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Information on EC 4.2.3.5 - chorismate synthase and Organism(s) Helicobacter pylori and UniProt Accession P56122

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.5 chorismate synthase
IUBMB Comments
Requires FMN. The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH(.)). Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
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This record set is specific for:
Helicobacter pylori
UNIPROT: P56122
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Word Map
The taxonomic range for the selected organisms is: Helicobacter pylori
The enzyme appears in selected viruses and cellular organisms
Synonyms
chorismate synthase, chorismate synthetase, 5-enolpyruvylshikimate-3-phosphate phospholyase, vlaro2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-enolpyruvylshikimate-3-phosphate phospholyase
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chorismate synthetase
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-
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VEG216
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Vegetative protein 216
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SYSTEMATIC NAME
IUBMB Comments
5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase (chorismate-forming)
Requires FMN. The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH(.)). Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
CAS REGISTRY NUMBER
COMMENTARY hide
9077-07-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
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-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
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-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
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last step of shikimate pathway
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMNH2
required. The unique FMN-binding site is formed largely by a single subunit, with a small contribution from a neighboring subunit. The isoalloxazine ring of the bound FMN is significantly non-planar
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
198000
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dynamic light scattering analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of chorismate synthase in both FMN-bound and FMN-free form. It is a tetrameric enzyme, with each monomer possessing a novel beta-alpha-beta sandwich fold
hanging-drop vapour-diffusion method, crystallization at 296 K using polyethylene glycol 400 as precipitant, recombinant enzyme fused with an eight-residue C-terminal tag
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme fused with an eight-residue C-terminal tag
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli, fused with an eight-residue C-terminal tag
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ahn, H.J.; Yang, J.K.; Lee, B.I.; Yoon, H.J.; Kim, H.W.; Suh, S.W.
Crystallization and preliminary X-ray crystallographic studies of chorismate synthase from Helicobacter pylori
Acta Crystallogr. Sect. D
59
569-571
2003
Helicobacter pylori
Manually annotated by BRENDA team
Ahn, H.J.; Yoon, H.J.; Lee, B.2nd.; Suh, S.W.
Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights
J. Mol. Biol.
336
903-915
2004
Helicobacter pylori (P56122), Helicobacter pylori
Manually annotated by BRENDA team