BRENDA - Enzyme Database show

Threonine-insensitive homoserine dehydrogenase from soybean: genomic organization, kinetic mechanism, and in vivo activity

Schroeder, A.C.; Zhu, C.; Yanamadala, S.R.; Cahoon, R.E.; Arkus, K.A.; Wachsstock, L.; Bleeke, J.; Krishnan, H.B.; Jez, J.M.; J. Biol. Chem. 285, 827-834 (2010)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.1.1.3
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
Glycine max
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.1.1.3
L-threonine
-
Glycine max
1.1.1.3
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
Glycine max
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1.1.3
0.028
-
NADPH
pH 8.0, 25C
Glycine max
1.1.1.3
0.034
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.039
-
NADPH
pH 8.0, 25C; pH 8.0, 25C
Glycine max
1.1.1.3
0.098
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
0.158
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
0.19
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
0.213
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
0.235
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.245
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.275
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.569
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
0.69
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.845
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
1.08
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
1.19
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
1.25
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
2.19
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
2.7
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
9.57
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
13.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
17.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
24.1
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
24.9
-
NAD+
pH 8.0, 25C
Glycine max
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.1.1.3
40000
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
1.1.1.3
40600
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
1.1.1.3
70000
-
gel filtration
Glycine max
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.1.1.3
Glycine max
O63067
bifunctional aspartokinase-homoserine dehydrogenase AK-HSD-2
-
1.1.1.3
Glycine max
O65027
bifunctional aspartokinase-homoserine dehydrogenase AK-HSD-1
-
1.1.1.3
Glycine max
Q3S3F6
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.1.1.3
recombinant enzyme; recombinant enzyme; recombinant enzyme
Glycine max
Reaction
EC Number
Reaction
Commentary
Organism
1.1.1.3
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
ordered bi bi kinetic mechanism in which nicotinamide cofactor binds first and leaves last in the reaction sequence
Glycine max
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.1.1.3
13
-
pH 8.0, 25C
Glycine max
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.3
L-aspartate 4-semialdehyde + NADH
-
712490
Glycine max
L-homoserine + NAD+
-
-
-
r
1.1.1.3
L-aspartate 4-semialdehyde + NADPH
-
712490
Glycine max
L-homoserine + NADP+
-
-
-
r
1.1.1.3
L-homoserine + NAD+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADH
-
-
-
r
1.1.1.3
L-homoserine + NADP+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
1.1.1.3
additional information
enzyme does not show aspartate kinase activity
712490
Glycine max
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
1.1.1.3
dimer
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.1.1.3
0.042
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.052
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.07
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
1.43
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
2.8
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
7
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
9.68
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
10.15
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
11.58
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
12.98
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
19.3
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
22.58
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.3
NADH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
1.1.1.3
NADPH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.1.1.3
160
240
L-threonine
pH 8.0, 25C
Glycine max
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.1.1.3
expression in Escherichia coli
Glycine max
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.3
NADH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
1.1.1.3
NADPH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
Glycine max
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.1.1.3
L-threonine
-
Glycine max
1.1.1.3
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
Glycine max
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.1.1.3
160
240
L-threonine
pH 8.0, 25C
Glycine max
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1.1.3
0.028
-
NADPH
pH 8.0, 25C
Glycine max
1.1.1.3
0.034
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.039
-
NADPH
pH 8.0, 25C
Glycine max
1.1.1.3
0.098
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
0.158
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
0.19
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
0.213
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
0.235
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.245
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.275
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.569
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
0.69
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.845
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
1.08
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
1.19
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
1.25
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
2.19
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
2.7
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
9.57
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
13.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
17.4
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
24.1
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
24.9
-
NAD+
pH 8.0, 25C
Glycine max
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.1.1.3
40000
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
1.1.1.3
40600
-
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
1.1.1.3
70000
-
gel filtration
Glycine max
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.1.1.3
recombinant enzyme
Glycine max
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.1.1.3
13
-
pH 8.0, 25C
Glycine max
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.3
L-aspartate 4-semialdehyde + NADH
-
712490
Glycine max
L-homoserine + NAD+
-
-
-
r
1.1.1.3
L-aspartate 4-semialdehyde + NADPH
-
712490
Glycine max
L-homoserine + NADP+
-
-
-
r
1.1.1.3
L-homoserine + NAD+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADH
-
-
-
r
1.1.1.3
L-homoserine + NADP+
-
712490
Glycine max
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
1.1.1.3
additional information
enzyme does not show aspartate kinase activity
712490
Glycine max
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.1.1.3
dimer
2 * 40600, calculated, 2 * 40000, SDS-PAGE
Glycine max
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.1.1.3
0.042
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.052
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.07
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
1.43
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
2.8
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
7
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
9.68
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
10.15
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
11.58
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
12.98
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
19.3
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
22.58
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.1.1.3
0.039
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.082
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
0.095
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.18
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.256
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.268
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.281
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
0.421
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
0.53
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
0.731
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
0.757
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
2.07
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
5.29
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
10.39
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
16.22
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
17.02
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
26.73
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
28.54
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
61.29
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
90.61
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
101.4
-
NADPH
pH 8.0, 25C
Glycine max
1.1.1.3
118.9
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
296.2
-
NADPH
pH 8.0, 25C
Glycine max
1.1.1.3
331.2
-
NADPH
pH 8.0, 25C
Glycine max
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.1.1.3
0.039
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.082
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
0.095
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.18
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.256
-
L-homoserine
cosubstrate NADP+, pH 8.0, 25C
Glycine max
1.1.1.3
0.268
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
0.281
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
0.421
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
0.53
-
NAD+
pH 8.0, 25C
Glycine max
1.1.1.3
0.731
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
0.757
-
L-homoserine
cosubstrate NAD+, pH 8.0, 25C
Glycine max
1.1.1.3
2.07
-
NADP+
pH 8.0, 25C
Glycine max
1.1.1.3
5.29
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
10.39
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
16.22
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
17.02
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
26.73
-
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25C
Glycine max
1.1.1.3
28.54
-
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25C
Glycine max
1.1.1.3
61.29
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
90.61
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
101.4
-
NADPH
pH 8.0, 25C
Glycine max
1.1.1.3
118.9
-
NADH
pH 8.0, 25C
Glycine max
1.1.1.3
296.2
-
NADPH
pH 8.0, 25C
Glycine max
1.1.1.3
331.2
-
NADPH
pH 8.0, 25C
Glycine max