Information on EC 5.4.99.5 - Chorismate mutase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
5.4.99.5
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RECOMMENDED NAME
GeneOntology No.
Chorismate mutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Chorismate = prephenate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
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intramolecular
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isomerization
rearrangement
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacilysin biosynthesis
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L-phenylalanine biosynthesis I
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L-phenylalanine biosynthesis II
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L-tyrosine biosynthesis I
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L-tyrosine biosynthesis II
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L-tyrosine biosynthesis III
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salinosporamide A biosynthesis
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phenylalanine metabolism
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Phenylalanine, tyrosine and tryptophan biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
Chorismate pyruvatemutase
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CAS REGISTRY NUMBER
COMMENTARY hide
9068-30-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Anthophyta
contain 3 isoenzymes with the exception of some closely related Leguminosae
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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SwissProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain 23 and its derivatives have 3 distinct enzyme species: CM1, CM2, and CM3. Strain 168 has only the CM3 form. Enzyme forms CM1 and CM2 may represent different aggregation states involving at least one common subunit
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Claviceps sp.
SD 58
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Manually annotated by BRENDA team
Claviceps sp. SD 58
SD 58
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
cress
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Orchard grass
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain JFM-30
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Manually annotated by BRENDA team
strain JM101
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Nephrolysis sp.
2 isoenzymes: CM1, CM2
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
2 enzyme forms: CM1 and CM2
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Manually annotated by BRENDA team
no activity in Corynebacterium diphtheriae
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Manually annotated by BRENDA team
no activity in Mycobacterium leprae
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Manually annotated by BRENDA team
no activity in Nocardia farcinica
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
2 enzyme forms: CM1 and CM3
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Manually annotated by BRENDA team
Penicillium duponti
3 enzyme forms: CM1, CM2, CM3
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Manually annotated by BRENDA team
cultivar Mitchell Diploid
UniProt
Manually annotated by BRENDA team
Pinus sp.
2 isoenzymes: CM1, CM2
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
2 isoenzymes: CM1 and CM2
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
Selaginella sp.
2 isoenzymes: CM1, CM2
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Streptomyces aureofaciens tue 24
tue 24
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Xanthomonas oryzae pv. oryzae XKK.12
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Manually annotated by BRENDA team
yeasts
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
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structure-function relationships of chorismate-utilizing enzymes, structure comparisons, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbachorismate
carbaprephenate
show the reaction diagram
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?
Chorismate
?
show the reaction diagram
Chorismate
Prephenate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Chorismate
?
show the reaction diagram
Chorismate
Prephenate
show the reaction diagram
additional information
?
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isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform the chorismate mutase reaction
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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enhances activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S,3S,5S,7S)-10-hydroxy-3-oxo-2-oxa-5-azatricyclo[4.3.1.1(4,8)]undecane-8-carboxylate, sodium salt
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does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
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(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
(1R,3R,5S,8R)-2-azatricyclo[3.3.1.0(1,8)]-non-6-ene-3,5-dicarboxylate, disodium salt
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exo arizidine analogue, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
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(1R,3R,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate, disodium salt
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does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
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(1R,3S,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate, disodium salt
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does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
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(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
(1S,3S,5R,6R)-6-hydroxy-4-oxabicyclo[3.3.1]non-7-ene-1,3-dicarboxylate
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endo-oxabicyclic dicarboxylic acid is a good geometric mimic of transition state
(1S,4S,6R,8S,10S)-3-oxo-5-aza-2-oxa-tetracyclo[4.3.1.(4,8).0(6,10)]undecane-8-carboxylate, sodium salt
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tetracyclic lactone, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
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(2E)-8-exo-3-Hydroximino-8-hydroxy-2-oxabicyclo-[3.3.1]non-6-ene-5-carboxylic acid
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poor
(2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid
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(3R,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
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(3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
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(3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
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1-Substituted adamantane derivatives
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order of decreasing inhibitory activity with the various substituents: -PO32-, -P(OCH3)O2, CO2-, -CH2CO2-, -SO2-,Y -SO3-
2-(1-Carboxy-1,4-dihydrobenzyl)acrylic acid
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3-Chloroadamantane-1-acetic acid
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3-endo,6-exo-6-Hydroxy-7-bicyclo[3.3.1]-nonene-1,3-dicarboxylic acid
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poor
3-endo,8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
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potent
4-Methyl-DL-Trp
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enzyme form CM1 is inhibited, enzyme form CM2 not
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
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5,5'-dithiobis(2-nitrobenzoate)
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6-Methyl-DL-Trp
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enzyme form CM1 is inhibited, enzyme form CM2 not
8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]nona-3,6-diene-3,5-dicarboxylic acid
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slight
8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
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competitive inhibition
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Adamantane-1-acetic acid
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adamantane-1-phosphonate
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no inhibitory effect up to concentrations of 0.1 and 1 mM
caffeic acid
chlorogenic acid
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enzyme forms CM1 and CM2 are inhibited, enzyme form CM3 is unaffected
chorismate
DL-3-fluoro-Phe
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enzyme form CM1 is inhibited, enzyme form CM2 not
DL-5-Fluoro-Trp
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enzyme form CM1 is inhibited, enzyme form CM2 not
DL-5-hydroxy-Trp
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enzyme form CM1 is inhibited, enzyme form CM2 not
endo-Oxabicylic transition state analogue inhibitor
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ferulic acid
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inhibits enzyme form CM3
iodoacetamide
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L-Trp
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96% residual activity at 0.2 mM
L-tryptophan
methyl 4-(methylamino)-3-nitrobenzoate
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N-[[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]carbonyl]leucine
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NaCl
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inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe
oxabicyclic dicarboxylic acid
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transition state analogon, competitive inhibition
p-coumaric acid
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inhibits enzyme form CM1, CM2 and CM3
prephenate
Transition state analogue inhibitor
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tyrosine
Zn2+
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strong
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dimethoxycinnamic acid
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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arabinose
expression can be induced by arabinose under the control of the araBAD promoter
caffeic acid
tryptophan
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 16
chorismate
0.47 - 1
prephenate
additional information
Chorismic acid
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 366000
chorismate
94100 - 94140
prephenate
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 1.75
chorismate
204
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.051
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
0.00032 - 0.0076
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
0.23
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
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30C, pH 7.5, wild-type
0.01771
(2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid
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0.0057
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
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4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid shows the most potent inhibition with Ki value of 0.0057 mM against MtCM
0.0037
8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
-
-
0.0028
chorismate
30C, pH 7.6, in presence of 0.005 mM tyrosine
0.0288
methyl 4-(methylamino)-3-nitrobenzoate
-
-
0.0211
N-[[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]carbonyl]leucine
-
-
0.003 - 1.1
oxabicyclic dicarboxylic acid
0.07 - 0.17
prephenate
0.034
tyrosine
70C, pH 7.6
additional information
oxabicyclic dicarboxylic acid
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>> 1 mM mutant C88S/R90K
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 18
Saccharomyces cerevisiae chorismate mutase inhibitors
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.44
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cell-free supernatant
25
after affinity chromatography
48.6
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after 110.4fold purification
168
Superdex 200pg pool
210
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recombinant enzyme
1200
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0.1 mM tyrosine, wild-type
3300
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0.1 mM tyrosine, mutant T226D
3700
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unliganded, mutant T226D
4800
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unliganded, wild-type
8400
0.1 mM tyrosine, wild-type
11100
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0.5 mM tryptophan, mutant T226D
13400
0.1 mM tyrosine, mutant D233I
20600
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unliganded, mutant T226I
21700
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0.1 mM tyrosine, mutant T226I
22000
0.1 mM tyrosine, mutant D233T
26400
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0.5 mM tryptophan, mutant T226I
30300
unliganded, mutant D233I
32500
unliganded, wild-type
40200
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0.5 mM tryptophan, wild-type
41300
unliganded, mutant D233T
63000
0.5 mM tryptophan, mutant D233I
64300
0.5 mM tryptophan, mutant D233T
88500
0.5 mM tryptophan, wild-type
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
catalytic maximum in presence of tyrosine
6 - 8
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enzyme form CM1 and CM2
6 - 10
6.2
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55000 MW enzyme form
6.4
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low-activity strain 168
6.6 - 7
7.1
catalytic maximum in presence of tryptophan
7.5 - 9.5
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enzyme form CM2
7.8
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enzyme form CM1
8
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in absence of Trp
8.9
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high activity strain WB672
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 37
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enzyme form CM1
38
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decrease in turnover at temperatures higher than 38C
48
maximum enzymatic activity
56
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enzyme form CM2
70
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As the temperature is lowered, distances of electrostatic and hydrophobic interactions decrease. The distance between Glu77-COOH and the hydroxyl oxygen decreases from the optimum
additional information
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The average structures of the thermophilic E.S complex at three different temperatures are obtained from the MD simulations. A snapshot of the most important features of the active site of the TtCM E.S complex at 70C is shown. At this temperature the Boltzmann distribution is primarily composed of reactive conformers - near attack conformers (NACs). The effects of the different temperatures on the distances in the structure are shown. The distances between electrostatic and hydrophobic pairs decrease as temperature decreases
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE