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Literature summary for 1.4.1.8 extracted from

  • Kagan, Z.S.; Polyakov, V.A.; Kretovich, V.L.
    Further studies on plant valine dehydrogenase (1970), Enzymologia, 38, 201-224.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
NADPH shoots Pisum sativum
0.235
-
NADP+ shoots Pisum sativum
0.538
-
2-oxoisovalerate shoots Pisum sativum
1.1
-
L-valine shoots Pisum sativum
15.5
-
NH4+ shoots Pisum sativum

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
shoots: 21fold purification, 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.
-
root soluble enzyme Phaseolus vulgaris
-
root soluble enzyme Pisum sativum
-
root soluble enzyme Glycine max
-
seedling
-
Triticum aestivum
-
seedling
-
Zea mays
-
seedling subcellular structures Phaseolus vulgaris
-
seedling subcellular structures Pisum sativum
-
seedling subcellular structures Glycine max
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/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-isoleucine + H2O + NAD+
-
Pisum sativum 3-methyl-2-oxopentanoate + NADH + NH3 2-oxo-3-methylvalerate is identical with alpha-keto-beta-methylpentanoate ?
L-isoleucine + H2O + NAD+
-
Pisum sativum 3-methyl-2-oxopentanoate + NADH + NH3 reductive amination: 59% of the activity of 2-oxoisovalerate, but no oxidative deamination of L-isoleucine ?
L-valine + NAD(P)+ + H2O NADP+ Phaseolus vulgaris 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O NADP+ Triticum aestivum 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O NADP+ Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O NADP+ Zea mays 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O NADP+ Glycine max 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O NADP+ Plantago sp. 2-oxoisovalerate + NH3 + NAD(P)H
-
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
-
r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 5:1 Phaseolus vulgaris 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 5:1 Triticum aestivum 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 5:1 Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 5:1 Zea mays 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 5:1 Glycine max 2-oxoisovalerate + NH3 + NAD(P)H
-
r
L-valine + NAD(P)+ + H2O in the enzyme associated with subcellular structures in shoots it is 5:1 Plantago sp. 2-oxoisovalerate + NH3 + NAD(P)H
-
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
-
?
additional information
-
Phaseolus vulgaris additional information
-
?
additional information
-
Triticum aestivum additional information
-
?
additional information
-
Zea mays additional information
-
?
additional information
-
Glycine max additional information
-
?
additional information
-
Plantago sp. additional information
-
?
additional information no oxidative deamination of L-isoleucine and L-alanine Pisum sativum additional information no reductive amination of 2-oxobutyrate ?

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
40
-
enzyme in shoots Pisum sativum

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
9.5
-
oxidative deamination of L-valine Pisum sativum
11
-
roots, oxidative deamination of L-valine Pisum sativum

Cofactor

Cofactor Comment Organism Structure
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.
NADP+ shoots: enzyme affinity to NADP+ less than to NADPH Pisum sativum
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.