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Information on EC 4.1.3.1 - isocitrate lyase and Organism(s) Pseudomonas aeruginosa
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IUBMB Comments
The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate .
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
- 4.1.3.1
-
interstrand
- malate
- lens
- eyes
-
collamer
-
postoperative
-
intraocular
-
crosslinks
-
refract
-
preoperative
-
phakic
-
acuity
-
fanconi
- anemia
-
posterior
-
spherical
-
uncorrected
-
myopic
-
vault
-
fork
-
diopter
- corneal
- astigmatism
- glyoxysomal
-
fancd2
- pupil
- lymphocytopenia
-
translesion
-
logmar
- itaconate
-
anaplerotic
-
monoubiquitination
- psoralens
-
monoadducts
-
gaba-induced
-
vision-threatening
-
pupillary
-
incisions
-
hyperopic
-
keratomileusis
-
subcapsular
-
lasik
- microbodies
-
biomicroscopy
- drug development
-
snellen
- medicine
-
as-oct
-
best-corrected
- sn-glycerol-3-phosphate
-
spectacle
- molecular biology
- gelatinosa
showSynonyms
icl, isocitrate lyase, citrate lyase, mtbicl, eggce, isocitritase, isocitratase, isocitric lyase, fpicl1, petal death protein, more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ICL
isocitrase
-
-
-
-
isocitratase
-
-
-
-
isocitric lyase
-
-
-
-
isocitritase
-
-
-
-
lyase, isocitrate
-
-
-
-
threo-DS-Isocitrate glyoxylate-lyase
-
-
-
-
ICL
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
glyoxylate cycle
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
9045-78-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
isocitrate
recombinant His-tagged mutant N214D, pH 7.8, 30°C
0.29
isocitrate
recombinant His-tagged mutant Q211H, pH 7.8, 30°C
0.44
isocitrate
recombinant His-tagged wild-type enzyme, pH 7.8, 30°C
0.47
isocitrate
recombinant His-tagged mutant Q221K, pH 7.8, 30°C
0.94
isocitrate
recombinant His-tagged mutant E219A, pH 7.8, 30°C
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzyme's overview
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzyme's overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.56
isocitrate
recombinant His-tagged mutant N214D, pH 7.8, 30°C
3.25
isocitrate
recombinant His-tagged mutant Q221K, pH 7.8, 30°C
3.46
isocitrate
recombinant His-tagged mutant Q211H, pH 7.8, 30°C
4.63
isocitrate
recombinant His-tagged mutant E219A, pH 7.8, 30°C
9.81
isocitrate
recombinant His-tagged wild-type enzyme, pH 7.8, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.8
isocitrate
recombinant His-tagged mutant N214D, pH 7.8, 30°C
4.9
isocitrate
recombinant His-tagged mutant E219A, pH 7.8, 30°C
6.9
isocitrate
recombinant His-tagged mutant Q221K, pH 7.8, 30°C
11.9
isocitrate
recombinant His-tagged mutant Q211H, pH 7.8, 30°C
22.3
isocitrate
recombinant His-tagged wild-type enzyme, pH 7.8, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
high enzyme expression in cystic fibrosis samples
Highest Expressing Human Cell Lines
Cell Line LinksGENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
malfunction
metabolism
physiological function
additional information
malfunction
-
ICL (aceA) mutant displays reduced virulence on alfalfa seedlings and a reduction in histopathology in rat lungs
malfunction
-
an aceA mutant displays enhanced biofilm formation during anaerobic growth. Expression of PcrV, of PopN (a regulator of the T3SS translocation process), ExoS (a T3 effector protein), and ExsD (a T3S regulator) is greatly reduced in the aceA mutant. Expression of aceA from a plasmid in trans can restore PcrV expression and ICL activity in the aceA mutant
metabolism
-
the enzyme is important in the glyoxylate shunt pathway, which is strongly induced in Pseudomonas aeruginosa during anaerobic growth and during growth on C2-sources, such as acetate or fatty acids, as the sole carbon source, overview
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
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
conserved residues in the subfamily 3 signature of ICL-Pa play important roles in catalysis and thermostability and are likely associated with the catalytic loop structural conformation. Three-dimensional structural homology modeling of ICL-Pa wild-type and mutants, structure comparisons, active site modeling, overview. Residue N214 plays an essential role in ICL-Pa catalytic activity
additional information
-
conserved residues in the subfamily 3 signature of ICL-Pa play important roles in catalysis and thermostability and are likely associated with the catalytic loop structural conformation. Three-dimensional structural homology modeling of ICL-Pa wild-type and mutants, structure comparisons, active site modeling, overview. Residue N214 plays an essential role in ICL-Pa catalytic activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
additional information
transposition mutant PAO1SM::Himar1GmR is unable to grow on citronellol, n-octanol, leucine and acetate, and shows totally abolished ICL activity
additional information
-
transposition mutant PAO1SM::Himar1GmR is unable to grow on citronellol, n-octanol, leucine and acetate, and shows totally abolished ICL activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aceA, phylogenetic analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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 nidulans, Plenodomus lingam, Pyricularia grisea, Colletotrichum lagenaria, Candida albicans, Paracoccidioides brasiliensis, Aspergillus fumigatus, Cryptococcus neoformans, Mycobacterium avium, Salmonella enterica subsp. enterica serovar Typhimurium, Brucella suis, Yersinia enterocolitica, Yersinia pseudotuberculosis, Yersinia pestis, Prescottella equi, Talaromyces marneffei, Sinorhizobium meliloti, Rhizobium tropici, Pseudomonas aeruginosa, Escherichia coli, Mycobacterium tuberculosis
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
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
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
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