Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Activating Compound Comment 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 (Comment) 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 Comment 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 Comment 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Comment 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 (Comment) 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] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 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
1.4.1.8 L-norleucine + H2O + NAD+ VDH2: 34.5% of the activity with L-valine Streptomyces fradiae 2-oxocaproate + NADH + NH3
-
 r
1.4.1.8 L-norvaline + H2O + NAD+ VDH2: 96% of the activity with L-valine Streptomyces fradiae 2-oxovalerate + NH3 + NADH
-
 r
1.4.1.8 L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H NADH r
1.4.1.8 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
1.4.1.8 L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
1.4.1.8 L-valine + NAD(P)+ + H2O NAD+ Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H NADH r
1.4.1.8 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
1.4.1.8 L-valine + NAD(P)+ + H2O NAD+ Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
1.4.1.8 L-valine + NAD(P)+ + H2O reductive amination rate is twice the oxidative deamination rate Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H NADH r
1.4.1.8 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
1.4.1.8 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
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 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 Streptomyces fradiae 2-oxoisovalerate + NH3 + NAD(P)H
-
 ?
1.4.1.8 L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 30/3 2-oxoisovalerate + NH3 + NAD(P)H NADH r
1.4.1.8 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
1.4.1.8 L-valine + NAD(P)+ + H2O preferred substrate Streptomyces fradiae 30/3 2-oxoisovalerate + NH3 + NAD(P)H reductive amination: preferred substrate r
1.4.1.8 L-valine + NAD(P)+ + H2O NAD+ Streptomyces fradiae 30/3 2-oxoisovalerate + NH3 + NAD(P)H NADH r
1.4.1.8 additional information NH3 is the sole substrate as amino donor Streptomyces fradiae additional information
-
 ?
1.4.1.8 additional information NH3 is the sole substrate as amino donor Streptomyces fradiae 30/3 additional information
-
 ?
1.4.1.23 2-oxobutanoate + NH3 + NADH + H+ 100% of the activity with 2-oxoisovalerate Streptomyces fradiae L-2-aminobutanoate + H2O + NAD+
-
 r
1.4.1.23 2-oxoisohexanoate + NH3 + NADH + H+ 20% of the activity with 2-oxoisovalerate Streptomyces fradiae L-leucine + H2O + NAD+
-
 r
1.4.1.23 2-oxoisovalerate + NH3 + NADH + H+
-
 Streptomyces fradiae L-valine + H2O + NAD+
-
 r
1.4.1.23 2-oxoisovalerate + NH4+ + NADH
-
 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 Streptomyces fradiae L-isoleucine + H2O + NAD+
-
 r
1.4.1.23 L-2-aminobutanoate + H2O + NAD+ 158% of the activity with L-valine Streptomyces fradiae 2-oxobutanoate + NH3 + NADH + H+
-
 r
1.4.1.23 L-alanine + H2O + NAD+ 8.3% of the activity with L-valine Streptomyces fradiae pyruvate + NH3 + NADH + H+
-
 r
1.4.1.23 L-isoleucine + H2O + NAD+ 22% of the activity with L-valine 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 Streptomyces fradiae 2-oxoisohexanoate + NH3 + NADH + H+
-
 r
1.4.1.23 L-norleucine + H2O + NAD+ 34.5% of the activity with L-valine Streptomyces fradiae 2-oxohexanoate + NH3 + NADH + H+
-
 r
1.4.1.23 L-norvaline + H2O + NAD+ 96% of the activity with L-valine Streptomyces fradiae 2-oxovalerate + NH3 + NADH + H+
-
 r
1.4.1.23 L-valine + H2O + NAD+
-
 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 Streptomyces fradiae L-alanine + NH3 + NADH + H+
-
 r

Subunits

EC Number Subunits Comment 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 Comment Organism
1.4.1.23 VDH2
-
 Streptomyces fradiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment 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 Comment 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 Comment 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 Comment 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

Expression

EC Number Organism Comment 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