Tartrate dehydrogenase, an enzyme with multiple catalytic activities

Title:Tartrate dehydrogenase, an enzyme with multiple catalytic activities

Volume: 7 Issue: 5

Author(s): Peter A. Tipton

Affiliation:

Abstract: Tartrate dehydrogenase is found in a variety of microorganisms and operates as part of a pathway by which tartrate is converted into D-glycerate, providing entry for the carbon into primary metabolic pathways. Tartrate dehydrogenase was isolated from Pseudomonas putida grown on (+)-tartrate as the sole carbon source and characterized in the 1960's [l]. More recently, TDH was isolated from the same bacterial strain and its gene was cloned [2]. The properties of that enzyme are similar in several respects to the TDH described in the earlier work, but differ in several key features as well. It is difficult to know whether the discrepancies arose because different enzymes were isolated and studied or whether mutations occurred which changed the functional properties of the enzyme. A number of workers have described enzymes which tum over tartrate [3,4], but this article will concentrate on the recently isolated P. putida TDH, which exhibited several fascinating mechanistic features.

Cite this article as:

Tipton A. Peter, Tartrate dehydrogenase, an enzyme with multiple catalytic activities, Protein & Peptide Letters 2000; 7 (5) . https://dx.doi.org/10.2174/092986650705221207143232

DOI https://dx.doi.org/10.2174/092986650705221207143232	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305