BRENDA - Enzyme Database
show all sequences of 1.1.1.3

Crystal structures of a hyperthermophilic archaeal homoserine dehydrogenase suggest a novel cofactor binding mode for oxidoreductases

Hayashi, J.; Inoue, S.; Kim, K.; Yoneda, K.; Kawarabayasi, Y.; Ohshima, T.; Sakuraba, H.; Sci. Rep. 5, 11674 (2015)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene PH1075, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) codon plus-RIPL
Pyrococcus horikoshii
Crystallization (Commentary)
Crystallization (Commentary)
Organism
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, 20°C, 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, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement and modelling
Pyrococcus horikoshii
Engineering
Protein Variants
Commentary
Organism
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
Pyrococcus horikoshii
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
Pyrococcus horikoshii
Inhibitors
Inhibitors
Commentary
Organism
Structure
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
Pyrococcus horikoshii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
enzyme HseDH shows typical Michaelis-Menten kinetics for oxidation
Pyrococcus horikoshii
0.04
-
NADP+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
0.05
-
NAD+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
0.06
-
NADP+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
0.32
-
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
0.95
-
NAD+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
6.1
-
L-homoserine
pH 9.0, 50°C, recombinant enzyme
Pyrococcus horikoshii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
-
Pyrococcus horikoshii
92000
-
gel filtration, recombinant His-tagged enzyme HseDH
Pyrococcus horikoshii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-homoserine + NAD+
Pyrococcus horikoshii
-
L-aspartate 4-semialdehyde + NADH + H+
-
-
r
L-homoserine + NAD+
Pyrococcus horikoshii ATCC 700860
-
L-aspartate 4-semialdehyde + NADH + H+
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Pyrococcus horikoshii
O58802
-
-
Pyrococcus horikoshii ATCC 700860
O58802
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) codon plus-RIPL by heat treatment at 90°C for 10 min, nickel affinity chromatography, dialysis, gel filtration, and ultrafiltration
Pyrococcus horikoshii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-homoserine + NAD+
-
741408
Pyrococcus horikoshii
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
-
741408
Pyrococcus horikoshii ATCC 700860
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NADP+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
741408
Pyrococcus horikoshii
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
741408
Pyrococcus horikoshii ATCC 700860
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homodimer
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
Pyrococcus horikoshii
Synonyms
Synonyms
Commentary
Organism
HseDH
-
Pyrococcus horikoshii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
assay at
Pyrococcus horikoshii
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
75
-
purified recombinant His-tagged enzyme, 10 min, retains full activity
Pyrococcus horikoshii
90
-
purified recombinant His-tagged enzyme, 10 min, retains 70% activity
Pyrococcus horikoshii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.4
-
NADP+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
26.7
-
NADP+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
48.5
-
NAD+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
70.1
-
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
96.1
-
NAD+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
11
-
recombinant enzyme
Pyrococcus horikoshii
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
5
12
purified recombinant His-tagged enzyme, 10 min, 50°C, stable at
Pyrococcus horikoshii
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
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
Pyrococcus horikoshii
NAD+
-
Pyrococcus horikoshii
NADH
-
Pyrococcus horikoshii
NADP+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
Pyrococcus horikoshii
NADPH
no activity of the wild-type enzyme with NADPH, but only with enzyme mutants R40A and K57A
Pyrococcus horikoshii
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0000052
-
NADP+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene PH1075, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) codon plus-RIPL
Pyrococcus horikoshii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
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
Pyrococcus horikoshii
NAD+
-
Pyrococcus horikoshii
NADH
-
Pyrococcus horikoshii
NADP+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
Pyrococcus horikoshii
NADPH
no activity of the wild-type enzyme with NADPH, but only with enzyme mutants R40A and K57A
Pyrococcus horikoshii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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, 20°C, 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, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement and modelling
Pyrococcus horikoshii
Engineering (protein specific)
Protein Variants
Commentary
Organism
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
Pyrococcus horikoshii
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
Pyrococcus horikoshii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
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
Pyrococcus horikoshii
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0000052
-
NADP+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
enzyme HseDH shows typical Michaelis-Menten kinetics for oxidation
Pyrococcus horikoshii
0.04
-
NADP+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
0.05
-
NAD+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
0.06
-
NADP+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
0.32
-
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
0.95
-
NAD+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
6.1
-
L-homoserine
pH 9.0, 50°C, recombinant enzyme
Pyrococcus horikoshii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
-
Pyrococcus horikoshii
92000
-
gel filtration, recombinant His-tagged enzyme HseDH
Pyrococcus horikoshii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-homoserine + NAD+
Pyrococcus horikoshii
-
L-aspartate 4-semialdehyde + NADH + H+
-
-
r
L-homoserine + NAD+
Pyrococcus horikoshii ATCC 700860
-
L-aspartate 4-semialdehyde + NADH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) codon plus-RIPL by heat treatment at 90°C for 10 min, nickel affinity chromatography, dialysis, gel filtration, and ultrafiltration
Pyrococcus horikoshii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-homoserine + NAD+
-
741408
Pyrococcus horikoshii
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
-
741408
Pyrococcus horikoshii ATCC 700860
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NADP+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
741408
Pyrococcus horikoshii
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
741408
Pyrococcus horikoshii ATCC 700860
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
Pyrococcus horikoshii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
assay at
Pyrococcus horikoshii
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
75
-
purified recombinant His-tagged enzyme, 10 min, retains full activity
Pyrococcus horikoshii
90
-
purified recombinant His-tagged enzyme, 10 min, retains 70% activity
Pyrococcus horikoshii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.4
-
NADP+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
26.7
-
NADP+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
48.5
-
NAD+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
70.1
-
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
96.1
-
NAD+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
11
-
recombinant enzyme
Pyrococcus horikoshii
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
5
12
purified recombinant His-tagged enzyme, 10 min, 50°C, stable at
Pyrococcus horikoshii
General Information
General Information
Commentary
Organism
evolution
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
Pyrococcus horikoshii
General Information (protein specific)
General Information
Commentary
Organism
evolution
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
Pyrococcus horikoshii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
89.1
-
NADP+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
102
-
NAD+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
219
-
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
518
-
NADP+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
1020
-
NAD+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
89.1
-
NADP+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
102
-
NAD+
pH 9.0, 50°C, recombinant mutant R40A
Pyrococcus horikoshii
219
-
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
Pyrococcus horikoshii
518
-
NADP+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
1020
-
NAD+
pH 9.0, 50°C, recombinant mutant K57A
Pyrococcus horikoshii
Other publictions for EC 1.1.1.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740860
Tsai
Candida albicans Hom6 is a hom ...
Candida albicans, Candida albicans SC5314 / ATCC MYA-2876
J. Microbiol. Immunol. Infect.
50
863-871
2017
-
2
1
-
1
-
-
-
2
-
-
2
-
5
-
-
-
-
-
-
-
-
2
-
2
1
-
-
-
1
-
-
2
-
-
-
-
2
1
2
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
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1
-
-
-
-
2
2
-
-
-
738802
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Corynebacterium glutamicum, Corynebacterium glutamicum IWJ001
J. Ind. Microbiol. Biotechnol.
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873-885
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-
-
1
-
2
-
1
-
-
-
-
2
-
4
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
739779
Chen
Rational design of allosteric ...
Corynebacterium glutamicum
ACS Synth. Biol.
4
126-131
2015
-
-
-
-
1
-
3
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
739791
Navratna
Structural basis for the catal ...
Staphylococcus aureus, Staphylococcus aureus COL
Acta Crystallogr. Sect. D
71
1216-1225
2015
-
-
1
1
3
-
2
1
-
-
-
2
-
4
-
-
1
1
-
-
-
-
2
2
3
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
1
3
-
-
2
-
1
-
-
-
2
-
-
-
1
-
-
-
-
2
2
1
-
-
-
1
-
-
-
-
3
3
-
-
-
739972
Tomonaga
-
Structural insight into activa ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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3
14-17
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1
-
1
1
-
-
-
4
-
-
-
2
-
2
-
-
1
-
-
-
-
-
4
1
1
1
-
-
-
1
-
-
4
-
-
-
1
-
1
4
1
-
-
-
-
-
4
-
-
-
2
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
741408
Hayashi
Crystal structures of a hypert ...
Pyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860
Sci. Rep.
5
11674
2015
-
-
1
1
2
-
1
7
-
-
2
2
-
2
-
-
1
-
-
-
-
-
4
1
1
1
-
2
5
1
-
1
5
1
-
-
-
-
1
5
1
2
-
-
1
1
7
-
-
2
2
-
-
-
1
-
-
-
-
4
1
1
-
2
5
1
-
1
-
-
1
1
-
5
5
740548
Zhan
Exploring the molecular basis ...
Mycobacterium leprae, Mycobacterium leprae TN
Int. J. Mol. Sci.
15
1826-1841
2014
-
-
-
-
-
-
7
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
2
5
-
1
-
-
-
2
-
-
-
1
7
5
-
-
-
-
2
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
741465
Shen
-
Heterologous expression and ch ...
Corynebacterium pekinense, Corynebacterium pekinense AS1.299
Wei Sheng Wu Xue Bao
54
1178-1184
2014
-
-
1
-
5
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
1
-
1
-
-
-
-
-
-
-
-
-
739804
Navratna
Crystallization and preliminar ...
Staphylococcus aureus, Staphylococcus aureus COL
Acta Crystallogr. Sect. F
69
1216-1219
2013
-
-
1
1
-
-
-
-
1
-
-
2
-
4
-
-
1
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
-
1
-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
710978
Brautaset
Bacillus methanolicus pyruvate ...
Bacillus methanolicus, Bacillus methanolicus MGA3
Appl. Microbiol. Biotechnol.
87
951-964
2010
-
1
-
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
2
-
-
712490
Schroeder
Threonine-insensitive homoseri ...
Glycine max
J. Biol. Chem.
285
827-834
2010
-
-
1
-
-
-
2
23
-
-
3
-
-
5
-
-
1
1
-
-
1
-
15
1
2
-
-
-
12
-
-
-
2
1
-
-
-
-
3
2
-
-
-
-
2
1
24
-
-
3
-
-
-
-
3
-
-
1
-
15
1
-
-
-
12
-
-
-
-
-
-
-
-
24
24
688167
Yilmaz
Targeted disruption of homoser ...
Streptomyces clavuligerus, Streptomyces clavuligerus NRRL 3585
J. Ind. Microbiol. Biotechnol.
35
1-7
2008
-
-
1
-
1
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
689647
Varisi
Lysine biosynthesis and nitrog ...
Chenopodium quinoa
Plant Physiol. Biochem.
46
11-18
2008
-
-
-
-
-
-
2
-
-
-
-
-
-
3
-
-
1
-
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688822
Park
Characteristics of methionine ...
Corynebacterium glutamicum
Metab. Eng.
9
327-336
2007
-
-
1
-
1
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
670165
Cahyanto
Regulation of aspartokinase, a ...
Lactobacillus plantarum
Microbiology
152
105-112
2006
-
-
1
-
-
-
2
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662432
Curien
Identification of six novel al ...
Arabidopsis thaliana
J. Biol. Chem.
280
41178-41183
2005
-
-
1
-
-
-
1
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654955
Ejim
New phenolic inhibitors of yea ...
Saccharomyces cerevisiae
Bioorg. Med. Chem.
12
3825-3830
2004
-
1
-
1
-
-
13
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
2
1
-
-
-
13
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642341
Paris
Mechanism of control of Arabid ...
Arabidopsis thaliana
J. Biol. Chem.
278
5361-5366
2003
-
-
-
-
2
-
1
-
-
1
2
-
-
2
-
-
-
1
-
-
-
-
1
1
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
2
-
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
657018
Rognes
Transcriptional and biochemica ...
Arabidopsis thaliana, Saccharomyces cerevisiae
Plant Mol. Biol.
51
281-294
2003
-
-
1
-
2
-
1
-
-
1
-
2
-
6
-
-
-
1
-
4
-
-
3
-
3
-
-
-
-
-
-
-
3
-
-
-
-
-
1
3
-
2
-
-
1
-
-
-
1
-
2
-
-
-
-
-
4
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642340
Paris
Overproduction, purification, ...
Arabidopsis thaliana
Protein Expr. Purif.
24
105-110
2002
-
-
-
-
-
-
1
5
-
1
2
-
-
3
-
-
-
1
-
-
2
1
1
2
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
1
2
-
-
-
-
-
-
-
2
1
1
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
654640
James
Production and characterizatio ...
Escherichia coli
Biochemistry
41
3720-3725
2002
-
-
1
-
1
-
-
4
-
-
-
1
-
2
-
-
1
1
-
-
-
-
2
-
2
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
246401
Jacques
Homoserine dehydrogenase from ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1544
42-54
2001
-
-
-
-
-
-
4
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246402
Jacques
Characterization of yeast homo ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1544
28-41
2001
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246396
DeLaBarre
Crystal structures of homoseri ...
Saccharomyces cerevisiae
Nat. Struct. Biol.
7
238-244
2000
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246394
Morbach
-
Engineering the homoserine deh ...
Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
45
612-620
1996
-
-
-
-
1
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246395
Pavagi
Purification and characterizat ...
Spinacia oleracea
Biochem. Mol. Biol. Int.
36
649-658
1995
1
-
-
-
-
-
7
3
-
-
2
-
-
2
-
-
1
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
7
-
3
-
-
2
-
-
-
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246387
Wedler
Kinetic and regulatory mechani ...
Escherichia coli
J. Biol. Chem.
268
4880-4888
1993
-
-
-
-
-
-
1
4
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246403
Omori
Role of serine 352 in the allo ...
Serratia marcescens
J. Bacteriol.
175
959-965
1993
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246398
Hama
Inhibition of homoserine dehyd ...
Escherichia coli
J. Biochem.
109
604-608
1991
-
-
-
-
-
-
3
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246399
Yumoto
Rapid purification and charact ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
285
270-275
1991
-
-
-
-
-
-
2
-
-
-
2
-
-
6
-
-
1
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246397
Yamaki
The mechanism of antifungal ac ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
168
837-843
1990
-
-
-
-
-
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246400
Angeles
The kinetic mechanism of the b ...
Escherichia coli
Arch. Biochem. Biophys.
283
96-101
1990
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246383
Krishnaswamy
Use of monoclonal antibodies f ...
Zea mays
Arch. Biochem. Biophys.
246
250-262
1986
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246384
Krishnaswamy
Ligand-induced interconversion ...
Zea mays
Arch. Biochem. Biophys.
222
449-463
1983
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
1
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246382
Sainis
Localisation and characterisat ...
Hordeum vulgare, Pisum sativum
Planta
152
491-496
1981
-
-
-
-
-
-
4
7
4
-
4
2
-
5
-
-
2
-
-
2
-
-
6
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
4
-
7
4
-
4
2
-
-
-
2
-
2
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246386
Di Camelli
Comparison of sensitive and de ...
Zea mays
Plant Physiol.
65
176-183
1980
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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246388
Grego
-
Comparison of homoserine dehyd ...
Pisum sativum, Ricinus communis, Triticum aestivum
Phytochemistry
19
1619-1623
1980
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3
5
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15
5
3
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3
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3
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3
3
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8
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6
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6
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3
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5
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15
5
3
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3
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3
3
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8
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246385
Walter
Isolation and characterization ...
Zea mays
J. Biol. Chem.
254
1349-1355
1979
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1
4
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5
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4
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5
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1
2
1
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2
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246389
Epstein
Homoserine dehydrogenase of Rh ...
Rhodospirillum rubrum
Eur. J. Biochem.
82
453-461
1978
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1
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3
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2
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1
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1
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246390
Ogilvie
Reaction of Tris with aldehyde ...
Escherichia coli
Biochim. Biophys. Acta
445
525-536
1976
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-
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1
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246391
Aarnes
-
Threonine-sensitive aspartate ...
Pisum sativum
Phytochemistry
13
2717-2724
1974
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3
2
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1
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1
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246392
Cavari
Properties of homoserine dehyd ...
Thermophilic bacterium
Biochim. Biophys. Acta
302
183-190
1973
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-
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4
1
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5
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1
1
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1
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1
1
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1
1
-
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-
-
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246393
Saiki
Studies on homoserine dehydrog ...
Thermus thermophilus
J. Biochem.
74
1239-1248
1973
-
-
-
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-
-
1
1
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2
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