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Literature summary for 1.4.1.8 extracted from

  • Hyun, C.G.; Kim, S.S.; Lee, I.H.; Suh, J.W.
    Alteration of substrate specificity of valine dehydrogenase from Streptomyces albus (2000), Antonie van Leeuwenhoek, 78, 237-242.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
valDH gene cloned to identify the active site, coding region expressed in Escherichia coli using a pET expression system Streptomyces albus

Protein Variants

Protein Variants Comment Organism
A124G lower activity toward aliphatic amino acid substrates, e.g. catalytic rate constant for oxidative deamination of L-valine is only 12% of the wild type, but higher activities toward L-phenylalanine, L-tyrosine, and L-methionine Streptomyces albus

Inhibitors

Inhibitors Comment Organism Structure
diethyldicarbonate 20 mM, 60% loss of activity Streptomyces albus
N-bromosuccinimide 0.5 mM, complete inhibition Streptomyces albus
oxo(phenyl)acetaldehyde 5 mM, 60% loss of activity Streptomyces albus
p-chloromercuribenzoate 0.5 mM, complete inhibition Streptomyces albus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
NAD+
-
Streptomyces albus
0.43
-
NAD+ A124G mutant Streptomyces albus
1.5
-
L-valine
-
Streptomyces albus
55.06
-
L-valine A124G mutant Streptomyces albus

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble soluble enzyme expressed in Escherichia coli Streptomyces albus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
2 * 38000, SDS-PAGE Streptomyces albus
67000
-
gel filtration Streptomyces albus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-valine + NAD(P)+ + H2O Streptomyces albus metabolic connection between valine catabolism and biosynthesis of macrolide or polyether antibiotics 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O Streptomyces albus first catabolic step of L-valine and some other branched chain L-amino acids, important role in providing precursors for biosynthesis of polyether antibiotic, salinomycin, that is produced at a high level 2-oxoisovalerate + NH3 + NAD(P)H
-
?

Organism

Organism UniProt Comment Textmining
Streptomyces albus
-
salinomycin producer
-

Purification (Commentary)

Purification (Comment) Organism
VDH and A124G mutant, His-bind resin column   Streptomyces albus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
activities of wild type and A124G mutant enzymes Streptomyces albus
21.16
-
L-valine Streptomyces albus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + H2O + NAD+ 3.75% of the activity with L-valine, A124G mutant: 0.063% Streptomyces albus 3-mercapto-2-oxopropanoate + NH3 + NADH
-
r
L-isoleucine + H2O + NAD+ 27.5% of the activity with L-valine, A124G mutant: 9.98% Streptomyces albus 3-methyl-2-oxopentanoate + NADH + NH3
-
r
L-leucine + H2O + NAD+ 15% of the activity with L-valine, A124G mutant: 5.03% Streptomyces albus 2-oxoisocaproate + NADH + NH3
-
r
L-norleucine + H2O + NAD+ 15% of the activity with L-valine, A124G mutant: 15% Streptomyces albus 2-oxocaproate + NADH + NH3
-
r
L-norvaline + H2O + NAD+ 100.5% of the activity of L-valine, A124G mutant: 28.77% Streptomyces albus 2-oxovalerate + NH3 + NADH
-
r
L-phenylalanine + H2O + NAD+ 1.25% of the activity with L-valine, A124G mutant: 2.5% Streptomyces albus 2-oxo-3-phenylpropanoic acid + NH3 + NADH
-
r
L-valine + NAD(P)+ + H2O NAD+ Streptomyces albus 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O NAD+ Streptomyces albus 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O A124G mutant: 3.75% of the activity with L-valine in wild type Streptomyces albus 2-oxoisovalerate + NH3 + NAD(P)H NADH r
L-valine + NAD(P)+ + H2O A124G mutant: 3.75% of the activity with L-valine in wild type Streptomyces albus 2-oxoisovalerate + NH3 + NAD(P)H 2-oxoisovalerate is identical with 3-methyl-2-oxobutanoate and alpha-ketoisovalerate r
L-valine + NAD(P)+ + H2O metabolic connection between valine catabolism and biosynthesis of macrolide or polyether antibiotics Streptomyces albus 2-oxoisovalerate + NH3 + NAD(P)H
-
?
L-valine + NAD(P)+ + H2O first catabolic step of L-valine and some other branched chain L-amino acids, important role in providing precursors for biosynthesis of polyether antibiotic, salinomycin, that is produced at a high level Streptomyces albus 2-oxoisovalerate + NH3 + NAD(P)H
-
?
additional information Lys-79, Lys-91 are involved in substrate binding and catalysis Streptomyces albus additional information
-
?
additional information Ala-124 is involved in substrate binding, but less of nicotinamide coenzyme Streptomyces albus additional information
-
?

Subunits

Subunits Comment Organism
dimer 2 * 38000, SDS-PAGE Streptomyces albus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Streptomyces albus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.7
-
L-valine A124G mutant Streptomyces albus
47.5
-
L-valine
-
Streptomyces albus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
reductive amination of 2-oxoisovalerate Streptomyces albus
8 8.5 reductive amination of 2-oxoisovalerate, 2-oxoisocaproate, 2-oxobutyrate, and DL-2-oxo-3-methylvalerate Streptomyces albus
10 10.5 oxidative deamination of L-valine, L-norvaline, L-leucine, and L-norleucine Streptomyces albus
10.5
-
oxidative deamination of L-valine Streptomyces albus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Streptomyces albus
NADH
-
Streptomyces albus