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Literature summary extracted from

  • Kagan, Z.S.; Polyakov, V.A.; Kretovich, V.L.
    Purification and properties of valine dehydrogenase (1969), Biokhimiya, 34, 59-65.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.8 0.14
-
NADPH shoots Pisum sativum
1.4.1.8 0.235
-
NADP+ shoots Pisum sativum
1.4.1.8 0.538
-
2-oxoisovalerate shoots Pisum sativum
1.4.1.8 1.1
-
L-valine shoots Pisum sativum
1.4.1.8 15.5
-
NH4+ shoots Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.1.8 particle-bound sprout Pisum sativum
-
-
1.4.1.8 soluble roots Pisum sativum
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.8 Pisum sativum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.8 21fold purification Pisum sativum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.8 sprout
-
Pisum sativum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.8 additional information
-
-
Pisum sativum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.8 L-isoleucine + H2O + NAD+
-
Pisum sativum 3-methyl-2-oxopentanoate + NADH + NH3 2-oxo-3-methylvalerate is identical with alpha-keto-beta-methylpentanoate ?
1.4.1.8 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 ?
1.4.1.8 L-valine + NAD(P)+ + H2O NADP+ Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 L-valine + NAD(P)+ + H2O rate of reductive amination of ketoanalogue of valine 5 times greater than rate of oxidative deamination of L-valine Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H NADPH r
1.4.1.8 L-valine + NAD(P)+ + H2O rate of reductive amination of ketoanalogue of valine 5 times greater than rate of oxidative deamination of L-valine Pisum sativum 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
1.4.1.8 additional information no oxidative deamination of L-isoleucine and L-alanine Pisum sativum additional information no reductive amination of 2-oxobutyrate ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.8 9.5
-
oxidative deamination of L-valine Pisum sativum

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.8 NADP+ in plants enzyme is coupled exclusively to NADP+ Pisum sativum
1.4.1.8 NADPH in plants valine dehydrogenase coupled exclusively to NADPH Pisum sativum