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Information on EC 3.3.2.1 - isochorismatase and Organism(s) Escherichia coli and UniProt Accession P0ADI4

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EC Tree
     3 Hydrolases
         3.3 Acting on ether bonds
             3.3.2 Ether hydrolases
                3.3.2.1 isochorismatase
IUBMB Comments
The enzyme is involved in the biosynthesis of several siderophores, such as 2,3-dihydroxybenzoylglycine, enterobactin, bacillibactin, and vibriobactin.
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Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0ADI4
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
isochorismatase, isoc2, isochorismatase hydrolase, 2,3-dihydro-2,3-dihydroxybenzoate synthase, isochorismatase domain containing 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EntB
contains an N-terminal isochorismate lyase domain
2,3 dihydro-2,3 dihydroxybenzoate synthase
-
-
-
-
2,3-dihydro-2,3-dihydroxybenzoate synthase
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-
-
-
2,3-dihydroxy-2,3-dihydrobenzoate synthase
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-
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2,3-dihydroxy-2,3-dihydrobenzoic synthase
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-
-
-
SOI1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ether hydrolysis
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-
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-
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
-
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-carboxyethenyl)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 + 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
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
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
-
biosynthesis of enterobactin
-
?
INHIBITOR
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
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-
disodium 3-[(E)-2-carboxylatoethenyl]benzoate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
(+/-)-3-[(1-carboxyethenyl)oxy]-2-hydroxy-6-cyclohexene-1-carboxylic acid
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-
0.12
(+/-)-3-[(1-carboxyethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate
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-
0.086
(+/-)-3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid
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-
0.28
(+/-)-cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid
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-
35
chorismate
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-
0.015
isochorismate
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.17
(+/-)-3-[(1-carboxyethenyl)oxy]-2-hydroxy-6-cyclohexene-1-carboxylic acid
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-
9
(+/-)-3-[(1-carboxyethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate
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-
21.7
(+/-)-3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid
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-
16.3
(+/-)-cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid
-
-
217
chorismate
-
-
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
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33090
calculated molecular mass
33100
determinecd by MALDI-TOF spectrometry
159000
-
gel filtration
32554
-
5 * 32554, sequence of DNA
35000
-
5 * 35000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the EntB protein is determined at a resolution of 2.3 A
PROTEIN VARIANTS
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM Tris buffer, pH 8.0, 5 mM dithiothreitol, 50% glycerol, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification is obtained by two metal chelate chromatography steps seperated by emoval of the His tag with TEV protease
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the pGEM7z and the pET15bTEV vector for expression in Escherichia coli BL21DE3 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rusnak, F.; Liu, J.; Quinn, N.; Berchtold, G.A.; Walsh, C.T.
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase
Biochemistry
29
1425-1435
1990
Escherichia coli
Manually annotated by BRENDA team
Nahlik, M.S.; Fleming, T.P.; McIntosh, M.A.
Cluster of genes controlling synthesis and activation of 2,3-dihydroxybenzoic acid in production of enterobactin in Escherichia coli
J. Bacteriol.
169
4163-4170
1987
Escherichia coli
Manually annotated by BRENDA team
Hantash, F.M.; Earhart, C.F.
Membrane association of the Escherichia coli enterobactin synthase proteins EntB/G, EntE, and EntF
J. Bacteriol.
182
1768-1773
2000
Escherichia coli
Manually annotated by BRENDA team
Drake, E.J.; Nicolai, D.A.; Gulick, A.M.
Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain
Chem. Biol.
13
409-419
2006
Escherichia coli (P0ADI4)
Manually annotated by BRENDA team
Hubrich, F.; Mordhorst, S.; Andexer, J.N.
Cinnamic acid derivatives as inhibitors for chorismatases and isochorismatases
Bioorg. Med. Chem. Lett.
23
1477-1481
2013
Escherichia coli
Manually annotated by BRENDA team