Tauropine dehydrogenase

Oxidoreductase enzyme From Wikipedia, the free encyclopedia

In enzymology, tauropine dehydrogenase (EC 1.5.1.23) is an enzyme that catalyzes the oxidoreduction reaction :

2D representation of the chemical structure of Q27101919.
tauropine
+ NAD+
 
 
H2O
H+
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
H2O
H+
 
+ NADH +
 

The three substrates of this enzyme are tauropine, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are taurine, reduced NADH, pyruvic acid, and a proton.[1][2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming). This enzyme is also called 2-N-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming).

References

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