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MetaCyc Enzyme: L-carnitine dehydrogenase

Species: Xanthomonas translucens

Subunit composition of L-carnitine dehydrogenase = [L-carnitine dehydrogenase subunit]2

Summary:
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]

Gene-Reaction Schematic

Gene-Reaction Schematic


Enzymatic reaction of: L-carnitine dehydrogenase

Inferred from experiment

EC Number: 1.1.1.108

L-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.

In Pathways: γ-butyrobetaine degradation, L-carnitine degradation II

Cofactors or Prosthetic Groups: NAD+ [Mori88]

Inhibitors (Unknown Mechanism): Ag+ [Mori88], Ni2+ [Mori88], Hg2+ [Mori88], p-chloromercuribenzoate [Mori88], Li+ [Mori88], Ca2+ [Mori88], Mn2+ [Mori88], Co2+ [Mori88], Cu2+ [Mori88], Zn2+ [Mori88]Kinetic Parameters:
Substrate Km (μM) Citations
L-carnitine 10000.0 [Mori88]
NADH 40.0 [Mori88]
3-dehydrocarnitine 1710.0 [Mori88]
NAD+ 250.0 [Mori88]

pH(opt): 9.5 [Mori88]


References

Mori88: Mori, N., Kasugai, T., Kitamato, Y., Ichikawa, Y. (1988). "Purification and some properties of carnitine dehydrogenase from Xanthomonas translucens." Agric. Biol. Chem. 52, 249-250.


Report Errors or Provide Feedback
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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