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Literature summary extracted from

  • Schroeder, A.C.; Zhu, C.; Yanamadala, S.R.; Cahoon, R.E.; Arkus, K.A.; Wachsstock, L.; Bleeke, J.; Krishnan, H.B.; Jez, J.M.
    Threonine-insensitive homoserine dehydrogenase from soybean: genomic organization, kinetic mechanism, and in vivo activity (2010), J. Biol. Chem., 285, 827-834.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.3 expression in Escherichia coli Glycine max

Inhibitors

EC Number Inhibitors Comment 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 Comment Organism Structure
1.1.1.3 0.028
-
 NADPH pH 8.0, 25°C Glycine max
1.1.1.3 0.034
-
 NADP+ pH 8.0, 25°C Glycine max
1.1.1.3 0.039
-
 NADPH pH 8.0, 25°C Glycine max
1.1.1.3 0.098
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 0.158
-
 NADH pH 8.0, 25°C Glycine max
1.1.1.3 0.19
-
 NADH pH 8.0, 25°C Glycine max
1.1.1.3 0.213
-
 NADH pH 8.0, 25°C Glycine max
1.1.1.3 0.235
-
 NADP+ pH 8.0, 25°C Glycine max
1.1.1.3 0.245
-
 NADP+ pH 8.0, 25°C Glycine max
1.1.1.3 0.275
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 0.569
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 0.69
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 0.845
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 1.08
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 1.19
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 1.25
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 2.19
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 2.7
-
 NAD+ pH 8.0, 25°C Glycine max
1.1.1.3 9.57
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 13.4
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 17.4
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 24.1
-
 NAD+ pH 8.0, 25°C Glycine max
1.1.1.3 24.9
-
 NAD+ pH 8.0, 25°C Glycine max

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment 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 UniProt Comment 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 Purification (Comment) Organism
1.1.1.3 recombinant enzyme Glycine max

Reaction

EC Number Reaction Comment Organism Reaction ID
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
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.3 13
-
 pH 8.0, 25°C Glycine max

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.3 L-aspartate 4-semialdehyde + NADH
-
 Glycine max L-homoserine + NAD+
-
 r
1.1.1.3 L-aspartate 4-semialdehyde + NADPH
-
 Glycine max L-homoserine + NADP+
-
 r
1.1.1.3 L-homoserine + NAD+
-
 Glycine max L-aspartate 4-semialdehyde + NADH
-
 r
1.1.1.3 L-homoserine + NADP+
-
 Glycine max L-aspartate 4-semialdehyde + NADPH
-
 r
1.1.1.3 additional information enzyme does not show aspartate kinase activity Glycine max ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.3 dimer 2 * 40600, calculated, 2 * 40000, SDS-PAGE Glycine max

Synonyms

EC Number Synonyms Comment Organism
1.1.1.3 AK-HSD-1
-
 Glycine max

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.3 0.042
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 0.052
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 0.07
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 1.43
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 2.8
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 7
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 9.68
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 10.15
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 11.58
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 12.98
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 19.3
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 22.58
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max

Cofactor

EC Number Cofactor Comment 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 Comment Organism Structure
1.1.1.3 160 240 L-threonine pH 8.0, 25°C Glycine max

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.3 0.039
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 0.082
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 0.095
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 0.18
-
 NADP+ pH 8.0, 25°C Glycine max
1.1.1.3 0.256
-
 L-homoserine cosubstrate NADP+, pH 8.0, 25°C Glycine max
1.1.1.3 0.268
-
 NADP+ pH 8.0, 25°C Glycine max
1.1.1.3 0.281
-
 NAD+ pH 8.0, 25°C Glycine max
1.1.1.3 0.421
-
 NAD+ pH 8.0, 25°C Glycine max
1.1.1.3 0.53
-
 NAD+ pH 8.0, 25°C Glycine max
1.1.1.3 0.731
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 0.757
-
 L-homoserine cosubstrate NAD+, pH 8.0, 25°C Glycine max
1.1.1.3 2.07
-
 NADP+ pH 8.0, 25°C Glycine max
1.1.1.3 5.29
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 10.39
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 16.22
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 17.02
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 26.73
-
 L-aspartate 4-semialdehyde cosubstrate NADH, pH 8.0, 25°C Glycine max
1.1.1.3 28.54
-
 L-aspartate 4-semialdehyde cosubstrate NADPH, pH 8.0, 25°C Glycine max
1.1.1.3 61.29
-
 NADH pH 8.0, 25°C Glycine max
1.1.1.3 90.61
-
 NADH pH 8.0, 25°C Glycine max
1.1.1.3 101.4
-
 NADPH pH 8.0, 25°C Glycine max
1.1.1.3 118.9
-
 NADH pH 8.0, 25°C Glycine max
1.1.1.3 296.2
-
 NADPH pH 8.0, 25°C Glycine max
1.1.1.3 331.2
-
 NADPH pH 8.0, 25°C Glycine max