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Information on EC 5.4.99.5 - chorismate mutase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32178

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.5 chorismate mutase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P32178 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
chorismate mutase, p-protein, chorismate mutase/prephenate dehydratase, chorismate mutase-prephenate dehydrogenase, bacillus subtilis chorismate mutase, cm type 2, atcm1, rv1885c, cm0819, chorismate mutase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chorismate mutase
-
-
Chorismate mutase/prephenate dehydratase
-
-
-
-
Mutase, chorismate
-
-
-
-
P protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Chorismate pyruvatemutase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9068-30-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Chorismate
Prephenate
show the reaction diagram
Chorismate
Prephenate
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
Chorismate
Prephenate
show the reaction diagram
Chorismate
Prephenate
show the reaction diagram
-
enzyme of the first branch point of aromatic amino acid biosynthesis
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tyrosine
heterotrophic feedback inhibitor
endo-Oxabicylic transition state analogue inhibitor
-
-
-
L-Tyr
-
wild-type enzyme is inhibited. Mutant enzymes with amino acid exchange at Thr234, especially Tyr234Phe, mutant enzyme Ile225Thr and Ile225Thr/Thr226Ile are insensitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tryptophan
heterotrophic positive effector
L-Trp
-
wild-type enzyme, mutant enzyme Ile225Thr/Thr226Ile and enzymes with mutations at Tyr234 are activated. No activation of mutant enzyme Thr226Ile
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 6.3
chorismate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14 - 625
chorismate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11100
-
0.5 mM tryptophan, mutant T226D
1200
-
0.1 mM tyrosine, wild-type
20600
-
unliganded, mutant T226I
21700
-
0.1 mM tyrosine, mutant T226I
26400
-
0.5 mM tryptophan, mutant T226I
3300
-
0.1 mM tyrosine, mutant T226D
3700
-
unliganded, mutant T226D
40200
-
0.5 mM tryptophan, wild-type
4800
-
unliganded, wild-type
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
decrease in turnover at temperatures higher than 38°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the T state of the allosteric enzyme and comparison with the R state
-
crystal structure of wild-type enzyme cocrystallized with Trp and an endo-exabicyclic transition state analogue inhibitor, of wild-type enzyme cocrystallized with Tyr and the endo-oxabicyclic transition state analogue inhibitor and of the Thr226Ser mutant enzyme in complex with Trp
-
Thr226Ile mutant enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E23D
abolishes the substrate-induced homotrophic effect, but retains the effector-induced heterotrophic effecs, the coupling between helix 11 and helix 12 is weakened
N139L/R156L
increase in global flexibility
I225T
-
mutant enzyme Ile225Thr is activated by Trp, but is insensitive to Tyr
T226D
-
reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
T226I
Y234F
-
enzymes with mutations of Tyr234, especially Tyr234Phe are unresponsive to Tyr but are activated by Trp
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ball, S.G.; Wickner, R.B.; Cottarel, G.; Schmaus, M.; Tirtiaux, C.
Chorismate mutase-prephenate dehydratase from Escherichia coli
Mol. Gen. Genet.
205
326-330
1986
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Xue, Y.; Lipscomb, W.N.; Graf, R.; Schnappauf, G.; Braus, G.
The crystal structure of allosteric chorismate mutase at 2.2-A resolution
Proc. Natl. Acad. Sci. USA
91
10814-10818
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Xue, Y.; Lipscomb, W.N.
The crystallization and preliminary X-ray analysis of allosteric chorismate mutase
J. Mol. Biol.
241
273-274
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Strter, N.; Schnappauf, G.; Braus, G.; Lipscomb, W.N.
Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures
Structure
5
1437-1452
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Schnappauf, G.; Lipscomb, W.N.; Braus, G.H.
Separation of inhibition and activation of the allosteric yeast chorismate mutase
Proc. Natl. Acad. Sci. USA
95
2868-2873
1998
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Strter, N.; Hakansson, K.; Schnappauf, G.; Braus, G.; Lipscomb, W.N.
Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state
Proc. Natl. Acad. Sci. USA
93
3330-3334
1996
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Krappmann, S.; Pries, R.; Gellissen, G.; Hiller, M.; Braus, G.H.
HARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula polymorpha and is derepressed upon methanol utilization
J. Bacteriol.
182
4188-4197
2000
Saccharomyces cerevisiae (P32178), Saccharomyces cerevisiae, Ogataea angusta (Q9P4D8), Ogataea angusta
Manually annotated by BRENDA team
Krappmann, S.; Helmstaedt, K.; Gerstberger, T.; Eckert, S.; Hoffmann, B.; Hoppert, M.; Schnappauf, G.; Braus, G.H.
The aroC gene of Aspergillus nidulans codes for a monofunctional, allosterically regulated chorismate mutase
J. Biol. Chem.
274
22275-22282
1999
Saccharomyces cerevisiae, Aspergillus nidulans (Q9Y7B2), Aspergillus nidulans
Manually annotated by BRENDA team
Kong, Y.; Ma, J.; Karplus, M.; Lipscomb, W.N.
The allosteric mechanism of yeast chorismate mutase: a dynamic analysis
J. Mol. Biol.
356
237-247
2006
Saccharomyces cerevisiae (P32178), Saccharomyces cerevisiae
Manually annotated by BRENDA team