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Literature summary for 1.4.1.8 extracted from

  • Nguyen, L.T.; Nguyen, K.T.; Kopecky, J.; Nova, P.; Novotna, J.; Behal, V.
    Purification and characterization of a novel valine dehydrogenase from Streptomyces aureofaciens (1995), Biochim. Biophys. Acta, 1251, 186-190.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
L-valine VDH synthesis induced by L-valine, but severely repressed by ammonia Kitasatospora aureofaciens

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide VDH2: 1 mM, 50% loss of activity Kitasatospora aureofaciens
Mn2+ VDH2: 1 mM, 60% loss of activity Kitasatospora aureofaciens
p-hydroxymercuribenzoate VDH2: 0.01 mM, complete inhibition Kitasatospora aureofaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.46
-
2-oxoisovalerate VDH2 Kitasatospora aureofaciens
0.75
-
L-valine VDH2 Kitasatospora aureofaciens
1.06
-
2-oxo-3-methylvalerate VDH2 Kitasatospora aureofaciens
1.2
-
2-oxoisocaproate VDH2 Kitasatospora aureofaciens
1.66
-
L-norvaline VDH2 Kitasatospora aureofaciens
1.72
-
L-isoleucine VDH2 Kitasatospora aureofaciens
1.85
-
L-leucine VDH2 Kitasatospora aureofaciens
4.35
-
L-2-aminobutyrate VDH2 Kitasatospora aureofaciens
17.2
-
pyruvate VDH2 Kitasatospora aureofaciens
22.5
-
L-norleucine VDH2 Kitasatospora aureofaciens
117.6
-
L-methionine VDH2 Kitasatospora aureofaciens
333.3
-
L-alanine VDH2 Kitasatospora aureofaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
6 * 41000, VDH2, SDS-PAGE Kitasatospora aureofaciens
240000
-
VDH2, gel filtration Kitasatospora aureofaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-valine + NAD(P)+ + H2O Kitasatospora aureofaciens VDH is required for utilization of branched chain amino acids, the catabolism appears to be an alternative source of n-butyrate, 2-methylmalonate, and propionate needed for biosynthesis of macrolide and polyether antibiotics 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O Kitasatospora aureofaciens first step in valine catabolism 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O Kitasatospora aureofaciens BS-5 VDH is required for utilization of branched chain amino acids, the catabolism appears to be an alternative source of n-butyrate, 2-methylmalonate, and propionate needed for biosynthesis of macrolide and polyether antibiotics 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O Kitasatospora aureofaciens BS-5 first step in valine catabolism 2-oxoisovalerate + NH3 + NAD(P)H
-
?

Organism

Organism UniProt Comment Textmining
Kitasatospora aureofaciens
-
-
-
Kitasatospora aureofaciens
-
two isoenzymes: VDH1 and VDH2
-
Kitasatospora aureofaciens BS-5
-
-
-

Purification (Commentary)

Purification (Comment) Organism
VDH2, 52.6fold purification Kitasatospora aureofaciens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
45.01
-
NAD+ Kitasatospora aureofaciens
64.31
-
oxidative deamination Kitasatospora aureofaciens
366.5
-
reductive amination Kitasatospora aureofaciens

Storage Stability

Storage Stability Organism
-80┬░C, 100 mM Tris-HCl buffer, pH 7.4, 20% v/v glycerol, 2 months, stable Kitasatospora aureofaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2-aminobutyrate + H2O + NAD+ VDH2: 125% of the activity with L-valine Kitasatospora aureofaciens 2-oxobutyrate + NADH + NH3 VDH2: reductive amination, 116% of the activity with 2-oxoisovalerate r
L-2-aminobutyrate + H2O + NAD+ VDH2: 125% of the activity with L-valine Kitasatospora aureofaciens 2-oxobutyrate + NADH + NH3 2-oxobutyrate is identical with alpha-ketobutyrate r
L-2-aminobutyrate + H2O + NAD+ L-2-aminobutyrate is identical with L-alpha-aminobutyrate Kitasatospora aureofaciens 2-oxobutyrate + NADH + NH3 VDH2: reductive amination, 116% of the activity with 2-oxoisovalerate r
L-2-aminobutyrate + H2O + NAD+ L-2-aminobutyrate is identical with L-alpha-aminobutyrate Kitasatospora aureofaciens 2-oxobutyrate + NADH + NH3 2-oxobutyrate is identical with alpha-ketobutyrate r
L-alanine + H2O + NAD+ VDH2: 4.5% of the activity with L-valine Kitasatospora aureofaciens pyruvate + NH3 + NADH pyruvate is identical with alpha-ketopropanoate and 2-oxopropanoate r
L-alanine + H2O + NAD+ VDH2: 4.5% of the activity with L-valine Kitasatospora aureofaciens pyruvate + NH3 + NADH VDH2: reductive amination, 20.8% of the activity with 2-oxoisovalerate r
L-isoleucine + H2O + NAD+ VDH2: 34% of the activity with L-valine Kitasatospora aureofaciens 3-methyl-2-oxopentanoate + NADH + NH3 2-oxo-3-methylvalerate is identical with alpha-keto-beta-methylpentanoate r
L-isoleucine + H2O + NAD+ VDH2: 34% of the activity with L-valine Kitasatospora aureofaciens 3-methyl-2-oxopentanoate + NADH + NH3 VDH2: reductive amination, 24.5% of the activity with 2-oxoisovalerate r
L-leucine + H2O + NAD+ VDH2: 52.8% of the activity with L-valine Kitasatospora aureofaciens 2-oxoisocaproate + NADH + NH3 2-oxoisocaproate is identical with 2-oxo-4-methylpentanoate, 2-oxoisohexanoate and alpha-ketoisocaproate r
L-leucine + H2O + NAD+ VDH2: 52.8% of the activity with L-valine Kitasatospora aureofaciens 2-oxoisocaproate + NADH + NH3 VDH2: reductive amination, 26.5% of the activity with 2-oxoisovalerate r
L-methionine + H2O + NAD+ VDH2: 2% of the activity with L-valine Kitasatospora aureofaciens 4-(methylthio)-2-oxobutanoic acid + NH3 + NADH
-
r
L-norleucine + H2O + NAD+ VDH2: 18.5% of the activity with L-valine Kitasatospora aureofaciens 2-oxocaproate + NADH + NH3
-
r
L-norvaline + H2O + NAD+ VDH2: 100% of the activity with L-valine Kitasatospora aureofaciens 2-oxovalerate + NH3 + NADH
-
r
L-valine + NAD(P)+ + H2O NAD+ Kitasatospora aureofaciens 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O NAD+ Kitasatospora aureofaciens 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NAD+ Kitasatospora aureofaciens 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
L-valine + NAD(P)+ + H2O VDH is required for utilization of branched chain amino acids, the catabolism appears to be an alternative source of n-butyrate, 2-methylmalonate, and propionate needed for biosynthesis of macrolide and polyether antibiotics Kitasatospora aureofaciens 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O first step in valine catabolism Kitasatospora aureofaciens 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O NAD+ Kitasatospora aureofaciens BS-5 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O NAD+ Kitasatospora aureofaciens BS-5 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O NAD+ Kitasatospora aureofaciens BS-5 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
L-valine + NAD(P)+ + H2O VDH is required for utilization of branched chain amino acids, the catabolism appears to be an alternative source of n-butyrate, 2-methylmalonate, and propionate needed for biosynthesis of macrolide and polyether antibiotics Kitasatospora aureofaciens BS-5 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O first step in valine catabolism Kitasatospora aureofaciens BS-5 2-oxoisovalerate + NH3 + NAD(P)H
-
?

Subunits

Subunits Comment Organism
hexamer 6 * 41000, VDH2, SDS-PAGE Kitasatospora aureofaciens

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
65
-
-
Kitasatospora aureofaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
VDH2: reductive amination of 2-oxoisovalerate, 0.3 M Tris-HCl buffer Kitasatospora aureofaciens
10.4
-
VDH2: oxidative deamination of L-valine, 0.3 M glycine-KCl-KOH buffer Kitasatospora aureofaciens

Cofactor

Cofactor Comment Organism Structure
1,N6-etheno-NAD+ VDH2: 62.4% of the activity with NAD+ Kitasatospora aureofaciens
3-pyridinealdehyde-NAD+ VDH2: 37.5% of the activity with NAD+ Kitasatospora aureofaciens
Alpha-NAD+ VDH2: 5% of the activity with NAD+, VDH1: no activity Kitasatospora aureofaciens
deamino-NAD+ VDH2: 375.5% of the activity with NAD+ Kitasatospora aureofaciens
additional information VDH2: not with 3-acetylpyridine-NAD+, compared to VDH1 with 100% of the activity with NAD+ Kitasatospora aureofaciens
additional information not with NADP+ and NADPH Kitasatospora aureofaciens
NAD+ NAD+ required, no use of NADP+ Kitasatospora aureofaciens
NAD+ natural cofactor for oxidative deamination Kitasatospora aureofaciens
NADH NADH could not be replaced with NADPH for the reductive amination Kitasatospora aureofaciens
nicotinamide guanine dinucleotide VDH2: 80% of the activity with NAD+ Kitasatospora aureofaciens