Information on EC 3.3.2.1 - isochorismatase

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

EC NUMBER
COMMENTARY hide
3.3.2.1
-
RECOMMENDED NAME
GeneOntology No.
isochorismatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ether hydrolysis
-
-
-
-
hydrolysis of ether bond
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2,3-dihydroxybenzoate biosynthesis
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of siderophore group nonribosomal peptides
-
-
enterobactin biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
isochorismate pyruvate-hydrolase
The enzyme is involved in the biosynthesis of several siderophores, such as 2,3-dihydroxybenzoylglycine, enterobactin, bacillibactin, and vibriobactin.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-64-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additionally acts as (+)-gamma-lactamase and as amidase, EC 3.5.1.4
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isoform PchB, possessing mainly chorismate lyase activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
highly, Vd1396-9, and weakly, Vs06-14, aggressive isolates from soil
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
O1 biovar El Tor
UniProt
Manually annotated by BRENDA team
O1 biovar El Tor
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the biosynthesis of salicylic acid in plants occurs through phenylpropanoid and isochorismate pathways
physiological function
-
isochorismatase hydrolase may be acting as a plant-defense suppressor produced by the highly aggressive isolate to overcome host resistance
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+/-)-3-[(1-carboxyethenyl)oxy]-2-hydroxy-6-cyclohexene-1-carboxylic acid + H2O
3,4-dihydroxy-cyclohex-1-enecarboxylic acid + pyruvate
show the reaction diagram
-
-
-
?
(+/-)-3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate + H2O
(S)-3-hydroxy-cyclohepta-1,6-dienecarboxylic acid + pyruvate
show the reaction diagram
-
i.e. (S)-3-(1-carboxyvinyloxy)-cyclohepta-1,6-dienecarboxylic acid
-
?
(+/-)-3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid + H2O
(S)-3-hydroxycyclohex-1-enecarboxylic acid + pyruvate
show the reaction diagram
-
-
-
?
(+/-)-cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid + H2O
(R)-5-hydroxycyclohex-3-enecarboxylic acid + pyruvate
show the reaction diagram
-
-
-
?
Chorismate
Prephenate
show the reaction diagram
-
promiscuous reaction
-
-
?
chorismate + H2O
3,4-dihydroxy-cyclohexa-1,5-dienecarboxylic acid + pyruvate
show the reaction diagram
-
slow hydrolysis
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
show the reaction diagram
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
show the reaction diagram
isochorismate + H2O
salicylate + pyruvate
show the reaction diagram
-
main reaction
-
-
?
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
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
show the reaction diagram
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+/-)-3-[(carboxyethenyl)oxy]-6-hydroxy-1-benzoic acid
-
i.e. 5-(1-carboxyvinyloxy)-2-hydroxybenzoic acid
-
3-[(carboxyethenyl)oxy]benzoic acid
-
i.e. 3-(1-carboxyvinyloxy)benzoic acid
disodium 3-(2-carboxylatoethyl)benzoate
-
-
disodium 3-[(E)-2-carboxylatoethenyl]benzoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
(+/-)-3-[(1-carboxyethenyl)oxy]-2-hydroxy-6-cyclohexene-1-carboxylic acid
-
-
0.12
(+/-)-3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate
-
-
-
0.086
(+/-)-3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid
-
-
-
0.28
(+/-)-cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid
-
-
-
35
chorismate
-
-
0.015 - 1.06
isochorismate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.17
(+/-)-3-[(1-carboxyethenyl)oxy]-2-hydroxy-6-cyclohexene-1-carboxylic acid
Escherichia coli
-
-
9
(+/-)-3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate
Escherichia coli
-
-
-
21.7
(+/-)-3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid
Escherichia coli
-
-
-
16.3
(+/-)-cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid
Escherichia coli
-
-
-
0.003 - 217
chorismate
0.1 - 10
isochorismate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.282
disodium 3-(2-carboxylatoethyl)benzoate
-
pH and temperature not specified in the publication
0.122
disodium 3-[(E)-2-carboxylatoethenyl]benzoate
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.472
disodium 3-(2-carboxylatoethyl)benzoate
Escherichia coli
-
pH and temperature not specified in the publication
0.209
disodium 3-[(E)-2-carboxylatoethenyl]benzoate
Escherichia coli
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
a yeast two-hybrid assay is performed to screen the proteins interacting with p16INK4a in pretransformed human liver cDNA library, ISOC2 is identified as an interacting protein
Manually annotated by BRENDA team
additional information
-
proteomic analysis of highly, Vd1396-9, and weakly, Vs06-14, aggressive isolates from soil, isochorismatase family motifs occur in the secretome of five phytopathogenic but in no species of non-phytopathogenic filamentous ascomycete fungi
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
predominantly
Manually annotated by BRENDA team
-
small fraction membrane-bound, predominantly cytosolic
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19700
2 * 19700, calculated, 2 * 20000, SDS-PAGE
20000
2 * 19700, calculated, 2 * 20000, SDS-PAGE
23000
-
determinated by Western blot analysis
32400
-
x * 32400, calculated, x * 37000., SDS-PAGE
32554
-
5 * 32554, sequence of DNA
33090
calculated molecular mass
33100
determinecd by MALDI-TOF spectrometry
35000
-
5 * 35000, SDS-PAGE
159000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 32400, calculated, x * 37000., SDS-PAGE
homodimer
x-ray crystallography
pentamer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the EntB protein is determined at a resolution of 2.3 A
sitting drop vapor diffusion method, using 50 mM CaCl2, 0.1 M bis-Tris pH 6.5, 28% (w/v) polyethylene glycol monomethyl ether 550, 1% (w/v) n-octyl-beta-D-glucoside at 20C
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
stable within
735550
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
30 min, 38% residual activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 25 mM Tris buffer, pH 8.0, 5 mM dithiothreitol, 50% glycerol, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+ chelating Sepharose column chromatography and Superdex 200 gel filtration
purification is obtained by two metal chelate chromatography steps seperated by emoval of the His tag with TEV protease
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
angB gene, involved in anguibactin biosynthesis
-
expressed in Escherichia coli BL21(DE3) cells
into the pGEM7z and the pET15bTEV vector for expression in Escherichia coli BL21DE3 cells
ISOC2 cDNA is cloned into the pECFP and pCMV-HA vector
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D227R
mutant constructed for functional analysis of EntB-EntE interaction
D240R
mutant constructed for functional analysis of EntB-EntE interaction
D244R
mutant constructed for functional analysis of EntB-EntE interaction
D263R
mutant constructed for functional analysis of EntB-EntE interaction
F264E
mutant constructed for functional analysis of EntB-EntE interaction
I239D
mutant constructed for functional analysis of EntB-EntE interaction
K269E
mutant constructed for functional analysis of EntB-EntE interaction
M249E
mutant constructed for functional analysis of EntB-EntE interaction
R247E
mutant constructed for functional analysis of EntB-EntE interaction
S245A
mutant constructed for functional analysis of EntB-EntE interaction
D227R
-
mutant constructed for functional analysis of EntB-EntE interaction
-
D240R
-
mutant constructed for functional analysis of EntB-EntE interaction
-
I239D
-
mutant constructed for functional analysis of EntB-EntE interaction
-
K269E
-
mutant constructed for functional analysis of EntB-EntE interaction
-
S245A
-
mutant constructed for functional analysis of EntB-EntE interaction
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C118A
complete loss of activity
D9A
complete loss of activity
H51A
complete loss of activity
K84A
9% decrease in activity compared to wild-type
Q11A
20% decrease in activity compared to wild-type
Q91N
-
4fold reduction in kcat-value of enzymic activity, 10fold reduction in chorismate mutase activity
R54K
-
1000fold reduction in enzymic and in chorismate mutase activity
D35N
the mutation results in almost complete loss of enzyme activity
H34A
the mutant has about 80% of wild type activity
H34N
the mutant has about 35% of wild type activity
K118A
the mutant has about 30% of wild type activity
K118H
the mutation results in almost complete loss of enzyme activity
K118N
the mutation results in almost complete loss of enzyme activity
D35N
-
the mutation results in almost complete loss of enzyme activity
-
H34A
-
the mutant has about 80% of wild type activity
-
K118A
-
the mutant has about 30% of wild type activity
-
K118H
-
the mutation results in almost complete loss of enzyme activity
-
K118N
-
the mutation results in almost complete loss of enzyme activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
synthesis of homochiral cis-cyclohexa-3,5-diene-1,2-diols
Show AA Sequence (1573 entries)
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