketopantoate reductaseKPA reductase

Competitive inhibition of ketopantoate reductase active site impairs pantothenate and CoA biosynthesis, leading to inhibition of bacterial growth