4.3.3.7: 4-hydroxy-tetrahydrodipicolinate synthase
This is an abbreviated version!
For detailed information about 4-hydroxy-tetrahydrodipicolinate synthase, go to the full flat file.
Word Map on EC 4.3.3.7
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4.3.3.7
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diaminopimelate
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4.2.1.52
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s-lysine
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drug development
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homoserine
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meso-diaminopimelate
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aspartokinase
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l-threonine
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s-aspartate
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s-2-aminoethyl-l-cysteine
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feedback-insensitive
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lysine-insensitive
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beta-semialdehyde
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pharmacology
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l-aspartate-beta-semialdehyde
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2.7.2.4
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aspartate-derived
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medicine
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synthesis
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agriculture
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biotechnology
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industry
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food industry
- 4.3.3.7
- diaminopimelate
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4.2.1.52
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s-lysine
- drug development
- homoserine
- meso-diaminopimelate
- aspartokinase
- l-threonine
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s-aspartate
- s-2-aminoethyl-l-cysteine
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feedback-insensitive
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lysine-insensitive
- beta-semialdehyde
- pharmacology
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l-aspartate-beta-semialdehyde
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2.7.2.4
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aspartate-derived
- medicine
- synthesis
- agriculture
- biotechnology
- industry
- food industry
Reaction
Synonyms
Aq_1143, AT2G45440, BA3935 gene product, cDHDPS, CjDHDPS, DapA, DapA2, DHDPA synthase, DHDPS, DHDPS2, dihydro-dipicolinic acid synthase, dihydrodipicolinate synthase, dihydrodipicolinic acid synthase, dihydrodipocolinate synthase, dihydropicolinate synthetase, EC 4.2.1.52, FaDHDPS, HTPA synthase, More, MosA, MosA protein, MRSA-DHDPS, PA1010, pyruvate-aspartic semialdehyde condensing enzyme, Rv2753c, synthase, dihydrodipicolinate, VEG81, Vegetative protein 81
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Subunits
Subunits on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase
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dimer
homodimer
homotetramer
tetramer
additional information
dimer
three-dimensional structure determination shows that DHDPS forms a homodimer which is stabilized by several hydrogen bonds and van der Waals forces at the interface, active site structure, overview. Each monomer is composed of two domains, the N-terminal domain consists of residues 1-224, and forms an 8-fold parallel alpha/beta barrel
in solution and in the crystal, gel filtration, crystallization and dynamic light scattering experiments
homodimer
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in solution and in the crystal, gel filtration, crystallization and dynamic light scattering experiments
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the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state
homotetramer
Agrobacterium tumefaciens C58 / ATCC 33970
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the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state
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homotetramer
ribbons rendition of homotetramer in the crystal lattice shown
homotetramer
wild-type, mixture of primarily monomer and tetramer in solution determined for mutant form Y107W, hydrodynamic properties of Y107W oligomers calculated by sedimentation velocity analyses
homotetramer
the enzyme shows the typical homotetrameric form exhibited by bacterial DHDPS enzymes, present as a dimer of tight dimers. Each monomer consists of an N-terminal domain (residues 1-224) showing a parallel (beta/alpha)8-barrel (TIM barrel) motif. The smaller C-terminal domain, residues 224-292, is comprised of three alpha-helices
homotetramer
homotetramer of four identical (beta/alpha)8-barrel monomers, a dimer of tight dimers, with two tight-dimers binding in a head-to-head manner, with the active site situated near the center of the barrel, molecular dynamics simulations
the overall quaternary structure of the enzyme consists of four crystallographically independent molecules (A, C, D, and E) forming dimer of dimers. The monomer exhibits a TIM barrel fold and comprises of 11 alpha helices built by 146 amino acids out of which the first 8 helices form the TIM barrel domain and remaining three helices present in the C-terminal. The monomer also has 10 beta strands composed of 42 amino acids. The enzyme molecule has two types of dimer interfaces, weak-dimer interface and tight-dimer interfaces, structure model, overview
tetramer
similar to oligomeric states of other homologous enzyme
tetramer
homotetramer of (alpha/beta)8 barrels, each containing one active site, crystal structure
tetramer
the dimer-dimer interface is small, accounts only 4.3% of the subunit surface area
tetramer
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4 * 62400, crystal structure, the tetrameric structure is not essential for activity in DHDPS from Mycobacterium tuberculosis
tetramer
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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
tetramer
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4 * 37000-38000 + x * 72000, the 72000 Da subunit possibly modifies the structure and kinetic properties, SDS-PAGE
Q81WN7
the tetramer-dimer dissociation constant of the enzyme is 3fold tighter in the presence of pyruvate compared with the apo form
additional information
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the tetramer-dimer dissociation constant of the enzyme is 3fold tighter in the presence of pyruvate compared with the apo form
additional information
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the tetramer-dimer dissociation constant of the enzyme is 3fold tighter in the presence of pyruvate compared with the apo form
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additional information
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disruption of quaternary structure of DHDPS generates a functional monomer that is no longer inhibited by lysine, overview
additional information
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flexibility and its relationship to quaternary structure and function from molecular dynamic simulations of native tetrameric and mutant dimeric enzyme forms, it shows that the mutant dimeric enzyme form displays high flexibility, resulting in monomer reorientation within the dimer and increased flexibility at the tight-dimer interface, whereas the enzyme tetramer is relatively rigid. The enzyme dimer exhibits disorder within its active site with deformation of critical catalytic residues and removal of key hydrogen bonds that render it inactive
additional information
the recombinant enzyme adopts a characteristic alpha/beta conformation which is retained up to 65°C
additional information
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the recombinant enzyme adopts a characteristic alpha/beta conformation which is retained up to 65°C
additional information
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flexibility and its relationship to quaternary structure and function from molecular dynamic simulations show that the native dimeric enzyme form from a methicillin-resistant strain displays high flexibility, resulting in monomer reorientation within the dimer and increased flexibility at the tight-dimer interface and maintains its catalytic geometry and is thus fully functional