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Literature summary extracted from

  • Pearce, F.G.; Dobson, R.C.; Jameson, G.B.; Perugini, M.A.; Gerrard, J.A.
    Characterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization (2011), Biochim. Biophys. Acta, 1814, 1900-1909.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) 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

Protein Variants

EC Number Protein Variants Comment 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 Comment 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, 30°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 0.07
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 0.08
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 0.08
-
 pyruvate pH not specified in the publication, 30°C, recombinant wild-type enzyme Thermotoga maritima
4.3.3.7 0.1
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 0.15
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 0.15
-
 pyruvate pH not specified in the publication, 45°C, recombinant wild-type enzyme Thermotoga maritima
4.3.3.7 0.16
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 0.18
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 0.18
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 0.23
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 0.23
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant wild-type enzyme Thermotoga maritima
4.3.3.7 0.32
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 0.36
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant wild-type enzyme Thermotoga maritima
4.3.3.7 0.42
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 0.46
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 1.1
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 1.2
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima
4.3.3.7 1.3
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 1.5
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 1.5
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 1.7
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 1.7
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima
4.3.3.7 1.7
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima
4.3.3.7 2.1
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 2.2
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 2.4
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 2.6
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate Thermotoga maritima
-
 (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Thermotoga maritima
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate
-
 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 Thermotoga maritima ?
-
 ?

Subunits

EC Number Subunits Comment 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

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DHDPS
-
 Thermotoga maritima
4.3.3.7 More the enzyme belongs to the TIM-barrel family of enzymes Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.3.7 30 45 assay at 30°C and at 45°C Thermotoga maritima

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.3.7 35
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 35
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 39
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 39
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 52
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 52
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 63
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 63
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 68
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima
4.3.3.7 68
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima
4.3.3.7 88
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 88
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp237 Thermotoga maritima
4.3.3.7 97
-
 pyruvate pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 97
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 108
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 108
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp171 Thermotoga maritima
4.3.3.7 111
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 111
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168 Thermotoga maritima
4.3.3.7 134
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 134
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171/Arg237 Thermotoga maritima
4.3.3.7 136
-
 pyruvate pH not specified in the publication, 30°C, recombinant wild-type enzyme Thermotoga maritima
4.3.3.7 136
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 30°C, recombinant wild-type enzyme Thermotoga maritima
4.3.3.7 141
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima
4.3.3.7 141
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp237 Thermotoga maritima
4.3.3.7 233
-
 pyruvate pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 233
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171 Thermotoga maritima
4.3.3.7 465
-
 pyruvate pH not specified in the publication, 45°C, recombinant wild-type enzyme Thermotoga maritima
4.3.3.7 465
-
 L-aspartate 4-semialdehyde pH not specified in the publication, 45°C, recombinant wild-type enzyme Thermotoga maritima

General Information

EC Number General Information Comment 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