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]
Enzymatic reaction of: tartrate dehydrogenase
EC Number: 18.104.22.168L-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:
pH(opt): 8.5 [Kohn68]
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