Species: Xanthomonas translucens
Subunit composition of L-carnitine dehydrogenase = [L-carnitine dehydrogenase subunit]2
L-carnitine dehydrogenase has been purified from Xanthomonas translucnes [Mori88]. The enzyme was specific to the L-carnitine enantiomer, and did not recognize D-carnitine or any other carnitine analogs such as choline and glycine betaine. It requires NAD+, and does not accept NADP+. The optimal pH was 9.5 for the oxidation reaction, and 6.5 for the reduction reaction.
Molecular Weight of Polypeptide: 37 kD (experimental) [Mori88]
Molecular Weight of Multimer: 74 kD (experimental) [Mori88]
Enzymatic reaction of: L-carnitine dehydrogenase
EC Number: 18.104.22.168L-carnitine + NAD+ ⇄ 3-dehydrocarnitine + 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.Ag+ [Mori88], Ni2+ [Mori88], Hg2+ [Mori88], p-chloromercuribenzoate [Mori88], Li+ [Mori88], Ca2+ [Mori88], Mn2+ [Mori88], Co2+ [Mori88], Cu2+ [Mori88], Zn2+ [Mori88]Kinetic Parameters:
pH(opt): 9.5 [Mori88]
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