Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases

Research output: Contribution to journalReview articlepeer-review

43 Scopus citations


D-3-Phosphoglycerate dehydrogenases (PGDH) exist with at least three different structural motifs and the enzymes from different species display distinctly different mechanisms. In many species, particularly bacteria, the catalytic activity is regulated allosterically through binding of l-serine to a distinct structural domain, termed the ACT domain. Some species, such as Mycobacterium tuberculosis, contain an additional domain, called the "allosteric substrate binding" or ASB domain, that functions as a co-domain in the regulation of catalytic activity. That is, both substrate and effector function synergistically in the regulation of activity to give the enzyme some interesting properties that may have physiological relevance for the persistent state of tuberculosis. Both enzymes function through a V-type regulatory mechanism and, in the Escherichia coli enzyme, it has been demonstrated that this results from a dead-end complex that decreases the concentration of active species rather than a decrease in the velocity of the active species. This review compares and contrasts what we know about these enzymes and provides additional insight into their mechanism of allosteric regulation.

Original languageEnglish
Pages (from-to)175-185
Number of pages11
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Mar 15 2012


  • ACT domain
  • ASB domain
  • Allosteric
  • Dehydrogenase
  • Phosphoglycerate
  • Serine


Dive into the research topics of 'Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases'. Together they form a unique fingerprint.

Cite this