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DL-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NADH
L-homoserine + NAD+
-
-
r
L-aspartate 4-semialdehyde + NADH + H+
L-homoserine + NAD+
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
additional information
?
-
L-aspartate 4-semialdehyde + NAD(P)H

L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
essential step in amino acids L-methionine, L-threonine, and L-isoleucine biosynthesis
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
Thermophilic bacterium
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NADPH

L-homoserine + NADP+
-
-
-
?
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
part of the aspartate pathway of amino acid biosynthesis
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
-
r
L-aspartate 4-semialdehyde + NADPH + H+

L-homoserine + NADP+
-
-
-
?
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
-
-
-
?
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
-
-
-
r
L-homoserine + NAD(P)+

L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
?
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
Thermophilic bacterium
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+

L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
r
L-homoserine + NAD+

L-aspartate 4-semialdehyde + NADH + H+
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
r
L-homoserine + NADP+

L-aspartate 4-semialdehyde + NADPH
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
?
L-homoserine + NADP+

L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
additional information

?
-
enzyme does not show aspartate kinase activity
-
?
additional information
?
-
enzyme does not show aspartate kinase activity
-
?
additional information
?
-
enzyme does not show aspartate kinase activity
-
?
additional information
?
-
-
enzyme does not show aspartate kinase activity
-
?
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(2S)-2-[[4-(propan-2-yl)phenyl]sulfanyl]propanenitrile
-
(S)-2-amino-4-oxo-5-hydroxypentanoic acid
-
RI-331
1-tert-butyl-4-[(difluoromethyl)sulfanyl]benzene
-
1-[(1S,2S)-2-(bromomethyl)cyclopropyl]-4-[(trifluoromethyl)sulfanyl]benzene
-
2,2'-[thiobis[[2-(1,1-dimethylethyl)-5-methyl-4,1-phenylene]oxy]]bis-acetic acid diethyl ester
-
-
3-[(4-tert-butylphenyl)sulfanyl]propane-1-thiol
-
4,4'-sulfanediylbis[2-(propan-2-yl)phenol]
-
4,4'-thiobis[2-(1,1-dimethylethyl)]-5-methyl-phenol
-
-
4,4'-thiobis[2-(1,1-dimethylethyl)]-phenol
-
-
4,4'-thiobis[2-(1-methylethyl)]-phenol
-
-
4,4'-thiobis[5-methyl-2-(1-methylethyl)]-phenol
-
-
4,4'-[1,2-ethanediylbis(thio)]bis[2,6-bis(1-methylpropyl)]-phenol
-
-
4,4'-[1,2-ethanediylbis(thio)]bis[2-(1,1-dimethylethyl)-6-methyl]-phenol
-
-
4-(1-methylheptyl)-1,3-benzenediol
-
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
competitive to L-aspartate 4-semialdehyde, enzyme binding structure anaysis from crystal structure, overview
4-[[2-(2-furanyl)ethyl]thio]-phenol
-
-
4-[[[4-(1,1-dimethylethyl)phenyl]thio]methyl]-2,6-bis(1-methylethyl)-phenol
-
-
bis(4-chlorophenyl)ethyloxiranyl-silane
-
-
D-threonine
Thermophilic bacterium
-
slight
DL-allo-threonine
Thermophilic bacterium
-
-
H-(1,2,4-triazol-3-yl)-DL-alanine
-
-
L-lysine
allosteric regulation of recombinant engineered homoserine dehydrogenase by nonnatural inhibitor L-lysine
p-chloromercuribenzoate
-
-
[2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid ethyl ester
-
-
L-cysteine

-
-
L-cysteine
-
slight inhibition of chloroplast isozyme, strong inhibition of cytoplasmic isozyme
L-cysteine
-
slight inhibition of chloroplast isozyme, strong inhibition of cytoplasmic isozyme
L-cysteine
Thermophilic bacterium
-
slight
L-serine

-
-
L-serine
allosteric inhibitor
L-threonine

strong inhibition of both enzyme activities, aspartate dehydrogenase and aspartate kinase activity, by decreasing the affinity of the enzyme for substrate and cofactors, kinetic effects
L-threonine
-
the regulatory domain of the enzyme contains 2 binding sites, interaction with Gln443 leads to inhibition of the aspartate kinase activity and facilitates the binding of a second threonine on Gln524 leading to inhibition of the homoserine dehydrogenase activity, inhibition of the forward reactions
L-threonine
the enzyme activity is subjected to feedback regulation by L-threonine
L-threonine
the natural threonine binding sites of the enzyme are predicted and verified by mutagenesis experiments
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
L-threonine
-
sensitive and insensitive isozymes
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
L-threonine
-
weakly inhibits reverse but not forward reaction
L-threonine
allosteric inhibitor
L-threonine
Thermophilic bacterium
-
-
L-threonine
-
not inhibitory
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
methionine

-
-
methionine
-
weakly inhibits reverse but not forward reaction
NADP+

-
-
NADP+
NADP+ does not act as a cofactor for this enzyme, but as a strong inhibitor of NAD+-dependent oxidation of Hse, evaluation of the factors responsible for the NADP+-mediated inhibition
Thr

-
-
Thr
-
90% inhibition of homoserine dehydrogenase 2 at 10 mM
threonine

-
feedback inhibition, one isozyme is resistant and another is sensitive to threonine inhibition, 46.9% inhibition at 1 mM, 63.9% at 5 mM
threonine
-
the methionine-producing strain contains a deregulated homoserine dehydrogenase that is not sensitive to feedback inhibition as the wild-type enzyme
additional information

-
Lys, Met, and S-2-aminoethyl-L-cysteine do not affect HSDH activity at 1-5 mM
-
additional information
the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
-
additional information
-
the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
-
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
-
Thr does not inhibit homoserine dehydrogenase 1
-
additional information
inhibitor docking study, overview
-
additional information
-
no inhibition by [2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid and 4-amino-butyric acid 2-tert-butyl-4-(3-tert-butyl-4-hydroxy-phenylsulfanyl)-phenyl ester
-
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0.04
aspartate 4-semialdehyde
-
isozyme II
5.5
ATP
pH 8.0, 37°C, purified recombinant soluble enzyme
0.1
DL-aspartate 4-semialdehyde
-
-
11.6
L-aspartate
pH 8.0, 37°C, purified recombinant soluble enzyme
0.066 - 2.19
L-aspartate 4-semialdehyde
0.013 - 17.4
L-homoserine
additional information
additional information
-
0.066
L-aspartate 4-semialdehyde

-
isozyme I
0.08
L-aspartate 4-semialdehyde
-
threonine insensitive isozyme
0.098
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
0.1
L-aspartate 4-semialdehyde
-
isozyme I
0.13 - 0.15
L-aspartate 4-semialdehyde
-
threonine resistant isozyme
0.15
L-aspartate 4-semialdehyde
-
threonine resistant isozyme
0.15
L-aspartate 4-semialdehyde
-
threonine-resistant enzyme, pH and temperature not specified in the publication
0.17
L-aspartate 4-semialdehyde
-
-
0.24 - 0.25
L-aspartate 4-semialdehyde
-
threonine sensitive isozyme
0.25
L-aspartate 4-semialdehyde
-
threonine sensitive isozyme
0.25
L-aspartate 4-semialdehyde
-
threonine-sensitive enzyme, pH and temperature not specified in the publication
0.36 - 0.4
L-aspartate 4-semialdehyde
-
isozyme II
0.5
L-aspartate 4-semialdehyde
-
-
0.5
L-aspartate 4-semialdehyde
-
threonine sensitive isozyme
0.569
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
0.845
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
1.19
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
1.25
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
2.19
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
0.013
L-homoserine

-
-
0.21
L-homoserine
pH 8.0, 30°C, oxidized enzyme
0.275
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
0.41
L-homoserine
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity
0.54
L-homoserine
pH 8.0, 30°C, reduced enzyme
0.68
L-homoserine
-
recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity
0.69
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
1.08
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
1.2
L-homoserine
-
recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity
5.2
L-homoserine
pH 8.0, 37°C, purified recombinant soluble enzyme
6.1
L-homoserine
pH 9.0, 50°C, recombinant enzyme
9.57
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
13.4
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
17.2
L-homoserine
-
recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity
17.4
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
0.05
NAD+

pH 9.0, 50°C, recombinant mutant K57A
0.31
NAD+
pH 8.0, 30°C, oxidized enzyme
0.32
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
0.33
NAD+
pH 8.0, 30°C, reduced enzyme
0.95
NAD+
pH 9.0, 50°C, recombinant mutant R40A
0.158
NADH

pH 8.0, 25°C
0.46
NADH
-
isoenzyme II, at pH 7.5, temperature not specified in the publication
0.034
NADP+

pH 8.0, 25°C
0.04
NADP+
pH 9.0, 50°C, recombinant mutant R40A
0.06
NADP+
pH 9.0, 50°C, recombinant mutant K57A
0.166
NADP+
pH 8.0, 37°C, purified recombinant soluble enzyme
0.17 - 0.18
NADP+
Thermophilic bacterium
-
-
0.235
NADP+
pH 8.0, 25°C
0.245
NADP+
pH 8.0, 25°C
0.027
NADPH

-
isozyme II
0.028
NADPH
pH 8.0, 25°C
0.031
NADPH
-
threonine sensitive isozyme
0.032 - 0.036
NADPH
-
threonine resistant isozyme
0.036
NADPH
-
threonine resistant isozyme
0.036
NADPH
-
threonine-resistant enzyme, pH and temperature not specified in the publication
0.039
NADPH
pH 8.0, 25°C
0.04
NADPH
-
threonine sensitive isozyme
0.04
NADPH
-
threonine-sensitive enzyme, pH and temperature not specified in the publication
0.043
NADPH
-
threonine sensitive isozyme
additional information
additional information

kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
enzyme HseDH shows typical Michaelis-Menten kinetics for oxidation
-
additional information
additional information
kinetic profile
-
additional information
additional information
-
kinetic profile
-
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evolution

the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
evolution
-
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
malfunction

HOM6 deletions cause translational arrest in cells grown under amino acid starvation conditions. HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices. HOM6-homozygous mutants are hypersensitive to hygromycin B and cycloheximide as compared with wild-type, HOM6-heterozygous, and HOM6-reintegrated strains. HOM6 deletion affects translation and leads to the accumulation of free ribosomes
malfunction
-
HOM6 deletions cause translational arrest in cells grown under amino acid starvation conditions. HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices. HOM6-homozygous mutants are hypersensitive to hygromycin B and cycloheximide as compared with wild-type, HOM6-heterozygous, and HOM6-reintegrated strains. HOM6 deletion affects translation and leads to the accumulation of free ribosomes
metabolism

homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine
metabolism
homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine
metabolism
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine
metabolism
homoserine dehydrogenase is a key enzyme in the L-threonine pathway
metabolism
-
homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine
metabolism
-
homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine
metabolism
-
homoserine dehydrogenase is a key enzyme in the L-threonine pathway
metabolism
-
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine
physiological function

contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol
physiological function
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
physiological function
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine
physiological function
the enzyme is involved in cell-wall maintenance and essential amino acid biosynthesis. Homoserine dehydrogenase catalyzes a reaction at the branch point of the pathway leading to lysine biosynthesis. This pathway is also referred to as the diaminopimelate (dap) pathway
physiological function
the enzyme is naturally allosterically regulated by threonine and isoleucine
physiological function
-
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine
physiological function
-
the enzyme is involved in cell-wall maintenance and essential amino acid biosynthesis. Homoserine dehydrogenase catalyzes a reaction at the branch point of the pathway leading to lysine biosynthesis. This pathway is also referred to as the diaminopimelate (dap) pathway
physiological function
-
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
physiological function
-
contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol
additional information

structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
additional information
structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207
additional information
-
structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
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Q443A
-
site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, asparate kinase activity is completely insensitive to inhibition by L-threonine, overview
Q524A
-
site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, overview
G378E
-
feedback resistance of the enzyme
L200F
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 degree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
L200F/D215A
-
site-directed mutagenesis
L200F/D215E
-
site-directed mutagenesis
L200F/D215G
-
site-directed mutagenesis
L200F/D215K
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 dgree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
L200F
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 degree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
L200F/D215A
-
site-directed mutagenesis
L200F/D215E
-
site-directed mutagenesis
L200F/D215G
-
site-directed mutagenesis
L200F/D215K
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 dgree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
K57Aa
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme
R40A
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is decreased compared to the wild-type enzyme
K57Aa
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme
R40A
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is decreased compared to the wild-type enzyme
H309A
decrease of catalytic activity and elimination of substrate inhibition
K105A
site-directed double-primer PCR mutagenesis
K105R
site-directed double-primer PCR mutagenesis
K205A
site-directed double-primer PCR mutagenesis
K105A
-
site-directed double-primer PCR mutagenesis
K105R
-
site-directed double-primer PCR mutagenesis
K205A
-
site-directed double-primer PCR mutagenesis
G378S

construction of a homoserine dehydrogenase mutant HDG378S, encoded by hom1, in Corynebacterium glutamicum strain IWJ001, one of the best L-isoleucine producing strains. Strain HDG378S is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. Overexpression of lysC1, hom1 and thrB1 increased L-threonine and L-lysine production in Corynebacterium glutamicum ATCC13869 by 96folds and 21.2folds, respectively, overview
G378S
-
construction of a homoserine dehydrogenase mutant HDG378S, encoded by hom1, in Corynebacterium glutamicum strain IWJ001, one of the best L-isoleucine producing strains. Strain HDG378S is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. Overexpression of lysC1, hom1 and thrB1 increased L-threonine and L-lysine production in Corynebacterium glutamicum ATCC13869 by 96folds and 21.2folds, respectively, overview
additional information

-
construction of transgenic Arabidopsis thaliana plants by transformation with gene akthr2 via Agrobacterium tumefaciens infection, determination of expression patterns of the gene akthr1 ans akthr2 in the transgenic plants
additional information
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
additional information
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
additional information
-
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
additional information
-
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
additional information
generation of HOM6-deleted (HOM6/hom6DELT and hom6DELTA/hom6DELTA) and HOM6-reintegrated (hom6DELTA/hom6DELTA::HOM6 and hom6DELTA::HOM6/hom6DELTA::HOM6) strains
additional information
-
generation of HOM6-deleted (HOM6/hom6DELT and hom6DELTA/hom6DELTA) and HOM6-reintegrated (hom6DELTA/hom6DELTA::HOM6 and hom6DELTA::HOM6/hom6DELTA::HOM6) strains
additional information
-
generation of HOM6-deleted (HOM6/hom6DELT and hom6DELTA/hom6DELTA) and HOM6-reintegrated (hom6DELTA/hom6DELTA::HOM6 and hom6DELTA::HOM6/hom6DELTA::HOM6) strains
additional information
-
engineering of a Corynebacterium glutamicum strain HL1049 for effective production of methionine by elimination of the threonine synthesis gene and desensitizing the homoserine dehydrogenase versus inhibition by threonine, analysis of the amino acid spectrum of the engineered strain, overview
additional information
design of an artificial allosteric enzyme to sense an unnatural signal for a precise and dynamical control of fluxes of growth-essential but byproduct pathways in metabolic engineering of industrial microorganisms. The natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
additional information
-
design of an artificial allosteric enzyme to sense an unnatural signal for a precise and dynamical control of fluxes of growth-essential but byproduct pathways in metabolic engineering of industrial microorganisms. The natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
additional information
releasing the enzymes of the L-threonine biosynthesis pathway from feedback control and coordinating their expression plays a pivotal role in engineering Corynebacterium glutamicum into L-isoleucine producers, construction of transgenic Corynebacterium glutamicum with deregulated L-threonine biosynthesis pathway enzymes for enhanced L-isoleucine biosynthesis
additional information
-
releasing the enzymes of the L-threonine biosynthesis pathway from feedback control and coordinating their expression plays a pivotal role in engineering Corynebacterium glutamicum into L-isoleucine producers, construction of transgenic Corynebacterium glutamicum with deregulated L-threonine biosynthesis pathway enzymes for enhanced L-isoleucine biosynthesis
additional information
-
releasing the enzymes of the L-threonine biosynthesis pathway from feedback control and coordinating their expression plays a pivotal role in engineering Corynebacterium glutamicum into L-isoleucine producers, construction of transgenic Corynebacterium glutamicum with deregulated L-threonine biosynthesis pathway enzymes for enhanced L-isoleucine biosynthesis
additional information
-
construction of a hybrid enzyme AKIII-HDHI+ by fusing a wild-type monofunctional aspartate kinase AKIII enzyme to the thrA2+ gene, encoding the homoserine dehydrogenase including the interface region of the wild-type bifunctional enzyme, the hybrid enzyme shows highly improved kinetic properties for homoserine dehydrogenase activity, and is not sensitive to L-threonine inhibition
additional information
-
mutant strain M20-20D is deficient in gene HOM6 and shows no activity, the defect can be complemented by recombinant expression of the Arabidopsis thaliana gene akthr2 in the mutant yeast cells
additional information
construction of a hom disruption mutant by insertional inactivation via double crossover leading to up to 4.3fold and 2fold increases in intracellular free L-lysine concentration and specific cephamycin C production, respectively, during stationary phase in chemically defined medium, overview
additional information
-
construction of a hom disruption mutant by insertional inactivation via double crossover leading to up to 4.3fold and 2fold increases in intracellular free L-lysine concentration and specific cephamycin C production, respectively, during stationary phase in chemically defined medium, overview
additional information
-
construction of a hom disruption mutant by insertional inactivation via double crossover leading to up to 4.3fold and 2fold increases in intracellular free L-lysine concentration and specific cephamycin C production, respectively, during stationary phase in chemically defined medium, overview
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