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Information on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57695

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
The reaction can be divided into three consecutive steps: Schiff base formation with pyruvate, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product. The product of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1,2], and the enzyme was classified accordingly as EC 4.2.1.52, dihydrodipicolinate synthase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual product of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate , and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate synthase. However, the identity of the product is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all .
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Methanocaldococcus jannaschii
UNIPROT: Q57695
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Synonyms
dhdps, dihydrodipicolinate synthase, dhdps2, pa1010, dihydrodipicolinic acid synthase, cjdhdps, cdhdps, 4-hydroxy-tetrahydrodipicolinate synthase, mrsa-dhdps, dhdpa synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrodipicolinate synthase
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DHDPS
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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]
The reaction can be divided into three consecutive steps: Schiff base formation with pyruvate, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product. The product of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1,2], and the enzyme was classified accordingly as EC 4.2.1.52, dihydrodipicolinate synthase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual product of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate [3], and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate synthase. However, the identity of the product is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all [5].
CAS REGISTRY NUMBER
COMMENTARY hide
9055-59-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by the oil-batch method at 291 K, to 2.2 A resolution. Belongs to space group P21 with unit-cell parameters a = 80.5 A, b = 76.5 A, c = 101.9 A, gamma = 106.9 A. The asymmetric unit contains four DHDPS molecules, forming a homotetramer with approximate 222 symmetry. The overall tertiary structure of DHDPS possesses a (beta/alpha)8-barrel fold (TIM barrel) with three additional alpha-helices (alpha9-alpha11) at the C-terminus of the chain. The beta-strands of the barrel form an intrinsic network of hydrogen-bonding interactions with the neighbouring beta-strands and are oriented in the same directions. The functional residue Lys161, which participates in Schiff-base formation, is located within the beta-barrel and the side chain of Tyr132 sits over this residue
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the pET-21a expression vector and introduced into Escherichia coli Rosetta (DE3) strain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Padmanabhan, B.; Strange, R.W.; Antonyuk, S.V.; Ellis, M.J.; Hasnain, S.S.; Iino, H.; Agari, Y.; Bessho, Y.; Yokoyama, S.
Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii
Acta Crystallogr. Sect. F
65
1222-1226
2009
Methanocaldococcus jannaschii (Q57695), Methanocaldococcus jannaschii
Manually annotated by BRENDA team