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Information on EC 4.1.3.1 - isocitrate lyase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9I0K4

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.1 isocitrate lyase
IUBMB Comments
The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate .
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9I0K4
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
icl, isocitrate lyase, citrate lyase, mtbicl, eggce, isocitritase, isocitratase, isocitric lyase, fpicl1, petal death protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isocitrase
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-
-
-
isocitratase
-
-
-
-
isocitrate lyase
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-
isocitric lyase
-
-
-
-
isocitritase
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-
-
-
lyase, isocitrate
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-
-
-
threo-DS-Isocitrate glyoxylate-lyase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
isocitrate glyoxylate-lyase (succinate-forming)
The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9045-78-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
isocitrate
succinate + glyoxylate
show the reaction diagram
isocitrate
succinate + glyoxylate
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
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-nitropropionic acid
-
-
Itaconic acid
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 0.94
isocitrate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.56 - 9.81
isocitrate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 22.3
isocitrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
wild-type enzyme and mutant E219A
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
high enzyme expression in cystic fibrosis samples
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the ICL family includes five subfamilies, and the 2-methylisocitrate lyase (MICL) family. The ICL from Pseudomonas aeruginosa (ICL-Pa) is identified in a different ICL node (subfamily 3) than other Pseudomonas ICL enzymes, phylogenetic analysis
physiological function
isocitrate lyase plays an important role in the ability of Pseudomonas aeruginosa to grow on fatty acids, acetate, acyclic terpenes, and amino acids
malfunction
metabolism
physiological function
-
the enzyme regulates the type III secretion system, T3SS, overview. Expression of the T3SS in oxygen-limited growth conditions is strongly dependent on the glyoxylate shunt enzyme, isocitrate lyase, which probably affects the RetS/LadS signalling pathways. ICL-dependent regulation of the T3SS does not alter the expression level of the master transcriptional regulator, ExsA, but affects expression of the T3 structural proteins, effectors and regulators, ExsC, ExsD and ExsE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E219A
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity compared to the wild-type enzyme
N214D
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows 10fold reduced activity compared to the wild-type enzyme
Q211H
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity and elevated temperature optimum compared to the wild-type enzyme
Q221K
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity and elevated temperature optimum compared to the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
purified enzyme, half-life of the wild-type enzyme is 40 min, half-lives of mutants E219A, Q211H, and Q221K are 25 min, 12 min, and 15 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ecombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Macro-Prep High Q Support column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
gene aceA, phylogenetic analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
lacZ fusion expressed Pseudomonas aeruginosa
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
regulated by carbon sources
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Diaz-Perez, A.L.; Roman-Doval, C.; Diaz-Perez, C.; Cervantes, C.; Sosa-Aguirre, C.R.; Lopez-Meza, J.E.; Campos-Garcia, J.
Identification of the aceA gene encoding isocitrate lyase required for the growth of Pseudomonas aeruginosa on acetate, acyclic terpenes and leucine
FEMS Microbiol. Lett.
269
309-316
2007
Pseudomonas aeruginosa (Q9I0K4), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Dunn, M.F.; Ramirez-Trujillo, J.A.; Hernandez-Lucas, I.
Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis
Microbiology
155
3166-3175
2009
Aspergillus fumigatus, Aspergillus nidulans, Candida albicans, Colletotrichum lagenaria, Rhodococcus equi, Cryptococcus neoformans, Escherichia coli, Leptosphaeria maculans, Pyricularia grisea, Mycobacterium tuberculosis, Mycobacterium avium, Yersinia pestis, Yersinia pseudotuberculosis, Pseudomonas aeruginosa, Sinorhizobium meliloti, Rhizobium tropici, Salmonella enterica subsp. enterica serovar Typhimurium, Yersinia enterocolitica, Paracoccidioides brasiliensis, Brucella suis, Talaromyces marneffei
Manually annotated by BRENDA team
Hagins, J.M.; Scoffield, J.A.; Suh, S.J.; Silo-Suh, L.
Influence of RpoN on isocitrate lyase activity in Pseudomonas aeruginosa
Microbiology
156
1201-1210
2010
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Chung, J.C.; Rzhepishevska, O.; Ramstedt, M.; Welch, M.
Type III secretion system expression in oxygen-limited Pseudomonas aeruginosa cultures is stimulated by isocitrate lyase activity
Open biology
3
120131
2013
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Campos-Garcia, J.; Diaz-Perez, C.; Diaz-Perez, A.L.
Residues Asn214, Gln211, Glu219 and Gln221 contained in the subfamily 3 catalytic signature of the isocitrate lyase from Pseudomonas aeruginosa are involved in its catalytic and thermal properties
World J. Microbiol. Biotechnol.
29
991-999
2013
Pseudomonas aeruginosa (Q9I0K4), Pseudomonas aeruginosa
Manually annotated by BRENDA team