1.4.1.9: leucine dehydrogenase
This is an abbreviated version!
For detailed information about leucine dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.9
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1.4.1.9
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sphaericus
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l-valine
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synthesis
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l-isoleucine
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l-2-aminobutyric
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l-tert-leucine
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intermedius
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thermoactinomyces
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l-threonine
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analysis
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space-time
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3.5.1.5
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trimethylpyruvate
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alpha-ketoisocaproate
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lysinibacillus
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drug development
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biotechnology
- 1.4.1.9
- sphaericus
- l-valine
- synthesis
- l-isoleucine
-
l-2-aminobutyric
- l-tert-leucine
- intermedius
-
thermoactinomyces
- l-threonine
- analysis
-
space-time
-
3.5.1.5
- trimethylpyruvate
- alpha-ketoisocaproate
-
lysinibacillus
- drug development
- biotechnology
Reaction
Synonyms
BCD, dehydrogenase, leucine, L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, LeuDH
ECTree
1.4.1.9 leucine dehydrogenaseAdvanced search results
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results (Temperature Stability
Temperature Stability on EC 1.4.1.9 - leucine dehydrogenase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
30
40
50
54
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pH 7.0-9.5, 60 min, chimeric enzyme consisting of an amino-terminal domain of phenylalanine dehydrogenase and a carboxy-terminal domain of leucine dehydrogenase, stable
55
58
60
65
70
75
80
83
additional information
30
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10 mM potassium phosphate buffer, pH 7.4, 0.01% 2-mercaptoethanol, 1 mM EDTA, 1.0 M NaCl, stable for more than 6 months
58
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pH 7.0-9.5, 60 min, chimeric enzyme consisting of an amino-terminal domain of phenylalanine dehydrogenase and a carboxy-terminal domain of leucine dehydrogenase, loss of activity
80
the residual activity of NAD+-bound form is approximately three times higher than that of the apo form after incubation at 80°C
additional information
A0A0K2HC96
binding of NAD+ ioncreases thermostability. The interaction between NAD+ and Ser147 transduces a series of conformational changes that increases intermolecular interactions in the oligomer interface
additional information
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binding of NAD+ ioncreases thermostability. The interaction between NAD+ and Ser147 transduces a series of conformational changes that increases intermolecular interactions in the oligomer interface
additional information
non-conserved residues Ala94 Tyr127, and the C-terminal region, are crucial for oligomeric thermostability
additional information
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non-conserved residues Ala94 Tyr127, and the C-terminal region, are crucial for oligomeric thermostability
additional information
A0A0K2HC96
residue Ala94 undergoes a hydrophobic interaction with Ala349 in a neighboring protomer. The side chain of Tyr127 undergoes hydrophobic interaction with Ile136 in the same subunit, and an electrostatic interaction with Arg364 in a neighboring protomer. Hydrophobic packing between protomers via domain I contributes to the high thermostability
additional information
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residue Ala94 undergoes a hydrophobic interaction with Ala349 in a neighboring protomer. The side chain of Tyr127 undergoes hydrophobic interaction with Ile136 in the same subunit, and an electrostatic interaction with Arg364 in a neighboring protomer. Hydrophobic packing between protomers via domain I contributes to the high thermostability
