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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General Information
General Information on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase
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malfunction
metabolism
physiological function
additional information
enzyme mutants with deleted dapA gene are viable and able to grow in a mouse lung infection model
malfunction
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the FaDHDPS1 deletion mutant is defective in conidiation, virulence and deoxynivalenol biosynthesis. In addition, deletion of FaDHDPS1 results in tolerance to sodium pyruvate, lysine, low temperature and Congo red
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sequential production of dihydrodipicolinate and dipicolinic acid appears to be catalysed by DHDPA synthase followed by an electron transfer flavoprotein, EtfA from Clostridium perfringens. Spontaneous dipicolinic acid formation in the presence of high concentrations of DapA
metabolism
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DHDPS is an oligomeric enzyme that catalyzes the first committed step of the lysine biosynthesis pathway in plants and bacteria, which yields essential building blocks for cell-wall and protein synthesis
metabolism
first enzyme unique to the diaminopimelate pathway of lysine biosynthesis
metabolism
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dihydrodipicolinate synthase is a key enzyme in the lysine biosynthesis pathway that catalyzes the condensation of pyruvate and aspartate semi-aldehyde
metabolism
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feedback regulation of the enzyme is directly correlated to L-lysine production
metabolism
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lysine biosynthesis in plants is tightly regulated by feedback inhibition of the end product on dihydrodipicolinate synthase, the first enzyme of the lysine-specific branch
metabolism
lysine biosynthesis in plants is tightly regulated by feedback inhibition of the end product on dihydrodipicolinate synthase, the first enzyme of the lysine-specific branch
metabolism
the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
metabolism
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the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
metabolism
the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
metabolism
the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
metabolism
the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
metabolism
the enzyme catalyzes the branch-point reaction in the biosynthetic pathway leading to meso-diaminopimelate and (S)-lysine in plants and bacteria: condensation of (S)-aspartate-4-semialdehyde and pyruvate to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid. There are four variants of the meso-diaminopimelate/(S)-lysine pathway, they all share the same enzymatic steps for the synthesis of tetrahydrodipicolinate from aspartate, which includes the reaction catalyzed by the enzyme, overview
metabolism
the enzyme catalyzes the first step in the diaminopimelic acid pathway of lysine biosynthesis
metabolism
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the enzyme catalyzes a step of the diaminopimelate biosynthetic pathway of lysine
metabolism
the enzyme catalyzes a step of the diaminopimelate biosynthetic pathway of lysine
metabolism
the enzyme catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis
metabolism
the enzyme catalyzes the first committed step in the diaminopimelate pathway
metabolism
the enzyme catalyzes the first committed step in the lysine biosynthesis pathway of plants
metabolism
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the enzyme catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis
-
metabolism
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DHDPS is an oligomeric enzyme that catalyzes the first committed step of the lysine biosynthesis pathway in plants and bacteria, which yields essential building blocks for cell-wall and protein synthesis
-
metabolism
-
the enzyme catalyzes a step of the diaminopimelate biosynthetic pathway of lysine
-
metabolism
-
the enzyme catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis
-
metabolism
Agrobacterium tumefaciens C58 / ATCC 33970
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the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
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metabolism
Agrobacterium tumefaciens C58 / ATCC 33970
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the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
-
metabolism
-
feedback regulation of the enzyme is directly correlated to L-lysine production
-
metabolism
-
the enzyme catalyzes the first committed step in the diaminopimelate pathway
-
metabolism
-
lysine biosynthesis in plants is tightly regulated by feedback inhibition of the end product on dihydrodipicolinate synthase, the first enzyme of the lysine-specific branch
-
complementation of the auxotrophy of Escherichia coli XL1-Blue KanRDELTAdapA cells only with the plasmid pUCX:dapA encoding wild-type DHDPS
physiological function
DHDPS can recover the DHDPS-deleted mutant of Escherichia coli
physiological function
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DHDPS catalyses a branch point reaction the condensation of pyruvate and (S)-aspartate beta-semialdehyde to form an unstable product, (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid, which is ultimately advanced to the final metabolites (S)-lysine and meso-diaminopimelate
physiological function
the enzyme catalyzes a rate-limiting step in the (S)-lysine biosynthetic pathway, which is regulated by a feedback mechanism through lysine
physiological function
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FaDHDPS1 plays an important role in the regulation of vegetative differentiation, pathogenesis and adaption to multiple stresses in Fusarium asiaticum. It is involved in diverse cellular processes in filamentous fungi Fusarium asiaticum, including conidiation, conidial germination, cell wall pressure response, low temperature tolerance, carbon/nitrogen sources utilization, secondary metabolism and virulence
physiological function
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the enzyme catalyzes a step in the pathway for the biosynthesis of L-lysine
physiological function
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the enzyme catalyzes a step in the pathway for the biosynthesis of L-lysine
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monomeric species exhibit an enhanced propensity for aggregation and inactivation, indicating that whilst the oligomerization is not an intrinsic criterion for catalysis, higher oligomeric forms may benefit from both increased catalytic efficiency and diminished aggregation propensity
additional information
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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
additional information
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the tetrameric structure is not essential for activity in DHDPS from Mycobacterium tuberculosis
additional information
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optimal activity is achieved by minimizing the inherent dimer flexibility using buttressing two dimers together in the case of the Escherichia coli tetrameric enzyme, active site structure simulations, overview
additional information
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optimal activity is achieved by minimizing the inherent dimer flexibility using strengthening and extending the dimer interface in the dimeric Staphylococcus aurus MRSA strain enzyme, active site structure simulations, overview
additional information
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structure comparison with the enzyme from Corynebacterium glutamicum
additional information
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structure comparison with the enzyme from Escherichia coli
additional information
structure-based sequence alignments, based on the DapA crystal structure, reveal the presence of two homologues, PA0223 and PA4188, in Pseudomonas aeruginosa that can substitute for DapA in the PAO1DELTAdapA mutant. In vitro experiments using recombinant PA0223 protein do not detect any DapA activity
additional information
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structure-based sequence alignments, based on the DapA crystal structure, reveal the presence of two homologues, PA0223 and PA4188, in Pseudomonas aeruginosa that can substitute for DapA in the PAO1DELTAdapA mutant. In vitro experiments using recombinant PA0223 protein do not detect any DapA activity
additional information
the catalytic site of DHDPS is situated at the C-terminal end of the TIM barrel where the pyruvate-binding residue, Lys161, lies in a solvent-accessible cleft with Arg138 capping the binding site. One-half of the active site is blocked by binding interactions of another monomer
additional information
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the catalytic site of DHDPS is situated at the C-terminal end of the TIM barrel where the pyruvate-binding residue, Lys161, lies in a solvent-accessible cleft with Arg138 capping the binding site. One-half of the active site is blocked by binding interactions of another monomer
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
-
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
additional information
the enzyme has unique disulfide linkage which is critical for the stability of the enzyme tetramer, but is not conserved in homologous enzymes, molecular dynamics simulation of the native structure of the enzyme tetramer and dimeric units containing complexes of enzyme-pyruvate or enzyme-lysine, enzyme structure comparisons and ligand docking analysis, overview
additional information
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the enzyme has unique disulfide linkage which is critical for the stability of the enzyme tetramer, but is not conserved in homologous enzymes, molecular dynamics simulation of the native structure of the enzyme tetramer and dimeric units containing complexes of enzyme-pyruvate or enzyme-lysine, enzyme structure comparisons and ligand docking analysis, overview
additional information
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structure comparison with the enzyme from Escherichia coli
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additional information
Agrobacterium tumefaciens C58 / ATCC 33970
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the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
-
additional information
-
structure comparison with the enzyme from Corynebacterium glutamicum
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