PgdA

PgdA, also known as phosphogluconate dehydrogenase, is an enzyme found in many organisms, playing a crucial role in metabolic pathways. It is a key component of the pentose phosphate pathway (PPP), a vital cellular process that generates NADPH and produces precursor molecules for nucleotide and amino acid biosynthesis. Specifically, PgdA catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose-5-phosphate, releasing carbon dioxide and NADPH in the process.

In bacteria, PgdA is essential for the efficient operation of the PPP, which is particularly important under conditions of oxidative stress and during rapid cell growth. The NADPH produced by PgdA is used as a reducing agent in various biosynthetic reactions and for the detoxification of reactive oxygen species. Mutations or deficiencies in PgdA can therefore have significant consequences for bacterial survival and virulence.

In eukaryotes, the enzyme is also present and contributes to the PPP. The regulation of PgdA activity is subject to cellular needs, and its expression levels can be modulated in response to metabolic cues. The structural features of PgdA, including its active site, have been studied to understand its catalytic mechanism and to explore potential therapeutic targets, particularly in the context of diseases where metabolic dysregulation is a factor.