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
-
4.2.1.52
-
s-lysine
- drug development
- homoserine
- meso-diaminopimelate
- aspartokinase
- l-threonine
-
s-aspartate
- s-2-aminoethyl-l-cysteine
-
feedback-insensitive
-
lysine-insensitive
- beta-semialdehyde
- pharmacology
-
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
results (
results (Molecular Weight
Molecular Weight on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase
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MOLECULAR WEIGHT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
123000
124000
125300
tetramer size of wild-type protein, mass spectrometry, mutant form Y107W reveals a mixture of primarily monomer and tetramer in solution
130000
134000
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calculation from sedimentation and diffusion coefficient, Stokes' radius
150000
native protein, gel filtration
158000
native protein, gel filtration, homotetramer predicted
31000
34000
62400
72000
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4 * 37000-38000 + x * 72000, the 72000 Da subunit possibly modifies the structure and kinetic properties, SDS-PAGE
73000
approximating the size of two DHDPS proteins interacting to form a dimer
34000
size of monomer inccluding His-tag, calculated from sequence
34000
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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
62400
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4 * 62400, crystal structure, the tetrameric structure is not essential for activity in DHDPS from Mycobacterium tuberculosis
