MetaCyc Enzyme: tartrate dehydrogenase

Species: Pseudomonas putida

Subunit composition of tartrate dehydrogenase = [tartrate dehydrogenase subunit]4

tartrate dehydrogenase has been purified and crystallized from Pseudomonas putida. The enzyme catalyzes the reversible, NAD-linked oxidation of meso-tartrate and of L-tartrate to 2-hydroxy-3-oxosuccinate. D-tartrate was not a substrate. (S)-malate and (R)-malate were inactive as either substrates or inhibitors, suggesting this enzyme os different from another Pseudomonas putida enzyme that is able to catalyze this reaction (see tartrate dehydrogenase/decarboxylase).

The enzyme requires Mn2+ ions and one of several monovalent cations for activity. Both qualitative and quantitative differences were found in the requirement for monovalent cation, depending on the nature of the substrate [Kohn68].

Molecular Weight of Polypeptide: 36.8 kD (experimental) [Kohn68]

Molecular Weight of Multimer: 145 kD (experimental) [Kohn68]

Gene-Reaction Schematic

Gene-Reaction Schematic

Created 31-Jan-2007 by Caspi R, SRI International

Enzymatic reaction of: tartrate dehydrogenase

Inferred from experiment

EC Number:

L-tartrate + NAD+ ⇄ 2-hydroxy-3-oxosuccinate + NADH + H+

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Activators (Allosteric): Mn2+ [Kohn68], K+ [Kohn68], Rb+ [Kohn68] Inhibitors (Competitive): dihydroxyfumarate [Kohn68]Kinetic Parameters:
Substrate Km (μM) Citations
L-tartrate 55000.0 [Kohn68]
NAD+ 90.0 [Kohn68]

pH(opt): 8.5 [Kohn68]


Kohn68: Kohn LD, Packman PM, Allen RH, Jakoby WB (1968). "Tartaric acid metabolism. V. Crystalline tartrate dehydrogenase." J Biol Chem 243(10);2479-85. PMID: 4297261

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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