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
-
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
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Purification
Purification on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase
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by anion-exchange chromatography, hydrophobic interaction and gel filtration
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by centrifugation and gel filtration
by centrifugation, anion-exchange liquid chromatography and gel filtration, 2fold, more than 95% pure
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by gel filtration, recombinant enzyme in the absence of the substrate pyruvate (with a yield of 36.3%) and presence of the substrate pyruvate (with a yield of 98%)
Q81WN7
by sonication, anion-exchange and hydrophobic interaction liquid chromatography
Q81WN7
gel filtration
gel filtration, SDS-PAGE
mutant T44S, no pyruvate added to the crude extract prior to sonication, purified by heat shock and ion-exchange chromatography, 20.7fold with a yield of 123%
partial
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, followed by dialysis
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recombinant enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by two different steps of anion exchange chromatography, dialysis, hydroxyapatite chromatography, another step of anion exchange chromatography, and gel filtration, to homogeneity
recombinant His-tagged DHDPS 9.7fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged DHDPS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme 8fold from Escherichia coli strain BL21 (DE3) by immobilized metal affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) Star by nickel affinity chromatography, cleavage of the His-tag by TEV protease
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain XL1-Blue by nickel affinity chromatography
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recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant His-tagged isozymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography and gel filtration
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recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the proteolytic cleavage by TEV protease does not remove the N-terminal His6-tag efficiently
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, tag cleavage by thrombin, and gel filtration
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recombinant wild-type 5.8fold, recombinant mutant Y107F 17.6fold, recombinant mutant T44V 15.8fold, and recombinant mutant Y133F 18fold
wild-type DHDPS, and the coupling enzyme, DHDPR, by ammonium sulphate fractionation