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Characterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization

Pearce, F.G.; Dobson, R.C.; Jameson, G.B.; Perugini, M.A.; Gerrard, J.A.; Biochim. Biophys. Acta 1814, 1900-1909 (2011)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.3.3.7
purified recombinant Tm-DHDPS-DELTAArg-237, vapor diffusion method, mixing of 150 nl protein solution, containing 11.2 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 150 nl reservoir solution, containing 40% v/v PEG 300, 100 mM phosphate-citrate, buffer, pH 4.2, and 0.02% w/v sodium azide, X-ray diffraction structure determination and analysis at 1.9-2.1 A resolution
Thermotoga maritima
Engineering
EC Number
Amino acid exchange
Commentary
Organism
4.3.3.7
additional information
construction of mutants Tm-DHDPS-DELTAAsp168, DELTAAsp171, or DELTAArg237 by mutating charged residues, reduction of the number of salt bridges at one of the two tetramerization interface of the enzyme and its interactions results in variants with altered quaternary structure, e.g. monomeric, as shown by analytical ultracentrifugation, gel filtration liquid chromatography, and small angle X-ray scattering, and X-ray crystallographic studies, overview
Thermotoga maritima
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
additional information
-
additional information
Michaelis-Menten kinetics for wild-type and mutant enzymes, overview
Thermotoga maritima
4.3.3.7
0.05
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.07
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
0.08
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237; pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.1
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.15
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.15
-
pyruvate
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.16
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
0.18
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.18
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
0.23
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237; pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.32
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
0.36
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.42
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
0.46
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
1.1
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
1.2
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
1.3
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
1.5
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
1.5
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
1.7
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
1.7
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168; pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
2.1
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
2.2
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
2.4
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
2.6
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
34000
-
4 * 34000, SDS-PAGE, role of quaternary structure in the TIM-barrel family of enzymes, overview. Unlike other DHDPS enzymes, but like many thermophilic enzymes, Tm-DHDPS has a large number of charged residues at the quaternary interface. Removal of electrostatic interactions disrupts quaternary structure
Thermotoga maritima
4.3.3.7
130000
-
gel filtration
Thermotoga maritima
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
Thermotoga maritima
-
(S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Thermotoga maritima
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
-
714351
Thermotoga maritima
(S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
-
-
?
4.3.3.7
additional information
the active site of the monomer is well conserved, with most active-site residues in the same conformation
714351
Thermotoga maritima
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
4.3.3.7
tetramer
4 * 34000, SDS-PAGE, role of quaternary structure in the TIM-barrel family of enzymes, overview. Unlike other DHDPS enzymes, but like many thermophilic enzymes, Tm-DHDPS has a large number of charged residues at the quaternary interface. Removal of electrostatic interactions disrupts quaternary structure
Thermotoga maritima
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
4.3.3.7
30
45
assay at 30C and at 45C
Thermotoga maritima
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3.3.7
35
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
35
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
39
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
39
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
52
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
52
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
63
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
63
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
68
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
68
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
88
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
88
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
97
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
97
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
108
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
108
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
111
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
111
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
134
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
134
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
136
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
136
-
pyruvate
pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
141
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
141
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
233
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
233
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
465
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
465
-
pyruvate
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.3.3.7
purified recombinant Tm-DHDPS-DELTAArg-237, vapor diffusion method, mixing of 150 nl protein solution, containing 11.2 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 150 nl reservoir solution, containing 40% v/v PEG 300, 100 mM phosphate-citrate, buffer, pH 4.2, and 0.02% w/v sodium azide, X-ray diffraction structure determination and analysis at 1.9-2.1 A resolution
Thermotoga maritima
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
4.3.3.7
additional information
construction of mutants Tm-DHDPS-DELTAAsp168, DELTAAsp171, or DELTAArg237 by mutating charged residues, reduction of the number of salt bridges at one of the two tetramerization interface of the enzyme and its interactions results in variants with altered quaternary structure, e.g. monomeric, as shown by analytical ultracentrifugation, gel filtration liquid chromatography, and small angle X-ray scattering, and X-ray crystallographic studies, overview
Thermotoga maritima
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
additional information
-
additional information
Michaelis-Menten kinetics for wild-type and mutant enzymes, overview
Thermotoga maritima
4.3.3.7
0.05
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.07
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
0.08
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237; pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.1
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.15
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.15
-
pyruvate
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.16
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
0.18
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
0.18
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
0.23
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237; pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.32
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
0.36
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
0.42
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
0.46
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
1.1
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
1.2
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
1.3
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
1.5
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
1.5
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
1.7
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
1.7
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168; pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
2.1
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
2.2
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
2.4
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
2.6
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
34000
-
4 * 34000, SDS-PAGE, role of quaternary structure in the TIM-barrel family of enzymes, overview. Unlike other DHDPS enzymes, but like many thermophilic enzymes, Tm-DHDPS has a large number of charged residues at the quaternary interface. Removal of electrostatic interactions disrupts quaternary structure
Thermotoga maritima
4.3.3.7
130000
-
gel filtration
Thermotoga maritima
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
Thermotoga maritima
-
(S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
L-aspartate 4-semialdehyde + pyruvate
-
714351
Thermotoga maritima
(S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
-
-
?
4.3.3.7
additional information
the active site of the monomer is well conserved, with most active-site residues in the same conformation
714351
Thermotoga maritima
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.3.3.7
tetramer
4 * 34000, SDS-PAGE, role of quaternary structure in the TIM-barrel family of enzymes, overview. Unlike other DHDPS enzymes, but like many thermophilic enzymes, Tm-DHDPS has a large number of charged residues at the quaternary interface. Removal of electrostatic interactions disrupts quaternary structure
Thermotoga maritima
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
4.3.3.7
30
45
assay at 30C and at 45C
Thermotoga maritima
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3.3.7
35
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
35
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
39
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
39
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
52
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
52
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
63
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
63
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
68
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
68
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
88
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
88
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp237
Thermotoga maritima
4.3.3.7
97
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
97
-
pyruvate
pH not specified in the publication, 30C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
108
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
108
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp171
Thermotoga maritima
4.3.3.7
111
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
111
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168
Thermotoga maritima
4.3.3.7
134
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
134
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171/Arg237
Thermotoga maritima
4.3.3.7
136
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
136
-
pyruvate
pH not specified in the publication, 30C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
141
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
141
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp168/Asp237
Thermotoga maritima
4.3.3.7
233
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
233
-
pyruvate
pH not specified in the publication, 45C, recombinant mutant DELTAAsp171
Thermotoga maritima
4.3.3.7
465
-
L-aspartate 4-semialdehyde
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
4.3.3.7
465
-
pyruvate
pH not specified in the publication, 45C, recombinant wild-type enzyme
Thermotoga maritima
General Information
EC Number
General Information
Commentary
Organism
4.3.3.7
additional information
pyruvate binding occurs near the large interface of DHDPS, and is likely, therefore, to stabilize this solvent-accessible face, which favors the formation of a dimer rather than a monomer. For the DELTAAsp168/Arg237 and DELTAAsp168/Asp171 DHDPS variants addition of pyruvate shifts the equilibrium from primarily monomer to favor almost exclusively dimers. On the other hand, for the DELTAAsp168 DHDPS variant, the monomer-tetramer equilibrium shifts from primarily monomer to primarily tetramer on addition of pyruvate
Thermotoga maritima
General Information (protein specific)
EC Number
General Information
Commentary
Organism
4.3.3.7
additional information
pyruvate binding occurs near the large interface of DHDPS, and is likely, therefore, to stabilize this solvent-accessible face, which favors the formation of a dimer rather than a monomer. For the DELTAAsp168/Arg237 and DELTAAsp168/Asp171 DHDPS variants addition of pyruvate shifts the equilibrium from primarily monomer to favor almost exclusively dimers. On the other hand, for the DELTAAsp168 DHDPS variant, the monomer-tetramer equilibrium shifts from primarily monomer to primarily tetramer on addition of pyruvate
Thermotoga maritima