BRENDA - Enzyme Database

The tylosin producer, Streptomyces fradiae, contains a second valine dehydrogenase

Nguyen, L.T.; Nguyen, K.T.; Spizek, J.; Behal, V.; Microbiology 141, 1139-1145 (1995)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
1.4.1.8
L-valine
VDH synthesis induced by L-valine, but severely repressed by ammonia
Streptomyces fradiae
Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
1.4.1.8
vdh gene encoding VDH2, only one gene responsible for VDH activity, VDH2 is the only active VDH
Streptomyces fradiae
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.4.1.8
Cu2+
VDH2 : 1 mM, 35.5% inhibition
Streptomyces fradiae
1.4.1.8
iodoacetamide
VDH2: 1 mM, complete inhibition
Streptomyces fradiae
1.4.1.8
L-valine
VDH2: 20 mM instead of 10 mM in reaction mixture caused 22% loss of activity, 50 mM 40% loss of activity
Streptomyces fradiae
1.4.1.8
p-hydroxymercuribenzoate
VDH2: 0.01 mM, 70% loss of activity
Streptomyces fradiae
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.4.1.8
0.028
-
NADH
VDH2
Streptomyces fradiae
1.4.1.8
0.04
-
NAD+
VDH2
Streptomyces fradiae
1.4.1.8
0.31
-
2-oxoisovalerate
VDH2
Streptomyces fradiae
1.4.1.8
0.43
-
L-valine
VDH2
Streptomyces fradiae
1.4.1.8
25.6
-
NH4+
VDH2
Streptomyces fradiae
1.4.1.23
0.028
-
NADH
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
0.04
-
NAD+
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
0.31
-
2-oxoisovalerate
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
0.43
-
L-valine
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
25.6
-
NH4+
pH 10.4, 30°C
Streptomyces fradiae
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.4.1.8
41000
-
2 * 41000, VDH2, SDS-PAGE
Streptomyces fradiae
1.4.1.8
80000
-
VDH2, gel filtration
Streptomyces fradiae
1.4.1.23
41000
-
2 * 41000, SDS-PAGE
Streptomyces fradiae
1.4.1.23
80000
-
gel filtration
Streptomyces fradiae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.4.1.8
L-valine + NAD(P)+ + H2O
Streptomyces fradiae
VDH2 rather than VDH1 plays a role in metabolism of branched chain amino acids and thus in tylosin biosynthesis, expression of VDH1 is unstable
2-oxoisovalerate + NH3 + NAD(P)H
-
-
?
1.4.1.8
L-valine + NAD(P)+ + H2O
Streptomyces fradiae
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
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.4.1.8
Streptomyces fradiae
-
-
-
1.4.1.8
Streptomyces fradiae
-
two enzymes: VDH1 and VDH2
-
1.4.1.8
Streptomyces fradiae
-
tylosin producer
-
1.4.1.8
Streptomyces fradiae 30/3
-
-
-
1.4.1.23
Streptomyces fradiae
-
-
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
1.4.1.8
VDH2, 346fold purification
Streptomyces fradiae
1.4.1.23
-
Streptomyces fradiae
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.4.1.8
19.56
-
oxidative deamination
Streptomyces fradiae
1.4.1.8
40.92
-
reductive amination
Streptomyces fradiae
Storage Stability
EC Number
Storage Stability
Organism
1.4.1.8
-20°C, 50 mM Tris-HCl buffer, pH 7.4, 5 mM 2-mercaptoethanol, 1 mM EDTA, 30% v/v glycerol, 24 h, 90% loss of activity
Streptomyces fradiae
1.4.1.8
4°C, 50 mM Tris-HCl buffer, pH 7.4, 5 mM 2-mercaptoethanol, 1 mM EDTA, 10% v/v glycerol, 48 h, stable
Streptomyces fradiae
1.4.1.23
-20°C, pH 7.4, presence of 2-mercaptoethanol and 30% glycerol, loss of 90% of activity with 24 h
Streptomyces fradiae
1.4.1.23
4°C, pH 7.4, presence of 2-mercaptoethanol and 10% glycerol, stable for 48 h
Streptomyces fradiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
VDH2: preferred substrate, 158% of the activity with L-valine
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
VDH2: reductive amination, 100% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
VDH2: preferred substrate, 158% of the activity with L-valine
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
2-oxobutyrate is identical with alpha-ketobutyrate
391703
Streptomyces fradiae
r
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
L-2-aminobutyrate is identical with L-alpha-aminobutyrate
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
VDH2: reductive amination, 100% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
L-2-aminobutyrate is identical with L-alpha-aminobutyrate
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
2-oxobutyrate is identical with alpha-ketobutyrate
391703
Streptomyces fradiae
r
1.4.1.8
L-alanine + H2O + NAD+
VDH2: 8.3% of the activity with L-valine
391703
Streptomyces fradiae
pyruvate + NH3 + NADH
pyruvate is identical with alpha-ketopropanoate and 2-oxopropanoate
391703
Streptomyces fradiae
r
1.4.1.8
L-alanine + H2O + NAD+
VDH2: 8.3% of the activity with L-valine
391703
Streptomyces fradiae
pyruvate + NH3 + NADH
VDH2: reductive amination, 23.3% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-isoleucine + H2O + NAD+
VDH2: 22% of the activity with L-valine
391703
Streptomyces fradiae
3-methyl-2-oxopentanoate + NADH + NH3
2-oxo-3-methylvalerate is identical with alpha-keto-beta-methylpentanoate
391703
Streptomyces fradiae
r
1.4.1.8
L-isoleucine + H2O + NAD+
VDH2: 22% of the activity with L-valine
391703
Streptomyces fradiae
3-methyl-2-oxopentanoate + NADH + NH3
VDH2: reductive amination, 16.6% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-leucine + H2O + NAD+
VDH2: 24% of the activity with L-valine
391703
Streptomyces fradiae
2-oxoisocaproate + NADH + NH3
2-oxoisocaproate is identical with 2-oxo-4-methylpentanoate, 2-oxoisohexanoate and alpha-ketoisocaproate
391703
Streptomyces fradiae
r
1.4.1.8
L-leucine + H2O + NAD+
VDH2: 24% of the activity with L-valine
391703
Streptomyces fradiae
2-oxoisocaproate + NADH + NH3
VDH2: reductive amination, 20% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-norleucine + H2O + NAD+
VDH2: 34.5% of the activity with L-valine
391703
Streptomyces fradiae
2-oxocaproate + NADH + NH3
-
-
-
r
1.4.1.8
L-norvaline + H2O + NAD+
VDH2: 96% of the activity with L-valine
391703
Streptomyces fradiae
2-oxovalerate + NH3 + NADH
-
-
-
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
reductive amination rate is twice the oxidative deamination rate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
reductive amination rate is twice the oxidative deamination rate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
reductive amination rate is twice the oxidative deamination rate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
VDH2 rather than VDH1 plays a role in metabolism of branched chain amino acids and thus in tylosin biosynthesis, expression of VDH1 is unstable
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
-
-
-
?
1.4.1.8
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
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
-
-
-
?
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae 30/3
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae 30/3
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae 30/3
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae 30/3
r
1.4.1.8
additional information
NH3 is the sole substrate as amino donor
391703
Streptomyces fradiae
additional information
-
-
-
?
1.4.1.8
additional information
NH3 is the sole substrate as amino donor
391703
Streptomyces fradiae 30/3
additional information
-
-
-
?
1.4.1.23
2-oxobutanoate + NH3 + NADH + H+
100% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-2-aminobutanoate + H2O + NAD+
-
-
-
r
1.4.1.23
2-oxoisohexanoate + NH3 + NADH + H+
20% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-leucine + H2O + NAD+
-
-
-
r
1.4.1.23
2-oxoisovalerate + NH3 + NADH + H+
-
391703
Streptomyces fradiae
L-valine + H2O + NAD+
-
-
-
r
1.4.1.23
2-oxoisovalerate + NH4+ + NADH
-
391703
Streptomyces fradiae
L-valine + H2O + NAD+
-
-
-
r
1.4.1.23
3-methyl-2-oxopentanoate + NH3 + NADH + H+
16.6% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-isoleucine + H2O + NAD+
-
-
-
r
1.4.1.23
L-2-aminobutanoate + H2O + NAD+
158% of the activity with L-valine
391703
Streptomyces fradiae
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-alanine + H2O + NAD+
8.3% of the activity with L-valine
391703
Streptomyces fradiae
pyruvate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-isoleucine + H2O + NAD+
22% of the activity with L-valine
391703
Streptomyces fradiae
3-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-leucine + H2O + NAD+
24% of the activity with L-valine
391703
Streptomyces fradiae
2-oxoisohexanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-norleucine + H2O + NAD+
34.5% of the activity with L-valine
391703
Streptomyces fradiae
2-oxohexanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-norvaline + H2O + NAD+
96% of the activity with L-valine
391703
Streptomyces fradiae
2-oxovalerate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-valine + H2O + NAD+
-
391703
Streptomyces fradiae
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
pyruvate + H2O + NAD+
23.3% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-alanine + NH3 + NADH + H+
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
1.4.1.8
dimer
2 * 41000, VDH2, SDS-PAGE
Streptomyces fradiae
1.4.1.23
dimer
2 * 41000, SDS-PAGE
Streptomyces fradiae
Synonyms
EC Number
Synonyms
Commentary
Organism
1.4.1.23
VDH2
-
Streptomyces fradiae
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.4.1.8
65
-
-
Streptomyces fradiae
1.4.1.23
65
-
both oxidative deamination and reductive amination
Streptomyces fradiae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.4.1.8
8.8
-
VDH2: reductive amination of 2-oxoisovalerate, 0.3 M Tris-HCl buffer
Streptomyces fradiae
1.4.1.8
10.4
-
VDH2: oxidative deamination of L-valine, 0.3 M glycine-KCl-KOH buffer
Streptomyces fradiae
1.4.1.23
8.8
-
reductive amination
Streptomyces fradiae
1.4.1.23
10.4
-
oxidative deamination
Streptomyces fradiae
pH Stability
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
1.4.1.8
6.3
-
VDH2: stable at pH 6.3 during purification step Reactive-Blue 2 Sepharose chromatography
Streptomyces fradiae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.4.1.8
1,N6-etheno-NAD+
VDH2: 70.5% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
3-pyridinealdehyde-NAD+
VDH2: 47.2% of the activity with NAD+, VDH1: no activity
Streptomyces fradiae
1.4.1.8
Alpha-NAD+
VDH2: 5.8% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
deamino-NAD+
VDH2: 124% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
deamino-NAD+
amino group in the adenine moiety of NAD+ is not essential
Streptomyces fradiae
1.4.1.8
additional information
VDH2: not with NADP+, compared to VDH1 with 10.8% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
NAD+
NAD+ required, no use of NADP+
Streptomyces fradiae
1.4.1.8
NAD+
natural cofactor for oxidative deamination
Streptomyces fradiae
1.4.1.8
NADH
-
Streptomyces fradiae
1.4.1.23
1,N6-etheno-NAD+
70.5% of the activity with NAD+
Streptomyces fradiae
1.4.1.23
3-pyridinealdehyde-NAD+
47% of the activity with NAD+
Streptomyces fradiae
1.4.1.23
deamino-NAD+
124% of the activity with NAD+
Streptomyces fradiae
1.4.1.23
additional information
no activity with NADP+
Streptomyces fradiae
1.4.1.23
NAD+
-
Streptomyces fradiae
1.4.1.23
NADH
-
Streptomyces fradiae
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
1.4.1.8
L-valine
VDH synthesis induced by L-valine, but severely repressed by ammonia
Streptomyces fradiae
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.4.1.8
vdh gene encoding VDH2, only one gene responsible for VDH activity, VDH2 is the only active VDH
Streptomyces fradiae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.4.1.8
1,N6-etheno-NAD+
VDH2: 70.5% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
3-pyridinealdehyde-NAD+
VDH2: 47.2% of the activity with NAD+, VDH1: no activity
Streptomyces fradiae
1.4.1.8
Alpha-NAD+
VDH2: 5.8% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
deamino-NAD+
VDH2: 124% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
deamino-NAD+
amino group in the adenine moiety of NAD+ is not essential
Streptomyces fradiae
1.4.1.8
additional information
VDH2: not with NADP+, compared to VDH1 with 10.8% of the activity with NAD+
Streptomyces fradiae
1.4.1.8
NAD+
NAD+ required, no use of NADP+
Streptomyces fradiae
1.4.1.8
NAD+
natural cofactor for oxidative deamination
Streptomyces fradiae
1.4.1.8
NADH
-
Streptomyces fradiae
1.4.1.23
1,N6-etheno-NAD+
70.5% of the activity with NAD+
Streptomyces fradiae
1.4.1.23
3-pyridinealdehyde-NAD+
47% of the activity with NAD+
Streptomyces fradiae
1.4.1.23
deamino-NAD+
124% of the activity with NAD+
Streptomyces fradiae
1.4.1.23
additional information
no activity with NADP+
Streptomyces fradiae
1.4.1.23
NAD+
-
Streptomyces fradiae
1.4.1.23
NADH
-
Streptomyces fradiae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.4.1.8
Cu2+
VDH2 : 1 mM, 35.5% inhibition
Streptomyces fradiae
1.4.1.8
iodoacetamide
VDH2: 1 mM, complete inhibition
Streptomyces fradiae
1.4.1.8
L-valine
VDH2: 20 mM instead of 10 mM in reaction mixture caused 22% loss of activity, 50 mM 40% loss of activity
Streptomyces fradiae
1.4.1.8
p-hydroxymercuribenzoate
VDH2: 0.01 mM, 70% loss of activity
Streptomyces fradiae
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.4.1.8
0.028
-
NADH
VDH2
Streptomyces fradiae
1.4.1.8
0.04
-
NAD+
VDH2
Streptomyces fradiae
1.4.1.8
0.31
-
2-oxoisovalerate
VDH2
Streptomyces fradiae
1.4.1.8
0.43
-
L-valine
VDH2
Streptomyces fradiae
1.4.1.8
25.6
-
NH4+
VDH2
Streptomyces fradiae
1.4.1.23
0.028
-
NADH
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
0.04
-
NAD+
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
0.31
-
2-oxoisovalerate
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
0.43
-
L-valine
pH 10.4, 30°C
Streptomyces fradiae
1.4.1.23
25.6
-
NH4+
pH 10.4, 30°C
Streptomyces fradiae
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.4.1.8
41000
-
2 * 41000, VDH2, SDS-PAGE
Streptomyces fradiae
1.4.1.8
80000
-
VDH2, gel filtration
Streptomyces fradiae
1.4.1.23
41000
-
2 * 41000, SDS-PAGE
Streptomyces fradiae
1.4.1.23
80000
-
gel filtration
Streptomyces fradiae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.4.1.8
L-valine + NAD(P)+ + H2O
Streptomyces fradiae
VDH2 rather than VDH1 plays a role in metabolism of branched chain amino acids and thus in tylosin biosynthesis, expression of VDH1 is unstable
2-oxoisovalerate + NH3 + NAD(P)H
-
-
?
1.4.1.8
L-valine + NAD(P)+ + H2O
Streptomyces fradiae
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
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.4.1.8
VDH2, 346fold purification
Streptomyces fradiae
1.4.1.23
-
Streptomyces fradiae
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.4.1.8
19.56
-
oxidative deamination
Streptomyces fradiae
1.4.1.8
40.92
-
reductive amination
Streptomyces fradiae
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
1.4.1.8
-20°C, 50 mM Tris-HCl buffer, pH 7.4, 5 mM 2-mercaptoethanol, 1 mM EDTA, 30% v/v glycerol, 24 h, 90% loss of activity
Streptomyces fradiae
1.4.1.8
4°C, 50 mM Tris-HCl buffer, pH 7.4, 5 mM 2-mercaptoethanol, 1 mM EDTA, 10% v/v glycerol, 48 h, stable
Streptomyces fradiae
1.4.1.23
-20°C, pH 7.4, presence of 2-mercaptoethanol and 30% glycerol, loss of 90% of activity with 24 h
Streptomyces fradiae
1.4.1.23
4°C, pH 7.4, presence of 2-mercaptoethanol and 10% glycerol, stable for 48 h
Streptomyces fradiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
VDH2: preferred substrate, 158% of the activity with L-valine
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
VDH2: reductive amination, 100% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
VDH2: preferred substrate, 158% of the activity with L-valine
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
2-oxobutyrate is identical with alpha-ketobutyrate
391703
Streptomyces fradiae
r
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
L-2-aminobutyrate is identical with L-alpha-aminobutyrate
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
VDH2: reductive amination, 100% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-2-aminobutyrate + H2O + NAD+
L-2-aminobutyrate is identical with L-alpha-aminobutyrate
391703
Streptomyces fradiae
2-oxobutyrate + NADH + NH3
2-oxobutyrate is identical with alpha-ketobutyrate
391703
Streptomyces fradiae
r
1.4.1.8
L-alanine + H2O + NAD+
VDH2: 8.3% of the activity with L-valine
391703
Streptomyces fradiae
pyruvate + NH3 + NADH
pyruvate is identical with alpha-ketopropanoate and 2-oxopropanoate
391703
Streptomyces fradiae
r
1.4.1.8
L-alanine + H2O + NAD+
VDH2: 8.3% of the activity with L-valine
391703
Streptomyces fradiae
pyruvate + NH3 + NADH
VDH2: reductive amination, 23.3% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-isoleucine + H2O + NAD+
VDH2: 22% of the activity with L-valine
391703
Streptomyces fradiae
3-methyl-2-oxopentanoate + NADH + NH3
2-oxo-3-methylvalerate is identical with alpha-keto-beta-methylpentanoate
391703
Streptomyces fradiae
r
1.4.1.8
L-isoleucine + H2O + NAD+
VDH2: 22% of the activity with L-valine
391703
Streptomyces fradiae
3-methyl-2-oxopentanoate + NADH + NH3
VDH2: reductive amination, 16.6% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-leucine + H2O + NAD+
VDH2: 24% of the activity with L-valine
391703
Streptomyces fradiae
2-oxoisocaproate + NADH + NH3
2-oxoisocaproate is identical with 2-oxo-4-methylpentanoate, 2-oxoisohexanoate and alpha-ketoisocaproate
391703
Streptomyces fradiae
r
1.4.1.8
L-leucine + H2O + NAD+
VDH2: 24% of the activity with L-valine
391703
Streptomyces fradiae
2-oxoisocaproate + NADH + NH3
VDH2: reductive amination, 20% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-norleucine + H2O + NAD+
VDH2: 34.5% of the activity with L-valine
391703
Streptomyces fradiae
2-oxocaproate + NADH + NH3
-
-
-
r
1.4.1.8
L-norvaline + H2O + NAD+
VDH2: 96% of the activity with L-valine
391703
Streptomyces fradiae
2-oxovalerate + NH3 + NADH
-
-
-
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
reductive amination rate is twice the oxidative deamination rate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
reductive amination rate is twice the oxidative deamination rate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
reductive amination rate is twice the oxidative deamination rate
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae
r
1.4.1.8
L-valine + NAD(P)+ + H2O
VDH2 rather than VDH1 plays a role in metabolism of branched chain amino acids and thus in tylosin biosynthesis, expression of VDH1 is unstable
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
-
-
-
?
1.4.1.8
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
391703
Streptomyces fradiae
2-oxoisovalerate + NH3 + NAD(P)H
-
-
-
?
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae 30/3
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate
391703
Streptomyces fradiae 30/3
r
1.4.1.8
L-valine + NAD(P)+ + H2O
preferred substrate
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
reductive amination: preferred substrate
391703
Streptomyces fradiae 30/3
r
1.4.1.8
L-valine + NAD(P)+ + H2O
NAD+
391703
Streptomyces fradiae 30/3
2-oxoisovalerate + NH3 + NAD(P)H
NADH
391703
Streptomyces fradiae 30/3
r
1.4.1.8
additional information
NH3 is the sole substrate as amino donor
391703
Streptomyces fradiae
additional information
-
-
-
?
1.4.1.8
additional information
NH3 is the sole substrate as amino donor
391703
Streptomyces fradiae 30/3
additional information
-
-
-
?
1.4.1.23
2-oxobutanoate + NH3 + NADH + H+
100% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-2-aminobutanoate + H2O + NAD+
-
-
-
r
1.4.1.23
2-oxoisohexanoate + NH3 + NADH + H+
20% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-leucine + H2O + NAD+
-
-
-
r
1.4.1.23
2-oxoisovalerate + NH3 + NADH + H+
-
391703
Streptomyces fradiae
L-valine + H2O + NAD+
-
-
-
r
1.4.1.23
2-oxoisovalerate + NH4+ + NADH
-
391703
Streptomyces fradiae
L-valine + H2O + NAD+
-
-
-
r
1.4.1.23
3-methyl-2-oxopentanoate + NH3 + NADH + H+
16.6% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-isoleucine + H2O + NAD+
-
-
-
r
1.4.1.23
L-2-aminobutanoate + H2O + NAD+
158% of the activity with L-valine
391703
Streptomyces fradiae
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-alanine + H2O + NAD+
8.3% of the activity with L-valine
391703
Streptomyces fradiae
pyruvate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-isoleucine + H2O + NAD+
22% of the activity with L-valine
391703
Streptomyces fradiae
3-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-leucine + H2O + NAD+
24% of the activity with L-valine
391703
Streptomyces fradiae
2-oxoisohexanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-norleucine + H2O + NAD+
34.5% of the activity with L-valine
391703
Streptomyces fradiae
2-oxohexanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-norvaline + H2O + NAD+
96% of the activity with L-valine
391703
Streptomyces fradiae
2-oxovalerate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
L-valine + H2O + NAD+
-
391703
Streptomyces fradiae
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
1.4.1.23
pyruvate + H2O + NAD+
23.3% of the activity with 2-oxoisovalerate
391703
Streptomyces fradiae
L-alanine + NH3 + NADH + H+
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.4.1.8
dimer
2 * 41000, VDH2, SDS-PAGE
Streptomyces fradiae
1.4.1.23
dimer
2 * 41000, SDS-PAGE
Streptomyces fradiae
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.4.1.8
65
-
-
Streptomyces fradiae
1.4.1.23
65
-
both oxidative deamination and reductive amination
Streptomyces fradiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.4.1.8
8.8
-
VDH2: reductive amination of 2-oxoisovalerate, 0.3 M Tris-HCl buffer
Streptomyces fradiae
1.4.1.8
10.4
-
VDH2: oxidative deamination of L-valine, 0.3 M glycine-KCl-KOH buffer
Streptomyces fradiae
1.4.1.23
8.8
-
reductive amination
Streptomyces fradiae
1.4.1.23
10.4
-
oxidative deamination
Streptomyces fradiae
pH Stability (protein specific)
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
1.4.1.8
6.3
-
VDH2: stable at pH 6.3 during purification step Reactive-Blue 2 Sepharose chromatography
Streptomyces fradiae
Expression
EC Number
Organism
Commentary
Expression
1.4.1.23
Streptomyces fradiae
activity is repressed in presence of ammonia
down
1.4.1.23
Streptomyces fradiae
activity is induced in presence of L-valine
up
Expression (protein specific)
EC Number
Organism
Commentary
Expression
1.4.1.23
Streptomyces fradiae
activity is repressed in presence of ammonia
down
1.4.1.23
Streptomyces fradiae
activity is induced in presence of L-valine
up