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Literature summary for 1.4.1.8 extracted from

  • Nguyen, L.T.; Nguyen, K.T.; Spizek, J.; Behal, V.
    The tylosin producer, Streptomyces fradiae, contains a second valine dehydrogenase (1995), Microbiology, 141, 1139-1145.
No PubMed abstract available

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
vdh gene encoding VDH2, only one gene responsible for VDH activity, VDH2 is the only active VDH Streptomyces fradiae

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ VDH2 : 1 mM, 35.5% inhibition Streptomyces fradiae
iodoacetamide VDH2: 1 mM, complete inhibition Streptomyces fradiae
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
p-hydroxymercuribenzoate VDH2: 0.01 mM, 70% loss of activity Streptomyces fradiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
NADH VDH2 Streptomyces fradiae
0.04
-
NAD+ VDH2 Streptomyces fradiae
0.31
-
2-oxoisovalerate VDH2 Streptomyces fradiae
0.43
-
L-valine VDH2 Streptomyces fradiae
25.6
-
NH4+ VDH2 Streptomyces fradiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
2 * 41000, VDH2, SDS-PAGE Streptomyces fradiae
80000
-
VDH2, gel filtration Streptomyces fradiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
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

Organism UniProt Comment Textmining
Streptomyces fradiae
-
-
-
Streptomyces fradiae
-
two enzymes: VDH1 and VDH2
-
Streptomyces fradiae
-
tylosin producer
-
Streptomyces fradiae 30/3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
VDH2, 346fold purification Streptomyces fradiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
19.56
-
oxidative deamination Streptomyces fradiae
40.92
-
reductive amination Streptomyces fradiae

Storage Stability

Storage Stability Organism
-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
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2-aminobutyrate + H2O + NAD+ VDH2: preferred substrate, 158% of the activity with L-valine Streptomyces fradiae 2-oxobutyrate + NADH + NH3 VDH2: reductive amination, 100% of the activity with 2-oxoisovalerate r
L-2-aminobutyrate + H2O + NAD+ VDH2: preferred substrate, 158% of the activity with L-valine Streptomyces fradiae 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 Streptomyces fradiae 2-oxobutyrate + NADH + NH3 VDH2: reductive amination, 100% of the activity with 2-oxoisovalerate r
L-2-aminobutyrate + H2O + NAD+ L-2-aminobutyrate is identical with L-alpha-aminobutyrate Streptomyces fradiae 2-oxobutyrate + NADH + NH3 2-oxobutyrate is identical with alpha-ketobutyrate r
L-alanine + H2O + NAD+ VDH2: 8.3% of the activity with L-valine Streptomyces fradiae pyruvate + NH3 + NADH pyruvate is identical with alpha-ketopropanoate and 2-oxopropanoate r
L-alanine + H2O + NAD+ VDH2: 8.3% of the activity with L-valine Streptomyces fradiae pyruvate + NH3 + NADH VDH2: reductive amination, 23.3% of the activity with 2-oxoisovalerate r
L-isoleucine + H2O + NAD+ VDH2: 22% of the activity with L-valine Streptomyces fradiae 3-methyl-2-oxopentanoate + NADH + NH3 2-oxo-3-methylvalerate is identical with alpha-keto-beta-methylpentanoate r
L-isoleucine + H2O + NAD+ VDH2: 22% of the activity with L-valine Streptomyces fradiae 3-methyl-2-oxopentanoate + NADH + NH3 VDH2: reductive amination, 16.6% of the activity with 2-oxoisovalerate r
L-leucine + H2O + NAD+ VDH2: 24% of the activity with L-valine Streptomyces fradiae 2-oxoisocaproate + NADH + NH3 2-oxoisocaproate is identical with 2-oxo-4-methylpentanoate, 2-oxoisohexanoate and alpha-ketoisocaproate r
L-leucine + H2O + NAD+ VDH2: 24% of the activity with L-valine Streptomyces fradiae 2-oxoisocaproate + NADH + NH3 VDH2: reductive amination, 20% of the activity with 2-oxoisovalerate r
L-norleucine + H2O + NAD+ VDH2: 34.5% of the activity with L-valine Streptomyces fradiae 2-oxocaproate + NADH + NH3
-
r
L-norvaline + H2O + NAD+ VDH2: 96% of the activity with L-valine Streptomyces fradiae 2-oxovalerate + NH3 + NADH
-
r
L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
L-valine + NAD(P)+ + H2O NAD+ Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O NAD+ Streptomyces fradiae 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+ Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
L-valine + NAD(P)+ + H2O reductive amination rate is twice the oxidative deamination rate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O reductive amination rate is twice the oxidative deamination rate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O reductive amination rate is twice the oxidative deamination rate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
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 Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H
-
?
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 Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 30/3 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 30/3 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 30/3 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
L-valine + NAD(P)+ + H2O NAD+ Streptomyces fradiae 30/3 2-oxoisovalerate + NH3 + NAD(P)H NADH r
additional information NH3 is the sole substrate as amino donor Streptomyces fradiae additional information
-
?
additional information NH3 is the sole substrate as amino donor Streptomyces fradiae 30/3 additional information
-
?

Subunits

Subunits Comment Organism
dimer 2 * 41000, VDH2, SDS-PAGE Streptomyces fradiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
Streptomyces fradiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
VDH2: reductive amination of 2-oxoisovalerate, 0.3 M Tris-HCl buffer Streptomyces fradiae
10.4
-
VDH2: oxidative deamination of L-valine, 0.3 M glycine-KCl-KOH buffer Streptomyces fradiae

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.3
-
VDH2: stable at pH 6.3 during purification step Reactive-Blue 2 Sepharose chromatography Streptomyces fradiae

Cofactor

Cofactor Comment Organism Structure
1,N6-etheno-NAD+ VDH2: 70.5% of the activity with NAD+ Streptomyces fradiae
3-pyridinealdehyde-NAD+ VDH2: 47.2% of the activity with NAD+, VDH1: no activity Streptomyces fradiae
Alpha-NAD+ VDH2: 5.8% of the activity with NAD+ Streptomyces fradiae
deamino-NAD+ VDH2: 124% of the activity with NAD+ Streptomyces fradiae
deamino-NAD+ amino group in the adenine moiety of NAD+ is not essential Streptomyces fradiae
additional information VDH2: not with NADP+, compared to VDH1 with 10.8% of the activity with NAD+ Streptomyces fradiae
NAD+ NAD+ required, no use of NADP+ Streptomyces fradiae
NAD+ natural cofactor for oxidative deamination Streptomyces fradiae
NADH
-
Streptomyces fradiae