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Literature summary for 1.4.1.8 extracted from

  • Kagan, Z.S.; Polyakov, V.A.; Kretovich, V.L.
    Soluble valine dehydrogenase from roots of plant seedlings (1968), Biokhimiya, 33, 89-96.
No PubMed abstract available

Localization

Localization Comment Organism GeneOntology No. Textmining
particle-bound leaves, seedling shoots Phaseolus vulgaris
-
-
particle-bound leaves, seedling shoots Triticum aestivum
-
-
particle-bound leaves, seedling shoots Pisum sativum
-
-
particle-bound leaves, seedling shoots Zea mays
-
-
particle-bound leaves, seedling shoots Glycine max
-
-
particle-bound leaves, seedling shoots Plantago sp.
-
-
soluble roots Phaseolus vulgaris
-
-
soluble roots Pisum sativum
-
-
soluble roots Glycine max
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-valine + NAD(P)+ + H2O Pisum sativum two forms of enzyme activity: enzyme associated with subcellular structures in shoots or leaves probably plays a biosynthetic role for valine production and the soluble enzyme in roots plays a degradative role in valine catabolism 2-oxoisovalerate + NH3 + NAD(P)H
-
?

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-
Phaseolus vulgaris
-
-
-
Pisum sativum
-
-
-
Plantago sp.
-
-
-
Triticum aestivum
-
-
-
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
soluble enzyme from roots, 3.9fold purification Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
leaf subcellular particles Triticum aestivum
-
leaf subcellular particles Zea mays
-
leaf subcellular particles Plantago sp.
-
additional information enzyme activity observed in seedling shoots, but not in roots Triticum aestivum
-
additional information enzyme activity observed in seedling shoots, but not in roots Zea mays
-
root soluble enzyme Phaseolus vulgaris
-
root soluble enzyme Pisum sativum
-
root soluble enzyme Glycine max
-
seedling enzyme associated with subcellular particles Phaseolus vulgaris
-
seedling enzyme associated with subcellular particles Triticum aestivum
-
seedling enzyme associated with subcellular particles Pisum sativum
-
seedling enzyme associated with subcellular particles Zea mays
-
seedling enzyme associated with subcellular particles Glycine max
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
values for reductive amination at pH 8.5 Phaseolus vulgaris
additional information
-
values for reductive amination at pH 8.5 Triticum aestivum
additional information
-
values for reductive amination at pH 8.5 Pisum sativum
additional information
-
values for reductive amination at pH 8.5 Zea mays
additional information
-
values for reductive amination at pH 8.5 Glycine max
additional information
-
values for reductive amination at pH 8.5 Plantago sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-valine + NAD(P)+ + H2O NADP+ Phaseolus vulgaris 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O NADP+ Triticum aestivum 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O NADP+ Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O NADP+ Zea mays 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O NADP+ Glycine max 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O NADP+ Plantago sp. 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O NADP+ Phaseolus vulgaris 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NADP+ Triticum aestivum 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NADP+ Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NADP+ Zea mays 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NADP+ Glycine max 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NADP+ Plantago sp. 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O soluble enzyme in roots: ratio of rate of reductive amination of valine ketoanalogue to the rate of oxidative deamination of L-valine is 1:1 Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O soluble enzyme in roots: ratio of rate of reductive amination of valine ketoanalogue to the rate of oxidative deamination of L-valine is 1:1 Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Phaseolus vulgaris 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Triticum aestivum 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Zea mays 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Glycine max 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Plantago sp. 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Phaseolus vulgaris 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Triticum aestivum 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Zea mays 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Glycine max 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 2.5:1 Plantago sp. 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O two forms of enzyme activity: enzyme associated with subcellular structures in shoots or leaves probably plays a biosynthetic role for valine production and the soluble enzyme in roots plays a degradative role in valine catabolism Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4 8.6 shoots, reductive amination of valine ketoanalogue Pisum sativum
9.3
-
roots, reductive amination of valine ketoanalogue Pisum sativum
9.4 9.6 shoots, oxidative deamination of L-valine Pisum sativum
11
-
roots, oxidative deamination of L-valine Pisum sativum

Cofactor

Cofactor Comment Organism Structure
additional information plant enzyme not coupled to NAD+ and NADH Phaseolus vulgaris
additional information plant enzyme not coupled to NAD+ and NADH Triticum aestivum
additional information plant enzyme not coupled to NAD+ and NADH Pisum sativum
additional information plant enzyme not coupled to NAD+ and NADH Zea mays
additional information plant enzyme not coupled to NAD+ and NADH Glycine max
additional information plant enzyme not coupled to NAD+ and NADH Plantago sp.
NADP+ in plants enzyme is coupled exclusively to NADP+ Phaseolus vulgaris
NADP+ in plants enzyme is coupled exclusively to NADP+ Triticum aestivum
NADP+ in plants enzyme is coupled exclusively to NADP+ Pisum sativum
NADP+ in plants enzyme is coupled exclusively to NADP+ Zea mays
NADP+ in plants enzyme is coupled exclusively to NADP+ Glycine max
NADP+ in plants enzyme is coupled exclusively to NADP+ Plantago sp.
NADPH in plants valine dehydrogenase coupled exclusively to NADPH Phaseolus vulgaris
NADPH in plants valine dehydrogenase coupled exclusively to NADPH Triticum aestivum
NADPH in plants valine dehydrogenase coupled exclusively to NADPH Pisum sativum
NADPH in plants valine dehydrogenase coupled exclusively to NADPH Zea mays
NADPH in plants valine dehydrogenase coupled exclusively to NADPH Glycine max
NADPH in plants valine dehydrogenase coupled exclusively to NADPH Plantago sp.