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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+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
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 + 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+
-
-
-
?
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+
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation
-
-
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+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
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+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
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+
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
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+
-
-
-
?
L-homoserine + NADP+
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+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
additional information
?
-
enzyme BsHSD exclusively prefers NADP+ to NAD+
-
-
-
additional information
?
-
-
enzyme BsHSD exclusively prefers NADP+ to NAD+
-
-
-
additional information
?
-
enzyme BsHSD exclusively prefers NADP+ to NAD+
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase activity, EC 2.7.2.4
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase activity, EC 2.7.2.4
-
-
-
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
-
-
?
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
substrates binding modes, overview
-
-
-
additional information
?
-
-
substrates binding modes, overview
-
-
-
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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
4-[[2-(2-furanyl)ethyl]thio]-phenol
-
-
4-[[[4-(1,1-dimethylethyl)phenyl]thio]methyl]-2,6-bis(1-methylethyl)-phenol
-
-
5-hydroxy-4-oxo-L-norvaline
HONV, the mechanism of antifungal action of HONV dipeptides (determined against Candida albicans strain ATCC 10231 cells in three different growth media) involves uptake by the oligopeptide transport system, subsequent intracellular cleavage by cytosolic peptidases, and inhibition of homoserine dehydrogenase by the released HONV. Chemical synthesis of HONV and construction of HONV dipeptides as potential antifungal agents, overview. Six dipeptides with L-alanine, L-valine, L-norvaline (Nva), L-leucine, L-isoleucine, and L-phenylalanine as the N-terminal residues are obtained, Gly-HONV and D-Leu-HONV are synthesized and evaluated for comparative purposes. Antifungal in vitro activity and MIC values of HONV and its dipeptides, overview. Activity of HONV strongly depends on growth medium composition. Dipeptide (S)-2-N-[(R)-leucyl]amino-5-hydroxy-4-oxopentanoic acid (D-Leu-HONV) is inactive in all growth media. Antifungal activity of the compounds against different Candida species. Lack of activity of HONV-containing dipeptides against the Candida albicans opt1-opt5DELTA ptr2DELTA ptr22DELTA mutant clearly indicates that these compounds are transported to Candida albicans cells by the oligopeptide transport system, most probably by the di-tripeptide permeases Ptr2p and Ptr22, uptake rates into Candida albicans strain ATCC 10231 cells at pH 5.0 and pH 7.0 are determined, the initial uptake velocities are generally higher at pH 5.0 than at pH 7.0
bis(4-chlorophenyl)ethyloxiranyl-silane
-
-
D-threonine
Thermophilic bacterium
-
slight
DL-allo-threonine
Thermophilic bacterium
-
-
glycyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-glycylamino-5-hydroxy-4-oxopentanoic acid
H-(1,2,4-triazol-3-yl)-DL-alanine
-
-
L-alanyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-alanyl]amino-5-hydroxy-4-oxopentanoic acid
L-isoleucyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-isoleucyl]amino-5-hydroxy-4-oxopentanoic acid
L-leucyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-leucyl]amino-5-hydroxy-4-oxopentanoic acid
L-lysine
allosteric regulation of recombinant engineered homoserine dehydrogenase by nonnatural inhibitor L-lysine
L-norvalyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-norvalyl]amino-5-hydroxy-4-oxopentanoic acid
L-phenylalanyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-phenylalanyl]amino-5-hydroxy-4-oxopentanoic acid
L-valyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-valyl]amino-5-hydroxy-4-oxopentanoic acid
NADH
acts as a competitive inhibitor of NAD+, product inhibition, non-competitive inhibition versus L-homoserine
p-chloromercuribenzoate
-
-
Zinc15967722
MIC/MCF is 0.032 mg/ml
Zinc20611644
MIC/MCF is 0.128 mg/ml
Zinc2123137
MIC/MCF is 0.008 mg/ml
[2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid ethyl ester
-
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
competitive to L-aspartate 4-semialdehyde, enzyme binding structure anaysis from crystal structure, overview
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
-
Amphotericin B
MIC value against strain Pb18 is 0.12 mg/ml
Amphotericin B
MIC value against strain Pb18 is 0.06 mg/ml
itraconazole
MIC value against strain Pb18 is 0.007 mg/ml
itraconazole
MIC value against strain Pb18 is 0.007 mg/ml
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
competitive versus L-homoserine, uncompetitive versus cofactors NAD+ and NADP+. 95% inhibition at 10 mM. The feedback inhibition of StHSD by cysteine occurs through the formation of an enzyme-NAD-cysteine complex. Cysteine situates within the homoserine binding site, formation of a covalent bond between cysteine and the nicotinamide ring. Cysteine interacts with six residues (Gly156, Thr157, Tyr183, Glu185, Asp191, and Lys200) in the StHSD active site, binding structure analysis, overview
L-cysteine
Thermophilic bacterium
-
slight
L-serine
-
-
L-serine
allosteric inhibitor
L-serine
14% inhibition at 10 mM
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
Zinc203432
MIC value is 0.032 mg/ml
Zinc203432
MIC value is 0.064 mg/ml
Zinc273730
MIC value is 0.064 mg/ml
Zinc273730
MIC value is 0.064. Zinc273730 makes important contacts with Gly215, Tyr216, Thr217, and Glu218
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
L-homoserine inhibits the activity of aspartokinase encoded by metL
-
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
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Synergistic effects of HS1 and HS2 in combination with itraconazole against Paracoccidioides brasiliensis. Zinc1531037 and Zinc52986906 are not inhibitory
-
additional information
-
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Synergistic effects of HS1 and HS2 in combination with itraconazole against Paracoccidioides brasiliensis. Zinc1531037 and Zinc52986906 are not inhibitory
-
additional information
PbHSD inhibitor screening using the Zinc library, molecular dynamics simulations of PbHSD and ligand docking, electrostatic contacts between protein residues and the respective ligand atoms, overview. The selected ligands remain bound to the protein by a common mechanism throughout the simulation. Cytotoxicity evaluation in HeLa and Vero cells
-
additional information
-
PbHSD inhibitor screening using the Zinc library, molecular dynamics simulations of PbHSD and ligand docking, electrostatic contacts between protein residues and the respective ligand atoms, overview. The selected ligands remain bound to the protein by a common mechanism throughout the simulation. Cytotoxicity evaluation in HeLa and Vero cells
-
additional information
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 Molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Zinc1531037 and Zinc52986906 are not inhibitory
-
additional information
-
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 Molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Zinc1531037 and Zinc52986906 are not inhibitory
-
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
-
additional information
tHSD is poorly inhibited by less than 5% by 10 mM L-methionine, L-isoleucine, or L-threonine, all of which are final products in the aspartate pathway, and by L-lysine
-
additional information
-
tHSD is poorly inhibited by less than 5% by 10 mM L-methionine, L-isoleucine, or L-threonine, all of which are final products in the aspartate pathway, and by L-lysine
-
additional information
L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine, while L-threonine inhibits AK activity in a cooperative manner. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine
-
additional information
-
L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine, while L-threonine inhibits AK activity in a cooperative manner. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine
-
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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 - 35.08
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
-
-
0.2
L-homoserine
pH 10.0, 50°C, recombinant enzyme, with NADP+
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
1.08
L-homoserine
pH 9.5, 50°C, recombinant enzyme, with NAD+
1.2
L-homoserine
-
recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity
1.81
L-homoserine
recombinant enzyme, pH 10.5, 55°C
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
35.08
L-homoserine
pH 9.0, 25°C, recombinant enzyme
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
0.74
NAD+
pH 9.5, 50°C, recombinant 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
0.039
NADP+
pH 9.0, 25°C, recombinant enzyme
0.04
NADP+
pH 9.0, 50°C, recombinant mutant R40A
0.06
NADP+
pH 9.0, 50°C, recombinant mutant K57A
0.064
NADP+
recombinant enzyme, pH 10.5, 55°C
0.11
NADP+
pH 10.0, 50°C, recombinant enzyme
0.166
NADP+
pH 8.0, 37°C, purified recombinant soluble enzyme
0.17 - 0.18
NADP+
Thermophilic bacterium
-
-
0.027
NADPH
-
isozyme II
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
0.04
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
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state 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
-
additional information
additional information
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation, Michaelis-Menten kinetics, overview
-
additional information
additional information
-
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation, Michaelis-Menten kinetics, overview
-
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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
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
evolution
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
evolution
structure-function analysis and comparisons
evolution
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
evolution
-
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
-
evolution
-
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
-
evolution
-
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
-
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 orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
-
evolution
-
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
-
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
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
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
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
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
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
metabolism
homoserine dehydrogenase (HSD) catalyzes the reversible conversion of L-aspartate-4-semialdehyde to L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine
metabolism
-
homoserine dehydrogenase (HSD) catalyzes the reversible conversion of L-aspartate-4-semialdehyde to L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine
-
metabolism
-
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
-
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
-
metabolism
-
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
-
metabolism
-
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
-
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
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
physiological function
homoserine dehydrogenase (HSD) is an important regulatory enzyme in the aspartate pathway, which mediates synthesis of methionine, threonine and isoleucine from aspartate
physiological function
the homoserine dehydrogenase enzyme is essentially required for the biosynthesis of methionine, threonine, and isoleucine in fungi
physiological function
-
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
-
physiological function
-
homoserine dehydrogenase (HSD) is an important regulatory enzyme in the aspartate pathway, which mediates synthesis of methionine, threonine and isoleucine from aspartate
-
physiological function
-
the homoserine dehydrogenase enzyme is essentially required for the biosynthesis of methionine, threonine, and isoleucine in fungi
-
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
-
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
-
physiological function
-
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
-
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
binding of L-Hse and NADPH induces the conformational changes of TtHSD from an open to a closed form: the mobile loop containing Glu180 approaches to fix L-Hse and NADPH, and both Lys99 and Lys195 make hydrogen bonds with the hydroxy group of L-Hse. The ternary complex of TtHSDs in the closed form mimicks a Michaelis complex better than the previously reported open form structures from other species. Lys99 seems to be the acidx02base catalytic residue of HSD. The substrate L-Hse and the nicotinamide-ribose moiety of the cofactor NADPH are bound to a crevice formed at the interface between the substrate and nucleotide binding domains. In contrast, the adenosine group of NADPH is located at the surface of the enzyme. The open-closed conformational change may play an important role in the formation of the enzymex02substrate-cofactor complex and subsequent enzymatic catalysis
additional information
-
binding of L-Hse and NADPH induces the conformational changes of TtHSD from an open to a closed form: the mobile loop containing Glu180 approaches to fix L-Hse and NADPH, and both Lys99 and Lys195 make hydrogen bonds with the hydroxy group of L-Hse. The ternary complex of TtHSDs in the closed form mimicks a Michaelis complex better than the previously reported open form structures from other species. Lys99 seems to be the acidx02base catalytic residue of HSD. The substrate L-Hse and the nicotinamide-ribose moiety of the cofactor NADPH are bound to a crevice formed at the interface between the substrate and nucleotide binding domains. In contrast, the adenosine group of NADPH is located at the surface of the enzyme. The open-closed conformational change may play an important role in the formation of the enzymex02substrate-cofactor complex and subsequent enzymatic catalysis
additional information
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
additional information
structure homology modeling of enzyme with bound substrate NAD+ and L-homoserine using the Saccharomyces cerevisiae enzyme (PDB ID 1EBU) as template, binding analysis, overview. The model with the best output is subjected to gradient minimization, redocking, and molecular dynamics simulation
additional information
-
structure homology modeling of enzyme with bound substrate NAD+ and L-homoserine using the Saccharomyces cerevisiae enzyme (PDB ID 1EBU) as template, binding analysis, overview. The model with the best output is subjected to gradient minimization, redocking, and molecular dynamics simulation
additional information
three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview
additional information
-
three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
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
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
structure homology modeling of enzyme with bound substrate NAD+ and L-homoserine using the Saccharomyces cerevisiae enzyme (PDB ID 1EBU) as template, binding analysis, overview. The model with the best output is subjected to gradient minimization, redocking, and molecular dynamics simulation
-
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
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
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hexamer
in absence of L-threonine
homopentamer or homohexamer
?
x * 35492, sequence calculation
?
-
x * 85000, SDS-PAGE, threonine sensitive isozyme
dimer
2 * 40600, calculated, 2 * 40000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits
dimer
-
StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits
-
dimer
-
2 * 38000, SDS-PAGE, threonine resistant isozyme
dimer
-
x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme
homodimer
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
homodimer
-
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
-
homodimer
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
homodimer
-
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
-
homodimer
dimeric enzyme structure, overview
homodimer
-
dimeric enzyme structure, overview
-
homopentamer or homohexamer
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
homopentamer or homohexamer
-
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
-
homopentamer or homohexamer
-
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
-
homopentamer or homohexamer
-
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
-
tetramer
in presence of L-threonine
tetramer
4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE
tetramer
-
4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE
-
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme
additional information
-
primary and secondary structure comparison, the bifunctional enzyme contains 2 homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif, the enzymes' regulatory domain is composed of 2 subdomains, amino acid residues 414-453 and 495-534
additional information
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
additional information
-
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
additional information
-
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
-
additional information
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
additional information
-
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
-
additional information
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
-
additional information
enzyme TtHSD folds into a dimer with a noncrystallographic 2fold axis. The subunit comprises three conserved domains of HSDs and a flexible tail at the C-terminus. The nucleotide-binding domain (residues 1-119 and 288-309) assumes an alpha/beta Rossmann fold with five beta-strands and four alpha-helices. The dimerization domain (residues 120-140 and 261-287) comprises two alpha-helices and two beta-strands that interact with the corresponding domain of the other subunit of the dimer to form an alpha/beta structure with the four-stranded beta-sheet. The substrate-binding domain (residues 141-260) comprises four beta-strands and five alpha-helices. The flexible tail at the C-terminus (310-332) extends from the nucleotide-binding domain to the substrate-binding domain
additional information
-
enzyme TtHSD folds into a dimer with a noncrystallographic 2fold axis. The subunit comprises three conserved domains of HSDs and a flexible tail at the C-terminus. The nucleotide-binding domain (residues 1-119 and 288-309) assumes an alpha/beta Rossmann fold with five beta-strands and four alpha-helices. The dimerization domain (residues 120-140 and 261-287) comprises two alpha-helices and two beta-strands that interact with the corresponding domain of the other subunit of the dimer to form an alpha/beta structure with the four-stranded beta-sheet. The substrate-binding domain (residues 141-260) comprises four beta-strands and five alpha-helices. The flexible tail at the C-terminus (310-332) extends from the nucleotide-binding domain to the substrate-binding domain
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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
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G433R
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
P458S
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
G433R
-
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
-
P458S
-
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
-
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
-
K195A
site-directed mutagenesis, inactive mutant. In the crystal structure, the positions of Lys195 and L-Hse are significantly retained with those of the wild-type enzyme, enzyme crystal structure analysis
K99A
site-directed mutagenesis, inactive mutant. In the crystal structure, the productive geometry of the ternary complex is almost preserved with one new water molecule taking over the hydrogen bonds associated with Lys99, mutant enzyme crystal structure analysis
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
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additional information
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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
generation of a knockout homoserine dehydrogenase (HSD) mutant by chemical mutagenesis. Auxotrophic mutant formed from ddh gene, encoding diaminopimelate dehydrogenase, recombinantly expressed in Corynebacterium glutamicum strain ATCC 13032 with blocked HSD shows increased yield of L-lysine of 24.89 g/l compared to ddh gene expressed in wild-type strain ATCC 13032 (20.66 g/l of L-lysine). The maximum yield of L-lysine for the auxotrophic mutant is attained at pH 7.5 and 30°C after 96 h incubation time. Method optimization, overview
additional information
-
generation of a knockout homoserine dehydrogenase (HSD) mutant by chemical mutagenesis. Auxotrophic mutant formed from ddh gene, encoding diaminopimelate dehydrogenase, recombinantly expressed in Corynebacterium glutamicum strain ATCC 13032 with blocked HSD shows increased yield of L-lysine of 24.89 g/l compared to ddh gene expressed in wild-type strain ATCC 13032 (20.66 g/l of L-lysine). The maximum yield of L-lysine for the auxotrophic mutant is attained at pH 7.5 and 30°C after 96 h incubation time. Method optimization, overview
-
additional information
-
generation of a knockout homoserine dehydrogenase (HSD) mutant by chemical mutagenesis. Auxotrophic mutant formed from ddh gene, encoding diaminopimelate dehydrogenase, recombinantly expressed in Corynebacterium glutamicum strain ATCC 13032 with blocked HSD shows increased yield of L-lysine of 24.89 g/l compared to ddh gene expressed in wild-type strain ATCC 13032 (20.66 g/l of L-lysine). The maximum yield of L-lysine for the auxotrophic mutant is attained at pH 7.5 and 30°C after 96 h incubation time. Method optimization, overview
-
additional information
-
generation of a knockout homoserine dehydrogenase (HSD) mutant by chemical mutagenesis. Auxotrophic mutant formed from ddh gene, encoding diaminopimelate dehydrogenase, recombinantly expressed in Corynebacterium glutamicum strain ATCC 13032 with blocked HSD shows increased yield of L-lysine of 24.89 g/l compared to ddh gene expressed in wild-type strain ATCC 13032 (20.66 g/l of L-lysine). The maximum yield of L-lysine for the auxotrophic mutant is attained at pH 7.5 and 30°C after 96 h incubation time. Method optimization, overview
-
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
-
generation of a knockout homoserine dehydrogenase (HSD) mutant by chemical mutagenesis. Auxotrophic mutant formed from ddh gene, encoding diaminopimelate dehydrogenase, recombinantly expressed in Corynebacterium glutamicum strain ATCC 13032 with blocked HSD shows increased yield of L-lysine of 24.89 g/l compared to ddh gene expressed in wild-type strain ATCC 13032 (20.66 g/l of L-lysine). The maximum yield of L-lysine for the auxotrophic mutant is attained at pH 7.5 and 30°C after 96 h incubation time. Method optimization, overview
-
additional information
-
generation of a knockout homoserine dehydrogenase (HSD) mutant by chemical mutagenesis. Auxotrophic mutant formed from ddh gene, encoding diaminopimelate dehydrogenase, recombinantly expressed in Corynebacterium glutamicum strain ATCC 13032 with blocked HSD shows increased yield of L-lysine of 24.89 g/l compared to ddh gene expressed in wild-type strain ATCC 13032 (20.66 g/l of L-lysine). The maximum yield of L-lysine for the auxotrophic mutant is attained at pH 7.5 and 30°C after 96 h incubation time. Method optimization, overview
-
additional information
-
generation of a knockout homoserine dehydrogenase (HSD) mutant by chemical mutagenesis. Auxotrophic mutant formed from ddh gene, encoding diaminopimelate dehydrogenase, recombinantly expressed in Corynebacterium glutamicum strain ATCC 13032 with blocked HSD shows increased yield of L-lysine of 24.89 g/l compared to ddh gene expressed in wild-type strain ATCC 13032 (20.66 g/l of L-lysine). The maximum yield of L-lysine for the auxotrophic mutant is attained at pH 7.5 and 30°C after 96 h incubation time. Method optimization, overview
-
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
key metabolic pathway for construction of an inducer-free L-homoserine-producing strain to maximize the productivity of L-homoserine based on genetic-engineering tools, comparison of L-homoserine production, cell growth, and glucose consumption in different engineered strains, overview. L-Homoserine is a nonessential amino acid for the biosynthesis of L-threonine and L-methionine. It is also an important precursor for the production of isobutanol, 1,4-butanediol, L-phosphinothricin, 2,4-ihydroxybutyrate, and 1,3-propanediol. The initial L-homoserine-producing strain HS1 is obtained by blocking the degradative and competitive pathways and overexpressing thrA (encoding homoserine dehydrogenase) based on an O-succinyl homoserine-producing strain, using the pull-push-block strategy, an efficient method to engineer microorganisms involved in biosynthesizing target products by modifying metabolic networks. L-homoserine-converting pathway-related genes (thrB, encoding homoserine kinase, and metA, encoding homoserine O-succinyltransferase) are successively deleted to block L-homoserine degradation. Gene thrA is overexpressed to push the carbon flux to L-homoserine production. Then, the lysine-auxotrophic strain HS2 is generated by deleting lysA to eliminate a precursor competing metabolic pathway on L-homoserine production. For strengthening the capability of the L-homoserine transport system and the transformation of other toxic intermediate metabolites, gene rhtA, encoding the inner membrane transporter that is involved in the export of L-homoserine, is overexpressed chromosomally by replacing the native promoter with the trc promoter to obtain strain HS3 (Trc-rhtA). The strain shows increased activity. Increase in the L-homoserine export capacity and relieve the growth burden of homoserine-producing strains to enable survival via replacement of the native promoter of the eamA gene by the trc promoter in strain HS4 (Trc-eamA). Two rhtA gene copies (the native rhtA gene and replacement of the lacI gene) and eamA are overexpressed under the trc promoter in the chromosome to construct strain HS5 (DELTAlacI::Trc-rhtA Trc-rhtA Trc-eamA). Under batch culture, strain HS5, with modification of the transport system and construction of a constitutive expression system, can produce 3.14 g/l L-homoserine, which is 54.2% higher than strain HS2 production. In addition, the specific production of strain HS5 is also increased. Repression of candidate genes by the CRISPRi system to further enhance L-homoserine production
additional information
-
key metabolic pathway for construction of an inducer-free L-homoserine-producing strain to maximize the productivity of L-homoserine based on genetic-engineering tools, comparison of L-homoserine production, cell growth, and glucose consumption in different engineered strains, overview. L-Homoserine is a nonessential amino acid for the biosynthesis of L-threonine and L-methionine. It is also an important precursor for the production of isobutanol, 1,4-butanediol, L-phosphinothricin, 2,4-ihydroxybutyrate, and 1,3-propanediol. The initial L-homoserine-producing strain HS1 is obtained by blocking the degradative and competitive pathways and overexpressing thrA (encoding homoserine dehydrogenase) based on an O-succinyl homoserine-producing strain, using the pull-push-block strategy, an efficient method to engineer microorganisms involved in biosynthesizing target products by modifying metabolic networks. L-homoserine-converting pathway-related genes (thrB, encoding homoserine kinase, and metA, encoding homoserine O-succinyltransferase) are successively deleted to block L-homoserine degradation. Gene thrA is overexpressed to push the carbon flux to L-homoserine production. Then, the lysine-auxotrophic strain HS2 is generated by deleting lysA to eliminate a precursor competing metabolic pathway on L-homoserine production. For strengthening the capability of the L-homoserine transport system and the transformation of other toxic intermediate metabolites, gene rhtA, encoding the inner membrane transporter that is involved in the export of L-homoserine, is overexpressed chromosomally by replacing the native promoter with the trc promoter to obtain strain HS3 (Trc-rhtA). The strain shows increased activity. Increase in the L-homoserine export capacity and relieve the growth burden of homoserine-producing strains to enable survival via replacement of the native promoter of the eamA gene by the trc promoter in strain HS4 (Trc-eamA). Two rhtA gene copies (the native rhtA gene and replacement of the lacI gene) and eamA are overexpressed under the trc promoter in the chromosome to construct strain HS5 (DELTAlacI::Trc-rhtA Trc-rhtA Trc-eamA). Under batch culture, strain HS5, with modification of the transport system and construction of a constitutive expression system, can produce 3.14 g/l L-homoserine, which is 54.2% higher than strain HS2 production. In addition, the specific production of strain HS5 is also increased. Repression of candidate genes by the CRISPRi system to further enhance L-homoserine production
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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
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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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Bacillus methanolicus pyruvate carboxylase and homoserine dehydrogenase I and II and their roles for L-lysine production from methanol at 50 degrees C
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Bacillus methanolicus (D8WXQ1), Bacillus methanolicus (D8WXQ2), Bacillus methanolicus, Bacillus methanolicus MGA3 (D8WXQ1), Bacillus methanolicus MGA3 (D8WXQ2), Bacillus methanolicus MGA3
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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
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Glycine max (O63067), Glycine max (O65027), Glycine max (Q3S3F6), Glycine max
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Dong, X.; Zhao, Y.; Zhao, J.; Wang, X.
Characterization of aspartate kinase and homoserine dehydrogenase from Corynebacterium glutamicum IWJ001 and systematic investigation of L-isoleucine biosynthesis
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873-885
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Corynebacterium glutamicum (P08499), Corynebacterium glutamicum, Corynebacterium glutamicum IWJ001 (P08499), Corynebacterium glutamicum IWJ001
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Chen, Z.; Rappert, S.; Zeng, A.P.
Rational design of allosteric regulation of homoserine dehydrogenase by a nonnatural inhibitor L-lysine
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Corynebacterium glutamicum (P08499), Corynebacterium glutamicum
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Navratna, V.; Reddy, G.; Gopal, B.
Structural basis for the catalytic mechanism of homoserine dehydrogenase
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Staphylococcus aureus (A0A0H2WVX4), Staphylococcus aureus, Staphylococcus aureus COL (A0A0H2WVX4)
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Navratna, V.; Gopal, B.
Crystallization and preliminary X-ray diffraction studies of Staphylococcus aureus homoserine dehydrogenase
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Staphylococcus aureus (A0A0H2WVX4), Staphylococcus aureus, Staphylococcus aureus COL (A0A0H2WVX4)
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Tomonaga, Y.; Kaneko, R.; Goto, M.; Ohshima, T.; Yoshimune, K.
Structural insight into activation of homoserine dehydrogenase from the archaeon
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Sulfurisphaera tokodaii (F9VNG5), Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 (F9VNG5)
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Zhan, D.; Wang, D.; Min, W.; Han, W.
Exploring the molecular basis for selective binding of homoserine dehydrogenase from Mycobacterium leprae TN toward inhibitors: a virtual screening study
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Mycobacterium leprae (P46806), Mycobacterium leprae TN (P46806), Mycobacterium leprae TN
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Tsai, P.W.; Chien, C.Y.; Yeh, Y.C.; Tung, L.; Chen, H.F.; Chang, T.H.; Lan, C.Y.
Candida albicans Hom6 is a homoserine dehydrogenase involved in protein synthesis and cell adhesion
J. Microbiol. Immunol. Infect.
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863-871
2017
Candida albicans (Q5AIA2), Candida albicans, Candida albicans SC5314 / ATCC MYA-2876 (Q5AIA2)
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Hayashi, J.; Inoue, S.; Kim, K.; Yoneda, K.; Kawarabayasi, Y.; Ohshima, T.; Sakuraba, H.
Crystal structures of a hyperthermophilic archaeal homoserine dehydrogenase suggest a novel cofactor binding mode for oxidoreductases
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Pyrococcus horikoshii (O58802), Pyrococcus horikoshii ATCC 700860 (O58802)
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Shen, S.; Zhu, Y.; Fang, L.; Xu, J.
Heterologous expression and characterization of L200F/D215K mutant of homoserine dehydrogenase from Corynebacterium pekinense AS1.299
Wei Sheng Wu Xue Bao
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Corynebacterium pekinense, Corynebacterium pekinense AS1.299
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Bagatin, M.C.; Pimentel, A.L.; Biavatti, D.C.; Basso, E.A.; Kioshima, E.S.; Seixas, F.A.V.; Gauze, G.F.
Targeting the homoserine dehydrogenase of Paracoccidioides species for treatment of systemic fungal infections
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Paracoccidioides brasiliensis (C1G1C3), Paracoccidioides brasiliensis, Paracoccidioides lutzii (C1GTZ6), Paracoccidioides lutzii, Paracoccidioides lutzii Pb01 (C1GTZ6), Paracoccidioides brasiliensis PB18 (C1G1C3)
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Liu, P.; Zhang, B.; Yao, Z.H.; Liu, Z.Q.; Zheng, Y.G.
Multiplex design of the metabolic network for production of L-homoserine in Escherichia coli
Appl. Environ. Microbiol.
86
e01477-20
2020
Escherichia coli (P00561), Escherichia coli W3110 (P00561)
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Ohshida, T.; Koba, K.; Hayashi, J.; Yoneda, K.; Ohmori, T.; Ohshima, T.; Sakuraba, H.
A novel bifunctional aspartate kinase-homoserine dehydrogenase from the hyperthermophilic bacterium, Thermotoga maritima
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82
2084-2093
2018
Thermotoga maritima (Q9WZ17), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WZ17), Thermotoga maritima ATCC 43589 (Q9WZ17), Thermotoga maritima JCM 10099 (Q9WZ17)
brenda
Akai, S.; Ikushiro, H.; Sawai, T.; Yano, T.; Kamiya, N.; Miyahara, I.
The crystal structure of homoserine dehydrogenase complexed with L-homoserine and NADPH in a closed form
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Thermus thermophilus (Q5SL04), Thermus thermophilus
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Kim, D.H.; Nguyen, Q.T.; Ko, G.S.; Yang, J.K.
Molecular and enzymatic features of homoserine dehydrogenase from Bacillus subtilis
J. Microbiol. Biotechnol.
30
1905-1911
2020
Bacillus subtilis (P19582), Bacillus subtilis, Bacillus subtilis 168 (P19582)
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Bueno, P.S.A.; Rodrigues, F.A.V.; Santos, J.L.; Canduri, F.; Biavatti, D.C.; Pimentel, A.L.; Bagatin, M.C.; Kioshima, E.S.; de Freitas Gauze, G.; Seixas, F.A.V.
New inhibitors of homoserine dehydrogenase from Paracoccidioides brasiliensis presenting antifungal activity
J. Mol. Model.
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325
2019
Paracoccidioides brasiliensis (C1G1C3), Paracoccidioides brasiliensis, Paracoccidioides brasiliensis PB18 (C1G1C3)
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Skwarecki, A.S.; Schielmann, M.; Martynow, D.; Kawczynski, M.; Wisniewska, A.; Milewska, M.J.; Milewski, S.
Antifungal dipeptides incorporating an inhibitor of homoserine dehydrogenase
J. Pept. Sci.
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Candida albicans (Q5AIA2), Candida albicans ATCC MYA-2876 (Q5AIA2)
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Vanasi, B.; Eppakayala, L.; Malothu, R.
L-lysine production by chemical mutagenesis of homoserine dehydrogenase of ddh gene in Corynebacterium glutamicum ATCC13032
Rasayan J. Chem.
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1245-1261
2020
Corynebacterium glutamicum (P08499), Corynebacterium glutamicum LMG 3730 (P08499), Corynebacterium glutamicum BCRC 11384 (P08499), Corynebacterium glutamicum ATCC 13032 (P08499), Corynebacterium glutamicum JCM 1318 (P08499), Corynebacterium glutamicum NCIMB 10025 (P08499), Corynebacterium glutamicum DSM 20300 (P08499)
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Ogata, K.; Yajima, Y.; Nakamura, S.; Kaneko, R.; Goto, M.; Ohshima, T.; Yoshimune, K.
Inhibition of homoserine dehydrogenase by formation of a cysteine-NAD covalent complex
Sci. Rep.
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5749
2018
Sulfurisphaera tokodaii (F9VNG5), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (F9VNG5)
brenda