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Information on EC 4.2.3.5 - chorismate synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P28777

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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:
Saccharomyces cerevisiae
UNIPROT: P28777
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
chorismate synthase, chorismate synthetase, vlaro2, 5-enolpyruvylshikimate-3-phosphate phospholyase, 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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-
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Vegetative protein 216
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
combination with flavin reductase activity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-trans elimination
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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
5-O-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
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?
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
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-
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?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
additional information
?
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enzyme shows flavin reductase activity
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?
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
seventh enzyme of shikimate pathway
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?
5-O-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme in shikimate pathway
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMNH2
absolute requirement
flavins
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required, reduced forms e.g. FMN, FAD
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FMNH2
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absolute requirement, Km: 42 nM
NADPH
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required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0097
O5-(1-carboxyvinyl)-3-phosphoshikimate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40800
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 40800, calculated from amino acid sequence
dimer
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2 * 40800, dimer or tetramer
tetramer
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4 * 40800, dimer or tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, three-dimensional X-ray structure from selenomethionine-labeled crystals at 2.2 A resolution. The structure shows a novel beta,alpha,beta,alpha fold consisting of an alternate tight packing of two alpha-helical and two beta-sheet layers. The molecule is arranged as a tight tetramer with D2 symmetry
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strains BL21(DE3) and DV1017 (the latter lacks chorismate synthase activity)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Henstrand, J.M.; Schaller, A.; Braun, M.; Amrhein, N.; Schmid, J.
Saccharomyces cerevisiae chorismate synthase has a flavin reductase activity
Mol. Microbiol.
22
859-866
1996
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Quevillon-Cheruel, S.; Leulliot, N.; Meyer, P.; Graille, M.; Bremang, M.; Blondeau, K.; Sorel, I.; Poupon, A.; Janin, J.; van Tilbeurgh, H.
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae
J. Biol. Chem.
279
619-625
2004
Saccharomyces cerevisiae (P28777), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Macheroux, P.; Schmid, J.; Amrhein, N.; Schaller, A.
A unique reaction in a common pathway. Mechanism and function of chorismate synthase in the shikimate pathway
Planta
207
325-334
1999
Bacillus subtilis (P31104), Capnoides sempervirens (P27793), Escherichia coli, Euglena gracilis, Neurospora crassa (Q12640), Saccharomyces cerevisiae, Solanum lycopersicum, Staphylococcus aureus
Manually annotated by BRENDA team
Slesareva, A.; Kuhn, L.; Doroshenko, V.
Comparative analysis of mono- and bifunctional chorismate synthases in Escherichia coli cells capable and incapable of phenylalanine production
Appl. Biochem. Microbiol.
53
867-873
2017
Saccharomyces cerevisiae, Escherichia coli
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Manually annotated by BRENDA team