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Information on EC 3.3.2.1 - isochorismatase
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EC Tree
3.3.2.1 isochorismataseIUBMB Comments
The enzyme is involved in the biosynthesis of several siderophores, such as 2,3-dihydroxybenzoylglycine, enterobactin, bacillibactin, and vibriobactin.
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Word Map
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3 dihydro-2,3 dihydroxybenzoate synthase
-
-
-
-
2,3-dihydro-2,3-dihydroxybenzoate synthase
-
-
-
-
2,3-dihydroxy-2,3-dihydrobenzoate synthase
-
-
-
-
2,3-dihydroxy-2,3-dihydrobenzoic synthase
-
-
-
-
AngB
AngB-ISC
EntB
ISC
ISOC2
isochorismatase
isochorismatase domain containing 2
isochorismate lyase
SOI1
-
-
-
-
VabB
VabB-ISC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
-
isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
(1,5)-sigmatropic reaction mechanism that invokes electrostatic catalysis
-
isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
extended active site is formed by inter-subunit association within a tetramer
-
isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
extended active site is formed by inter-subunit association within a tetramer
-
isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
extended active site is formed by inter-subunit association within a tetramer
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ether hydrolysis
-
-
-
-
hydrolysis of ether bond
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37288-64-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
(+/-)-3-[(1-carboxyethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate + H2O
(S)-3-hydroxy-cyclohepta-1,6-dienecarboxylic acid + pyruvate
-
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
-
-
-
?
(+/-)-cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid + H2O
(R)-5-hydroxycyclohex-3-enecarboxylic acid + pyruvate
-
-
-
?
chorismate + H2O
3,4-dihydroxy-cyclohexa-1,5-dienecarboxylic acid + pyruvate
-
slow hydrolysis
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
biosynthesis of enterobactin
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
main reaction
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
isochorismatase converts isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate and inhibits salicylic acid formation
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
biosynthesis of enterobactin
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
-
-
?
isochorismate + H2O
2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
-
isochorismatase converts isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate and inhibits salicylic acid formation
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
additional information
structure-based design of virulence inhibitors against Vibrio anguillarum, overview. The isochorismatase family can bind endogenous metabolite during the hetero-expression process, which is likely nicotinic acid, nicotinamide or pyrazinic acid, based on structural analysis and affinity prediction; structure-based design of virulence inhibitors against Vibrio anguillarum, overview. The isochorismatase family can bind endogenous metabolite during the hetero-expression process, which is likely nicotinic acid, nicotinamide or pyrazinic acid, based on structural analysis and affinity prediction
-
additional information
structure-based design of virulence inhibitors against Vibrio anguillarum, overview. The isochorismatase family can bind endogenous metabolite during the hetero-expression process, which is likely nicotinic acid, nicotinamide or pyrazinic acid, based on structural analysis and affinity prediction; structure-based design of virulence inhibitors against Vibrio anguillarum, overview. The isochorismatase family can bind endogenous metabolite during the hetero-expression process, which is likely nicotinic acid, nicotinamide or pyrazinic acid, based on structural analysis and affinity prediction
-
additional information
-
structure-based design of virulence inhibitors against Vibrio anguillarum, overview. The isochorismatase family can bind endogenous metabolite during the hetero-expression process, which is likely nicotinic acid, nicotinamide or pyrazinic acid, based on structural analysis and affinity prediction; structure-based design of virulence inhibitors against Vibrio anguillarum, overview. The isochorismatase family can bind endogenous metabolite during the hetero-expression process, which is likely nicotinic acid, nicotinamide or pyrazinic acid, based on structural analysis and affinity prediction
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Knockdown of ISOC1 suppresses cell proliferation in pancreatic cancer in vitro.
Gastrointestinal Neoplasms
Isochorismatase domain-containing protein 1 (ISOC1) participates in DNA damage repair and inflammation-related pathways to promote lung cancer development.
Infections
Critical role of bacterial isochorismatase in the autophagic process induced by Acinetobacter baumannii in mammalian cells.
Iron Deficiencies
Bacterial production of transdihydroxycyclohexadiene carboxylates by metabolic pathway engineering.
Lung Neoplasms
Isochorismatase domain-containing protein 1 (ISOC1) participates in DNA damage repair and inflammation-related pathways to promote lung cancer development.
Neoplasms
Identification and characterization of a novel protein ISOC2 that interacts with p16INK4a.
Stomach Neoplasms
ISOC1 promotes the proliferation of gastric cancer cells by positively regulating CDK19.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
(+/-)-3-[(1-carboxyethenyl)oxy]-2-hydroxy-6-cyclohexene-1-carboxylic acid
-
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.17
(+/-)-3-[(1-carboxyethenyl)oxy]-2-hydroxy-6-cyclohexene-1-carboxylic acid
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
additionally acts as (+)-gamma-lactamase and as amidase, EC 3.5.1.4
UniProt
brenda
highly, Vd1396-9, and weakly, Vs06-14, aggressive isolates from soil
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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
brenda
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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
small fraction membrane-bound, predominantly cytosolic
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the biosynthesis of salicylic acid in plants occurs through phenylpropanoid and isochorismate pathways
physiological function
additional information
physiological function
-
isochorismatase hydrolase may be acting as a plant-defense suppressor produced by the highly aggressive isolate to overcome host resistance
physiological function
isochorismatase (ISC) converts isochorismate to (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate, which is a critical step for the siderophore synthesis. Two different siderophores, anguibactin and vanchrobactin, are described in Vibrio anguillarum, both siderophores belong to the catecholate group, sharing a 2,3-dihydroxybenzoic acid (DHBA) moiety
physiological function
-
isochorismatase (ISC) converts isochorismate to (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate, which is a critical step for the siderophore synthesis. Two different siderophores, anguibactin and vanchrobactin, are described in Vibrio anguillarum, both siderophores belong to the catecholate group, sharing a 2,3-dihydroxybenzoic acid (DHBA) moiety
-
physiological function
-
isochorismatase (ISC) converts isochorismate to (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate, which is a critical step for the siderophore synthesis. Two different siderophores, anguibactin and vanchrobactin, are described in Vibrio anguillarum, both siderophores belong to the catecholate group, sharing a 2,3-dihydroxybenzoic acid (DHBA) moiety
-
additional information
isochorismatase domains of AngB and VabB from Vibrio anguillarum, which are required to synthesize the critical virulence factor siderophore, are highly similar to known isochorismatases in fold and active site. Active site structure analysis, overview
additional information
isochorismatase domains of AngB and VabB from Vibrio anguillarum, which are required to synthesize the critical virulence factor siderophore, are highly similar to known isochorismatases in fold and active site. Active site structure analysis, overview
additional information
-
isochorismatase domains of AngB and VabB from Vibrio anguillarum, which are required to synthesize the critical virulence factor siderophore, are highly similar to known isochorismatases in fold and active site. Active site structure analysis, overview
additional information
-
isochorismatase domains of AngB and VabB from Vibrio anguillarum, which are required to synthesize the critical virulence factor siderophore, are highly similar to known isochorismatases in fold and active site. Active site structure analysis, overview
-
additional information
-
isochorismatase domains of AngB and VabB from Vibrio anguillarum, which are required to synthesize the critical virulence factor siderophore, are highly similar to known isochorismatases in fold and active site. Active site structure analysis, overview
-
Show AA Sequence and Transmembrane Helices (4481 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19700
2 * 19700, calculated, 2 * 20000, SDS-PAGE
20000
2 * 19700, calculated, 2 * 20000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
pentamer
additional information
dimer
2 * 19700, calculated, 2 * 20000, SDS-PAGE
hexamer
six polypeptide chains are located in one asymmetric unit and appear to form hexamer, a trimer of dimers, for each monomer, the helix-sheet-helix sandwich architecture is determined
hexamer
-
six polypeptide chains are located in one asymmetric unit and appear to form hexamer, a trimer of dimers, for each monomer, the helix-sheet-helix sandwich architecture is determined
-
hexamer
-
six polypeptide chains are located in one asymmetric unit and appear to form hexamer, a trimer of dimers, for each monomer, the helix-sheet-helix sandwich architecture is determined
-
additional information
-
extended active site is formed by inter-subunit association within a tetramer
additional information
-
extended active site is formed by inter-subunit association within a tetramer
additional information
-
extended active site is formed by inter-subunit association within a tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the EntB protein is determined at a resolution of 2.3 A
purified recombinant detagged AngB-ISC, sitting drop vapor diffusion, mixing of 18 mg/ml protein in 10 mM HEPES, pH 7.5, 500 mM NaCl, and 1 mM DTT, with reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 2 M Li2SO4, and 2% PEG 400, at 20°C, X-ray diffraction structure determination and analysis, molecular replacement using structure VibB-ISC (PDB ID 3TB4) as the searching model, with two monomers in an asymmetric unit
purified recombinant detagged VabB-ISC, sitting drop vapor diffusion, mixing of 18 mg/ml protein in 10 mM HEPES, pH 7.5, 150 mM NaCl, and 1 mM DTT, with reservoir solution containing 10% PEG 8000, 0.1 M imidazole, and 0.2 M calcium acetate, at 20°C, X-ray diffraction structure determination and analysis, molecular replacement using the AngB-ISC dimer as search model
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 20°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM Tris buffer, pH 8.0, 5 mM dithiothreitol, 50% glycerol, stable for several months
-
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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
recombinant N-terminally His6-tagged AngB-ISC encoding residues 1-216 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by TEV protease, another step of nickel affinity chromatography, and gel filtration
recombinant N-terminally His6-tagged VabB-ISC encoding residues 1-217 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by TEV protease, another step of nickel affinity chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene angB-ISC encoding residues 1-216, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene vabB-ISC encoding residues 1-217, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
into the pGEM7z and the pET15bTEV vector for expression in Escherichia coli BL21DE3 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Young, I.G.; Gibson, F.
Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli
Biochim. Biophys. Acta
177
401-411
1969
Klebsiella aerogenes
brenda
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
brenda
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
brenda
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
brenda
Muller, R.; Breuer, M.; Wagner, A.; Schmidt, K.; Leistner, E.
Bacterial production of transdihydroxycyclohexadiene carboxylates by metabolic pathway engineering
Microbiology
142
1005-1012
1996
Klebsiella pneumoniae
-
brenda
Welch, T.J.; Chai, S.; Crosa, J.H.
The overlapping angB and angG genes are encoded within the trans-acting factor region of the virulence plasmid in Vibrio anguillarum: essential role in siderophore biosynthesis
J. Bacteriol.
182
6762-6773
2000
Vibrio anguillarum
brenda
Kunzler, D.E.; Sasso, S.; Gamper, M.; Hilvert, D.; Kast, P.
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection
J. Biol. Chem.
280
32827-32834
2005
Pseudomonas aeruginosa
brenda
Caruthers, J.; Zucker, F.; Worthey, E.; Myler, P.J.; Buckner, F.; Van Voorhuis, W.; Mehlin, C.; Boni, E.; Feist, T.; Luft, J.; Gulde, S.; Lauricella, A.; Kaluzhniy, O.; Anderson, L.; Le Trong, I.; Holmes, M.A.; Earnest, T.; Soltis, M.; Hodgson, K.O.; Hol, W.G.; Merritt, E.A.
Crystal structures and proposed structural/functional classification of three protozoan proteins from the isochorismatase superfamily
Protein Sci.
14
2887-2894
2005
Leishmania donovani, Leishmania major, Trypanosoma cruzi
brenda
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)
brenda
Huang, X.; Shi, Z.; Wang, W.; Bai, J.; Chen, Z.; Xu, J.; Zhang, D.; Fu, S.
Identification and characterization of a novel protein ISOC2 that interacts with p16INK4a
Biochem. Biophys. Res. Commun.
361
287-293
2007
Homo sapiens, Mus musculus
brenda
Maruyama, C.; Hamano, Y.
The biological function of the bacterial isochorismatase-like hydrolase SttH
Biosci. Biotechnol. Biochem.
73
2494-2500
2009
Verticillium dahliae
brenda
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
brenda
Liu, S.; Zhang, C.; Li, N.; Niu, B.; Liu, M.; Liu, X.; Wie, T.; Zhu, D.; Huang, Y.; Xu, S.; Gu, L.
Structural insight into the ISC domain of VibB from Vibrio cholerae at atomic resolution: a snapshot just before the enzymatic reaction
Acta Crystallogr. Sect. D
68
1329-1338
2012
Vibrio cholerae (P0C6D3), Vibrio cholerae, Vibrio cholerae N16961 (P0C6D3)
brenda
Goral, A.M.; Tkaczuk, K.L.; Chruszcz, M.; Kagan, O.; Savchenko, A.; Minor, W.
Crystal structure of a putative isochorismatase hydrolase from Oleispira antarctica
J. Struct. Funct. Genomics
13
27-36
2012
Oleispira Antarctica (L7MTK1), Oleispira Antarctica
brenda
Wang, J.; Zhu, Y.; Zhao, G.; Zhu, J.; Wu, S.
Characterization of a recombinant (+)-gamma-lactamase from Microbacterium hydrocarbonoxydans which provides evidence that two enantiocomplementary gamma-lactamases are in the strain
Appl. Microbiol. Biotechnol.
99
3069-3080
2015
Microbacterium hydrocarbonoxydans (A0A077AY47), Microbacterium hydrocarbonoxydans
brenda
Du, J.; Deng, T.; Ma, Q.
Crystal structures of the isochorismatase domains from Vibrio anguillarum
Biochem. Biophys. Res. Commun.
490
827-833
2017
Vibrio anguillarum (Q5DK16), Vibrio anguillarum (Q6W4P9), Vibrio anguillarum, Vibrio anguillarum 775 (Q5DK16), Vibrio anguillarum 775 (Q6W4P9), Vibrio anguillarum ATCC 68554 (Q5DK16), Vibrio anguillarum ATCC 68554 (Q6W4P9)
brenda
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