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Literature summary for 1.1.1.108 extracted from

  • Eltayeb, M.M.; Arima, J.; Mori, N.
    Alanine-scanning mutation approach for classification of the roles of conserved residues in the activity and substrate affinity of L-carnitine dehydrogenase (2014), Biotechnol. Lett., 36, 309-317.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Xanthomonas translucens

Protein Variants

Protein Variants Comment Organism
D298A inactive Xanthomonas translucens
E185A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
E196A inactive Xanthomonas translucens
E201A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
F189A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
F234A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
F249A inactive Xanthomonas translucens
F253A inactive Xanthomonas translucens
M231A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
M246A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
N144A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
Q252A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
R193A inactive Xanthomonas translucens
R200A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
R297A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
S117A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
S120A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
T262A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
W199A inactive Xanthomonas translucens
W228A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
W261A inactive Xanthomonas translucens
Y147A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens
Y237A the mutant shows reduced activity compared to the wild type enzyme Xanthomonas translucens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
NAD+ mutant enzyme W228A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.08
-
NAD+ mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.09
-
NAD+ mutant enzyme F234A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.09
-
NAD+ mutant enzyme M231A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.26
-
NAD+ mutant enzyme R297A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.31
-
NAD+ wild type enzyme, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.35
-
NAD+ mutant enzyme N144A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.35
-
NAD+ mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.36
-
NAD+ mutant enzyme E185A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.39
-
NAD+ mutant enzyme M246A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.39
-
NAD+ mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.4
-
NAD+ mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.53
-
NAD+ mutant enzyme T262A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
1.04
-
NAD+ mutant enzyme F189A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
2.25
-
NAD+ mutant enzyme R200A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
3.76
-
NAD+ mutant enzyme S117A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
9.66
-
NAD+ mutant enzyme S120A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
10.2
-
carnitine wild type enzyme, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
40.4
-
carnitine mutant enzyme E185A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
89.1
-
carnitine mutant enzyme T262A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
101.4
-
carnitine mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
164
-
carnitine mutant enzyme N144A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
205.7
-
carnitine mutant enzyme F189A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
284
-
carnitine mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
307.6
-
carnitine mutant enzyme S117A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
308.8
-
carnitine mutant enzyme M231A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
331.9
-
carnitine mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
336.2
-
carnitine mutant enzyme M246A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
667
-
carnitine mutant enzyme S120A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
767.1
-
carnitine mutant enzyme R200A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
799.7
-
carnitine mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
830.7
-
carnitine mutant enzyme R297A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
1010
-
carnitine mutant enzyme W228A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
1056
-
carnitine mutant enzyme F234A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
2000
-
carnitine Km above 2000 mM, mutant enzyme D298A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
2000
-
carnitine Km above 2000 mM, mutant enzyme F249A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
2000
-
carnitine Km above 2000 mM, mutant enzyme F253A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
2000
-
carnitine Km above 2000 mM, mutant enzyme W261A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
carnitine + NAD+ Xanthomonas translucens
-
3-dehydrocarnitine + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Xanthomonas translucens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
amylose resin column chromatography, and Superdex 200 gel filtration Xanthomonas translucens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carnitine + NAD+
-
Xanthomonas translucens 3-dehydrocarnitine + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
Cdh
-
Xanthomonas translucens
L-carnitine dehydrogenase
-
Xanthomonas translucens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.001
-
carnitine mutant enzyme F234A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.001
-
carnitine mutant enzyme R200A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.001
-
carnitine mutant enzyme S120A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.003
-
carnitine mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.007
-
carnitine mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.008
-
carnitine mutant enzyme W228A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.009
-
carnitine mutant enzyme F189A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.01
-
carnitine mutant enzyme M231A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.013
-
carnitine mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.016
-
carnitine mutant enzyme R297A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.019
-
carnitine mutant enzyme S117A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.044
-
carnitine mutant enzyme M246A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.068
-
carnitine mutant enzyme T262A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.079
-
carnitine mutant enzyme N144A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.157
-
carnitine mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
0.22
-
carnitine mutant enzyme E185A, at pH 9.5, temperature not specified in the publication Xanthomonas translucens
1.279
-
carnitine wild type enzyme, at pH 9.5, temperature not specified in the publication Xanthomonas translucens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Xanthomonas translucens