Chemical mechanism of 6-phosphogluconate dehydrogenase via kinetic studies and site­ directed mutagenesis

Title:Chemical mechanism of 6-phosphogluconate dehydrogenase via kinetic studies and site­ directed mutagenesis

Volume: 7 Issue: 5

Author(s): Lei Zhang and Paul F. Cook*

Affiliation:

• Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019

Abstract: 6-Phosphogluconate dehydrogenase catal)jzes the metal ion-independent oxidative decarboxylation of 6- phosphogluconate (6PG). The enzyme catalyzes a reaction in which 6PG is first oxidized at the 3-position, then decarboxylated to the 1,2-enediol of Ru5P , and then tautomerized to give the Ru5P ketone product. In the reaction, Kl83 acts as a general base, general acid, shuttling a proton between the 3-hydroxyl and itself, and E190 acts as a general acid to protonate C1 of the enediol intermediate in the tautomerization step.

Cite this article as:

Zhang Lei and Cook F. Paul*, Chemical mechanism of 6-phosphogluconate dehydrogenase via kinetic studies and site­ directed mutagenesis, Protein & Peptide Letters 2000; 7 (5) . https://dx.doi.org/10.2174/092986650705221207143039

DOI https://dx.doi.org/10.2174/092986650705221207143039	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305