1.4.1.21: aspartate dehydrogenase
This is an abbreviated version!
For detailed information about aspartate dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.21
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1.4.1.21
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analysis
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synthesis
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oxaloacetate
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dehydrogenases
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thermotoga
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maritima
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dehydrogenation
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fulgidus
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palustris
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archaeoglobus
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rhodopseudomonas
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eutropha
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ammonia-lyase
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d-aspartate
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electrocardiogram
- 1.4.1.21
- analysis
- synthesis
- oxaloacetate
- dehydrogenases
-
thermotoga
- maritima
-
dehydrogenation
- fulgidus
- palustris
-
archaeoglobus
-
rhodopseudomonas
- eutropha
-
ammonia-lyase
- d-aspartate
-
electrocardiogram
Reaction
Synonyms
AspDH, L-aspartate dehydrogenase, L-aspartate:NAD(P)+ oxidoreductase (deaminating), L-aspDH, NAD-dependent aspartate dehydrogenase, NADH2-dependent aspartate dehydrogenase, NADP+-dependent aspartate dehydrogenase, nadX
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General Information
General Information on EC 1.4.1.21 - aspartate dehydrogenase
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evolution
metabolism
physiological function
additional information
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L-aspartate dehydrogenase is a rare member of amino acid dehydrogenase superfamily
evolution
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L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
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L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
-
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
-
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
-
-
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
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involvement of L-AspDH in NAD biosynthesis, overview
physiological function
-
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
-
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
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the amination activity of the enzyme may be important for the fixation of inorganic nitrogen
physiological function
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the amination activity of the enzyme may be important for the fixation of inorganic nitrogen
physiological function
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not. The AspDH cluster might be involved in the biosynthesis of poly-3-hydroxyalkanoates
physiological function
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involvement of L-AspDH in NAD biosynthesis, overview
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physiological function
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involvement of L-AspDH in NAD biosynthesis, overview
-
physiological function
-
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not. The AspDH cluster might be involved in the biosynthesis of poly-3-hydroxyalkanoates
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physiological function
-
involvement of L-AspDH in NAD biosynthesis, overview
-
-
three-dimensional structure comparisons, overview
additional information
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three-dimensional structure comparisons, overview
additional information
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three-dimensional structure comparisons, overview
additional information
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three-dimensional structure comparisons, overview
additional information
three-dimensional structure comparisons, overview
additional information
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three-dimensional structure comparisons, overview
-
additional information
-
three-dimensional structure comparisons, overview
-
additional information
-
three-dimensional structure comparisons, overview
-