Literature summary for 1.1.1.254 extracted from

Setyahida, S.; Ueyama, T.; Arimoto, T.; Mori, N.; Kitamoto, Y.
Purification and properties of a new enzyme, D-carnitine dehydrogenase from Agrobacterium sp. 525a (1997), Biosci. Biotechnol. Biochem., 61, 1055-1058.

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Inhibitors

Inhibitors	Comment	Organism	Structure
5,5'-dithiobis(2-nitrobenzoate)	D-carnitine dehydrogenase, 1 mM, complete inactivation	Agrobacterium sp. 525a
Ag+	D-carnitine dehydrogenase, 1 mM, complete inactivation	Agrobacterium sp. 525a
Cu2+	D-carnitine dehydrogenase, 1 mM, complete inactivation	Agrobacterium sp. 525a
Hg2+	D-carnitine dehydrogenase, 1 mM, complete inactivation	Agrobacterium sp. 525a
N-ethylmaleimide	D-carnitine dehydrogenase, 1 mM, 77% inactivation after 3 min	Agrobacterium sp. 525a
p-chloromercuribenzoate	D-carnitine dehydrogenase, 0.1 mM, complete inactivation	Agrobacterium sp. 525a

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.06	-	NADH	D-carnitine dehydrogenase	Agrobacterium sp. 525a
0.07	-	NAD+	D-carnitine dehydrogenase	Agrobacterium sp. 525a
0.8	-	3-dehydrocarnitine	D-carnitine dehydrogenase	Agrobacterium sp. 525a
3.1	-	D-carnitine	D-carnitine dehydrogenase	Agrobacterium sp. 525a

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	D-carnitine dehydrogenase, 0.5 mM, 17% increase in activity, 1.0 mM 30% increase in activity, 5.0 mM, 35% increase in activity	Agrobacterium sp. 525a

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
29000	-	3 * 29000, D-carnitine dehydrogenase, SDS-PAGE	Agrobacterium sp. 525a
86000	-	gel filtration, D-carnitine dehydrogenase	Agrobacterium sp. 525a

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+	Agrobacterium sp. 525a	-	3-dehydrocarnitine + NADH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Agrobacterium sp. 525a	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
DEAE-Toyopearl, ammonium sulfate, Sephadex G-75, 5'-AMP-Sepharose 4B, Mono Q, TSK-gel G3000 SW, D-carnitine dehydrogenase	Agrobacterium sp. 525a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
30.7	-	D-carnitine dehydrogenase	Agrobacterium sp. 525a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+	-	Agrobacterium sp. 525a	3-dehydrocarnitine + NADH + H+	-	r
(S)-3-hydroxy-4-trimethylaminobutyrate + NAD+	D-carnitine dehydrogenase	Agrobacterium sp. 525a	3-dehydrocarnitine + NADH + H+	-	r
3-hydroxy-2-butanone + NAD+	enzyme specific for D-carnitine	Agrobacterium sp. 525a	2,3-butandione + NADH	-	?
DL-4-amino-3-hydroxy-n-butyrate + NAD+	D-carnitine dehydrogenase	Agrobacterium sp. 525a	DL-4-amino-3-keto-n-butyrate + NADH	-	?

Subunits

Subunits	Comment	Organism
trimer	3 * 29000, D-carnitine dehydrogenase, SDS-PAGE	Agrobacterium sp. 525a

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
40	-	D-carnitine dehydrogenase	Agrobacterium sp. 525a

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
40	-	D-carnitine dehydrogenase, enzyme is rapidly inactivated above 40°C	Agrobacterium sp. 525a

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	7	D-carnitine dehydrogenase, reduction of 3-dehydrocarnitine	Agrobacterium sp. 525a
9.3	-	D-carnitine dehydrogenase, oxidation of D-carnitine	Agrobacterium sp. 525a

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
6.5	9	D-carnitine dehydrogenase	Agrobacterium sp. 525a

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Agrobacterium sp. 525a

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Release 2023.1 (January 2023)