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Information on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase and Organism(s) Hahella chejuensis and UniProt Accession Q2S9K4

for references in articles please use BRENDA:EC4.3.3.7
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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.3 Amine-lyases
                4.3.3.7 4-hydroxy-tetrahydrodipicolinate synthase
IUBMB Comments
Studies of the enzyme from the bacterium Escherichia coli have shown that the reaction can be divided into three consecutive steps: Schiff base formation between pyruvate and an active-site lysine, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product.
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This record set is specific for:
Hahella chejuensis
UNIPROT: Q2S9K4
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Hahella chejuensis
Synonyms
dhdps, dihydrodipicolinic acid synthase, cdhdps, dhdps2, mrsa-dhdps, pa1010, dhdpa synthase, rv2753c, dapa2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DHDPS
dihydrodipicolinate synthase
291296
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dihydrodipicolinic acid synthase
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dihydropicolinate synthetase
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pyruvate-aspartic semialdehyde condensing enzyme
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synthase, dihydrodipicolinate
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VEG81
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Vegetative protein 81
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate-4-semialdehyde hydro-lyase [adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming]
Studies of the enzyme from the bacterium Escherichia coli have shown that the reaction can be divided into three consecutive steps: Schiff base formation between pyruvate and an active-site lysine, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product.
CAS REGISTRY NUMBER
COMMENTARY hide
9055-59-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
crystallography
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
at 239K using the hanging drop-vapor diffusion method, at 1.5 A resolution. The four subunits of the asymmetric unit assemble to form a tetramer with an approximate 222 symmetry. At the active site, three residues Tyr132, Thr43 and Tyr106 are observed to constitute a catalytic triad. Has a unique extensive dimer–dimer interface that is mediated by strong hydrophobic interactions supplemented by two sets of three hydrogen bonds between four polar residues. Belongs to space group P2(1)2(1)2(1) with cell parameters a = 67.03 A, b = 120.52 A, c = 161.1 A
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
by centrifugation and gel filtration
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
ligated into the expression vector pET30a and transformed into the Escherichia coli strain B834 for overexpression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kang, B.S.; Kim, Y.G.; Ahn, J.W.; Kim, K.J.
Crystal structure of dihydrodipicolinate synthase from Hahella chejuensis at 1.5 A resolution
Int. J. Biol. Macromol.
46
512-516
2010
Hahella chejuensis, Hahella chejuensis (Q2S9K4)
Manually annotated by BRENDA team
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