Information on EC 1.1.1.3 - homoserine dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.3
-
RECOMMENDED NAME
GeneOntology No.
homoserine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-homoserine biosynthesis
-
-
threonine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Cysteine and methionine metabolism
-
-
Lysine biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Microbial metabolism in diverse environments
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
L-homoserine:NAD(P)+ oxidoreductase
The yeast enzyme acts most rapidly with NAD+; the Neurospora enzyme with NADP+. The enzyme from Escherichia coli is a multi-functional protein, which also catalyses the reaction of EC 2.7.2.4 (aspartate kinase).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-13-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
Candida albicans SC5314 / ATCC MYA-2876
-
UniProt
Manually annotated by BRENDA team
two isozymes
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
-
O58802
UniProt
Manually annotated by BRENDA team
-
O58802
UniProt
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
also shows aspartase kinase activity
-
-
Manually annotated by BRENDA team
also shows aspartase kinase activity; spinach
-
-
Manually annotated by BRENDA team
gene hom
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
UniProt
Manually annotated by BRENDA team
Thermophilic bacterium
-
-
-
Manually annotated by BRENDA team
wheat
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
show the reaction diagram
L-aspartate 4-semialdehyde + NADH
L-homoserine + NAD+
show the reaction diagram
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
show the reaction diagram
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
show the reaction diagram
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH
show the reaction diagram
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
show the reaction diagram
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
show the reaction diagram
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
show the reaction diagram
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
show the reaction diagram
-
part of the aspartate pathway of amino acid biosynthesis
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
show the reaction diagram
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
show the reaction diagram
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
O58802
NADP does not act as a cofactor for this enzyme, but as a strong inhibitor of NAD+-dependent oxidation of Hse, analysis of the cofactor-binding site of the enzyme, Pyrococcus horikoshii HseDH shows a unique cofactor binding mode, which is not observed in conventional NAD(P)-dependent dehydrogenases. Superposition of the Hse/NADPH-bound K57A structure onto the NADPH-bound wild-type structure shows that the NADPH molecule in the mutant structure is positioned/configured nearly identically to the NADPH molecule in the wild-type structure, except for the positioning of the C2 phosphate group of the adenine ribose. The C2 phosphate is tightly held in position through five surrounding hydrogen bonds in the wild-type enzyme. In K57A mutant the C2 phosphate group is rotates in a clockwise direction around C2B of NADPH by about 30 relative to the wild-type structure. The guanidino group of Arg40 in the mutant is also rotated clockwise by about 90 around the NE atom of Arg40 relative to the wild-type structure
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for aspartate kinase activity
Rb+
Thermophilic bacterium
-
can partially replace K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
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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
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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-iopropylphenylthio)-2-isopropylphenol
-
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
competitive to L-aspartate 4-semialdehyde, enzyme binding structure anaysis from crystal structure, overview
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4-[[2-(2-furanyl)ethyl]thio]-phenol
-
-
4-[[[4-(1,1-dimethylethyl)phenyl]thio]methyl]-2,6-bis(1-methylethyl)-phenol
-
-
aspartate
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bis(4-chlorophenyl)ethyloxiranyl-silane
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-
D-threonine
Thermophilic bacterium
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slight
DL-allo-threonine
Thermophilic bacterium
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-
H-(1,2,4-triazol-3-yl)-DL-alanine
-
-
homoserine
-
-
L-cysteine
L-lysine
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allosteric regulation of recombinant engineered homoserine dehydrogenase by nonnatural inhibitor L-lysine
L-serine
L-threonine
methionine
NADP+
p-chloromercuribenzoate
-
-
threonine
Trifluoperazine
-
-
[2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid ethyl ester
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
-
in the presence of above 0.1 mM Ca2+
dithiothreitol
the enzyme is 2.5fold activated by the addition of 0.8 mM dithiothreitol. The activation is caused by cleavage of the disulfide bond formed between two cysteine residues in the C-terminal regions of the two subunits
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
aspartate 4-semialdehyde
-
isozyme II
5.5
ATP
pH 8.0, 37C, purified recombinant soluble enzyme
0.1
DL-aspartate 4-semialdehyde
-
-
11.6
L-aspartate
pH 8.0, 37C, purified recombinant soluble enzyme
0.066 - 2.19
L-aspartate 4-semialdehyde
0.013 - 17.4
L-homoserine
0.05 - 24.9
NAD+
0.158 - 0.46
NADH
0.034 - 0.245
NADP+
0.027 - 0.09
NADPH
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 22.58
L-aspartate 4-semialdehyde
0.042 - 24
L-homoserine
48.5 - 96.1
NAD+
3.4 - 26.7
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.29 - 28.54
L-aspartate 4-semialdehyde
0.039 - 0.757
L-homoserine
0.281 - 1020
NAD+
61.29 - 118.9
NADH
0.18 - 518
NADP+
101.4 - 331.2
NADPH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0131
(2S)-2-[[4-(propan-2-yl)phenyl]sulfanyl]propanenitrile
pH and temperature not specified in the publication
0.01307
1-tert-butyl-4-[(difluoromethyl)sulfanyl]benzene
pH and temperature not specified in the publication
0.00963
1-[(1S,2S)-2-(bromomethyl)cyclopropyl]-4-[(trifluoromethyl)sulfanyl]benzene
pH and temperature not specified in the publication
0.01568
3-[(4-tert-butylphenyl)sulfanyl]propane-1-thiol
pH and temperature not specified in the publication
0.01
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
pH and temperature not specified in the publication
-
160 - 240
L-threonine
pH 8.0, 25C
0.0000052
NADP+
O58802
pH 9.0, 50C, recombinant wild-type enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0051
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
Mycobacterium leprae
P46806
pH and temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0044 - 0.0046
-
enzyme activity at different seed developmental stages, overview
5.4
purified recombinant soluble enzyme, forward reaction of aspartate kinase
18.87
purified recombinant soluble enzyme, reverse reaction of homoserine dehydrogenase
343
-
-
360
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
mutants L200F/D215K and L200F
8.5
-
the catalytic activity of the enzyme for the conversion of L-homoserine to L-aspartate 4-semialdehyde (the reverse reaction) is enhanced at basic pH
9.8
Thermophilic bacterium
-
-
11
O58802
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
Thermophilic bacterium
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
35
-
mutant L200F
50
O58802
assay at
70
Thermophilic bacterium
-
-
additional information
-
above 50C temperature dependent conformational change
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
Thermophilic bacterium
-
no activity at 80C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
akthr2 is not or time-restricted expressed in stem, gynoecium, and during seed formation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thiobacillus denitrificans (strain ATCC 25259)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
-
gel filtration, isozyme II, cytoplasm
38000
-
2 * 38000, SDS-PAGE, threonine resistant isozyme
40600
2 * 40600, calculated, 2 * 40000, SDS-PAGE
69000
-
gel filtration, isozyme II, cytoplasm
80000
-
disc gel electrophoresis, threonine insensitive isozyme
81000
-
gel filtration
85000
-
x * 85000, SDS-PAGE, threonine sensitive isozyme
89000
-
x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme
92000
O58802
gel filtration, recombinant His-tagged enzyme HseDH
93000
-
x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme
110000
-
gel filtration, sedimentation equilibrium centrifugation
168000 - 174000
190000
-
gel filtration threonine sensitive isozyme
220000
280000
-
disc gel electrophoresis, threonine sensitive isozyme
290000
-
gel filtration, threonine sensitive isozyme
320000
470000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 85000, SDS-PAGE, threonine sensitive isozyme
hexamer
in absence of L-threonine
homodimer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for the purified ligand-free recombinant wild-type enzyme: sitting drop vapor diffusion method, mixing of 0.001 ml of 12.0 mg/ml protein solution with an equal volume of mother liquor composed of 0.1 M potassium phosphate, pH 6.2, and 20% MPD, 2 days, 20C, for the homoserine-bound K57A mutant enzyme: sitting drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution containing 1 mM homoserine with 0.002 ml of mother liquor containing 16% polyethylene glycol monomethyl ether 2000 and 0.1 M citrate buffer, pH 6.5, 7 days, 20C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement and modelling
O58802
10 mg/ml purified recombinant enzyme, in TAPS, pH 8.5, in complex with inhibitor 4,4'-thiobis[2-(1-methylethyl)-phenol] in a molar ratio of 1:1, precipitant solution contains either 0.1 CHES, pH 9.5, 35% PEG 600 or 0.1 M CHES, pH 8.5, 40% PEG 400, and 0.2 M NaCl, 0.005 ml protein complex solution are equilibrated against 0.7 ml of precipitant solution using sitting drop technique, 3 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, modeling
-
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, hanging drop and sitting drop methods of vapour diffusion, 8 mg/ml protein solution is mixed with reservoir solution, different conditions involving addition of 0.2 M magnesium acetate and PEG 3350 or 8000, and 3.5% glycerol, overview. X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
-
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
-
purified recombinant enzyme in oxidized and in reduced form, hanging drop vapor diffusion method, for the oxidized form: mixing of 0.0015 ml of 5.9 mg/ml protein solution with 0.0015 ml of reservoir solution, pH 4.1, containing 9.5% w/v PEG 3350, 19% w/v PEG 400, 0.19 M magnesium chloride, and 2.5% DMSO, for the reduced form: soaking of the oxidized enzyme crystals in a solution consisting of 0.003 ml of reservoir solution and 0.001 ml of 200 mM DTT for 60 min prior to the first diffraction data collection, 12C, X-ray diffraction structure determmination and analysis at 1.60-1.83 A resolution, molecular replacement and modelling
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 12
O58802
purified recombinant His-tagged enzyme, 10 min, 50C, stable at
741408
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
half-life of mutant L200F/D215K is 4.16 h, of mutant L200F 3.71 h
75
O58802
purified recombinant His-tagged enzyme, 10 min, retains full activity
80
-
slow inactivation, protection by K+, Na+
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.05 M potassium phosphate buffer, pH 7.5, 1.0 mM EDTA, 2.0 mM dithioerythritol, 5.0 mM L-threonine, 20% v/v glycerol, at least 2 years
-
-20C, 30 mM potassium phosphate buffer, pH 7.5, 50% v/v glycerol, threonine resistant isozyme at least 2 months stable, threonine sensitive isozyme at least 4 months stable
-
-25C, 50 mM potassium phosphate buffer, pH 7.2, 15% v/v glycerol, 1 mM EDTA, 1 mM threonine, 14 mM 2-mercaptoethanol
-
-80C, purified recombinant soluble enzyme, at 3 mg/ml, stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially from seeds by ammonium sulfate fractionation and desalting gel filtration
-
overexpressed in Escherichia coli
-
recombinant enzyme
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 70C for 3 h, anion exchange chromatography, dialysis, and ultrafiltration
recombinant enzyme; recombinant enzyme; recombinant enzyme
recombinant His-tagged enzyme from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) codon plus-RIPL by heat treatment at 90C for 10 min, nickel affinity chromatography, dialysis, gel filtration, and ultrafiltration
O58802
recombinant separated catalytic domains
-
separation of the two isozymes using Blue-Sepharose chromatography
-
separation of the two isozymes using Matrex Gel Red A affinity chromatography
-
threonine sensitive and threonine insensitive isozymes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both catalytic domains of the enzyme, performing each one of the enzyme activities, are expressed separately with or without the interface region, resulting in increased activity of each domain compared to the wild-type bifunctional holoenzyme, the isolated catalytic domains are no longer allosterically regulated, expression of hybrid holoenzyme AKIII-HDHI+
-
expression in Escherichia coli
-
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
gene akthr2, DNA sequence determination and analysis, located on chromosome 4, subcloning in Escherichia coli strain DH5alpha, functional complementation of the Saccharomyces cerevisiae homoserine dehydrogenase-deficient hom6 mutant strain and of the aspartate kinase-deficient hom3 mutant strain, conferring L-threonine and L-methionine prototrophy to the yeast cells
-
gene hom, DNA and amino acid sequence determination and analysis, expression in the auxotroph mutant Escherichia coli CGSC 5075
gene hom, recombinant expression of His-tagged enzyme in Echerichia coli strain Rosetta (DE3) pLysS
-
gene hom, recombinant expression of His-tagged wild-type and mutant enzymes in Echerichia coli strain Rosetta (DE3) pLysS
-
gene hom, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene hom1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), recombinant overexpression of constructs comprising the enzyme with homoserine kinase, aspartate kinase, acetohydroxy acid synthase, or threonine dehydratase, overview
-
gene HOM6, DNA and amino acid sequence determination and analysis from the strain SC5314 genome, sequence comparison, reintegration of the gene encoding the wild-type enzyme into HOM6-deletion strains
gene PH1075, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) codon plus-RIPL
O58802
introduction of the gene homFBR allele into strain HL1049
-
overexpression in Escherichia coli
-
overexpression of AK-HSDH isoform 1 in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
strongly repressed by L-methionine; strongly repressed by L-threonine
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
O58802
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
O58802
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
-
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
denatures in 3 M guanidine-HCl and refolds by simple dilution
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
pharmacology
-
enzyme is a target for inhibitor design for construction of antimicrobial agents
synthesis
additional information
Show AA Sequence (21521 entries)
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