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
ECTree
4.3.3.7 4-hydroxy-tetrahydrodipicolinate synthaseAdvanced search results
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Application on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
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expression of dapA gene of E coli, insensitive to feedback-inhibition by L-lysine
biotechnology
drug development
food industry
industry
considering the industrial application of this protein, such as its use for lysine biosynthesis, stable conformation via tight tetramerization interfaces may make this valuable protein to be more useful
medicine
pharmacology
synthesis
the enzyme can be commercially exploited for high-yield production of (S)-lysine
additional information
biotechnology
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enzyme is a target for herbicide and anti-microbial action
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drug development
the allosteric binding site of DHDPS may be a good starting point for development of an inhibitor specific to Neisseria meningitidis
drug development
the intracellular enzyme dihydrodipicolinate synthase a potential drug target because it is essential for the growth of bacteria while it is absent in humans
drug development
the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents
drug development
the enzyme is an attractive target for rational antibiotic and herbicide design
drug development
the enzyme is an attractive target for the design and synthesis of herbicides and antibiotics
drug development
Agrobacterium tumefaciens C58 / ATCC 33970
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the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents
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drug development
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the allosteric binding site of DHDPS may be a good starting point for development of an inhibitor specific to Neisseria meningitidis
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food industry
L-lysine, one of the essential amino acids required for nutrition in animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase
food industry
Escherichia coli LATR11
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L-lysine, one of the essential amino acids required for nutrition in animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase
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medicine
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development of species-specific inhibitors of DHDPS as potential antibacterials
medicine
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development of species-specific inhibitors of DHDPS as potential antibacterials
medicine
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development of species-specific inhibitors of DHDPS as potential antibacterials
medicine
L-lysine, one of the essential amino acids required for nutritionin animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase
medicine
Escherichia coli LATR11
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L-lysine, one of the essential amino acids required for nutritionin animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase
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pharmacology
enzyme structure analysis for design of novel therapeutics against bacterial pathogen
pharmacology
structure of the enzyme guides the design of novel therapeutics against the methicillin-resistant pathogen
pharmacology
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structure of the enzyme guides the design of novel therapeutics against the methicillin-resistant pathogen
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pharmacology
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enzyme structure analysis for design of novel therapeutics against bacterial pathogen
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additional information
the enzyme is not an optimal target for drug development against Pseudomonas aeruginosa
additional information
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the enzyme is not an optimal target for drug development against Pseudomonas aeruginosa
