4.1.3.1: isocitrate lyase
This is an abbreviated version!
For detailed information about isocitrate lyase, go to the full flat file.
Word Map on EC 4.1.3.1
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4.1.3.1
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interstrand
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malate
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lens
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eyes
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collamer
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postoperative
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intraocular
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crosslinks
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refract
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preoperative
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phakic
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acuity
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fanconi
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anemia
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posterior
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spherical
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uncorrected
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myopic
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vault
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fork
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diopter
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corneal
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astigmatism
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glyoxysomal
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fancd2
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pupil
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lymphocytopenia
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translesion
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logmar
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itaconate
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anaplerotic
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monoubiquitination
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psoralens
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monoadducts
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gaba-induced
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vision-threatening
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pupillary
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incisions
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hyperopic
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keratomileusis
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subcapsular
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lasik
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microbodies
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biomicroscopy
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drug development
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snellen
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medicine
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as-oct
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best-corrected
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sn-glycerol-3-phosphate
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spectacle
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molecular biology
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gelatinosa
- 4.1.3.1
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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
Reaction
Synonyms
AceA, acuD, citrate lyase, D-threo-isocitrate: glyoxylate lyase, EgGCE, FPICL1, ICL, ICL1, ICL2, isocitrase, isocitratase, isocitrate lyase, isocitrate lyase 1, isocitrate lyase 2, isocitric lyase, isocitritase, lyase, isocitrate, MtbIcl, PDP, petal death protein, SSO1333, threo-DS-Isocitrate glyoxylate-lyase
ECTree
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General Information
General Information on EC 4.1.3.1 - isocitrate lyase
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evolution
malfunction
metabolism
physiological function
additional information
the enzyme belongs to the isocitrate lyase ICL subfamily 3, one of two eubacterial groups, it has a substitution of M504I compared to the cold-adapted ICLs, rendering is less thermostable, phylogenetic analysis, overview
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
evolution
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the enzyme belongs to the isocitrate lyase ICL subfamily 3, one of two eubacterial groups, it has a substitution of M504I compared to the cold-adapted ICLs, rendering is less thermostable, phylogenetic analysis, overview
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a mutant deleted of the ICL gene (acuD) is fully virulent in a murine model
malfunction
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an ICL-deficient mutant is unable to utilize acetate, ethanol, citrate, glycerol, oleate, lactate, pyruvate, peptone, glutamate or alanine for growth, unlike the parental strain. ICL-deficient mutant is unable to utilize nonfermentable carbon sources and has reduced virulence in mice
malfunction
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an ICL1 mutant shows the same number of subarachnoidal yeast cells as the wild-type after 10 days in immunosuppressed rabbits. In an inhalation model of murine cryptococcosis, no differences in survival between an ICL1 mutant and the wild-type
malfunction
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deletion of the ICL1 gene causes a reduction in appressorium formation, conidiogenesis and cuticle penetration, and an overall decrease in damage to leaves of rice and barley
malfunction
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ICL (aceA) mutant displays reduced virulence on alfalfa seedlings and a reduction in histopathology in rat lungs
malfunction
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ICL1 mutant fails to grow on acetate or fatty acids, but is able to germinate and develop appressoria and is capable of degrading lipid bodies as well as the wild-type strain. Conidia from the ICL1-deficient mutant inoculated onto cucumber leaves and cotyledons form a reduced number of lesions on leaves, and especially on cotyledons, but nevertheless remain pathogenic. In invasive experiments such as the inoculation of conidia into wound sites, no defect is observed in the ICL1 mutant, while in penetration assays on cucumber cotyledons the mutant is unable to develop penetrating hyphae
malfunction
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inhibiting the activity of this enzyme during experimental chronic lung infection of rats forces the infection into an acute state, which can then be treated with antibiotics. If antibiotics are not provided in combination with isocitrate lyase inhibitors, the resulting infection overwhelms the host, resulting in death. ICL mutant is hypervirulent, it does not establish a chronic infection but establishes an acute infection. ICL mutants are significantly more cytotoxic than other strains. Complementation of the mutant strain restores the wild-type phenotype
malfunction
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mutations in the sole ICL gene (aceA) prevent growth on acetate but do not affect pathogenesis in a mouse model
malfunction
nutrient-starved bacilli lacking the glyoxylate shunt enzyme isocitrate lyase fail to reduce their intracellular ATP level and die, thus establishing a link between ATP control and intermediary metabolism. ICL loss-of-function mutant dies in the Loebel model. Viability is fully restored when the mutant strain is complemented with a wild-type copy of ICL
malfunction
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population of an ICL-deficient strain increases in macrophages after 12 h but then decline significantly
malfunction
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single ICL mutations have no dramatic effect on the growth. ICL mutant has a reduced ability to sustain the infection. An ICL/AceA double mutant is unable to grow on carbon source. The double mutant inoculated into mice is eliminated from lungs and spleen and is unable to induce splenomegaly or alterations in lungs
malfunction
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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
malfunction
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enzyme-deficient cells undergo a progressive depletion of TCA cycle intermediates and accumulation of propionyl-CoA when metabolizing fatty acid substrates, phenotype, overview. Enzyme-deficient cells are unable to metabolize both even- and odd-chain fatty acids because of the dead-end depletion of TCA cycle intermediates by a constitutively active, but broken, methylcitrate cycle. Addition of cobalamin is sufficient to selectively protect ICL-deficient cells from the bactericidal effects of acetate and propionate, and this attenuation is accompanied by a dose-dependent restoration of TCA cycle activity and propionyl-CoA levels
malfunction
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enzyme-deficient Mycobacterium tuberculosis strains are significantly more susceptible than wild type to the antibiotics isoniazid, rifampicin, and streptomycin
malfunction
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enzyme-deficient Mycobacterium tuberculosis strains are significantly more susceptible than wild type to the antibiotics isoniazid, rifampicin, and streptomycin
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malfunction
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nutrient-starved bacilli lacking the glyoxylate shunt enzyme isocitrate lyase fail to reduce their intracellular ATP level and die, thus establishing a link between ATP control and intermediary metabolism. ICL loss-of-function mutant dies in the Loebel model. Viability is fully restored when the mutant strain is complemented with a wild-type copy of ICL
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ICL overexpression and malonate addition has a significant impact on metabolism and on organic acid production profiles. Increased ICL expression does not result in an increased glyoxylate bypass flux, there is a global response with respect to gene expression, leading to an increased flux through the oxidative part of the TCA cycle. Instead of an increased production of succinate and malate, a major increase in fumarate production is observed. In the strain with overexpression of ICL the organic acid production shifts from fumarate towards malate production when malonate is added to the cultivation medium
metabolism
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participation of isoforms in metabolic regulation of the glyoxylate cycle, organic acid metabolism during photorespiration in leaves and acidosis in corn seeds
metabolism
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first enzyme of the glyoxylate shunt, which allows for the anaplerosis of citric acid cycle intermediates under nutrient limiting conditions
metabolism
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isocitrate lyase is a key enzyme in the glyoxylate cycle
metabolism
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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
metabolism
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the enzyme is an essential component of the glyoxylate cycle
metabolism
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the enzyme is required for the utilization of poly-beta-hydroxybutyrate for energy deriving during carbon starvation
metabolism
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the function of isoform ICL1 is related to the glyoxylate cycle while isoform ICL2 functions independently from the glyoxylate cycle and interconverts organic acids in the cytosol
metabolism
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ICL overexpression and malonate addition has a significant impact on metabolism and on organic acid production profiles. Increased ICL expression does not result in an increased glyoxylate bypass flux, there is a global response with respect to gene expression, leading to an increased flux through the oxidative part of the TCA cycle. Instead of an increased production of succinate and malate, a major increase in fumarate production is observed. In the strain with overexpression of ICL the organic acid production shifts from fumarate towards malate production when malonate is added to the cultivation medium
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metabolism
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isocitrate lyase is a key enzyme in the glyoxylate cycle
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ICL gene is required for non-growing survival in the Loebel model (nutrient deprivation in oxygen-rich medium)
physiological function
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ICL is essential for full virulence in the organism
physiological function
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ICL is essential for long-term survival and proliferation in macrophages
physiological function
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ICL is required for persistence during chronic infection, but not for acute lethal infection in mice
physiological function
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ICL1 contributes to virulence but is not essential for systemic infection. Role for the beta-oxidation pathway in virulence
physiological function
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important role for ICL in fungal virulence on plants. The ICL1 gene is expressed during its infection of Brassica napus cotyledons and inactivation of this locus causes low germination rates of pycnidiospores, reducing the pathogenicity of the fungus on cotyledons as well as limiting its hyphal growth on canola
physiological function
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isocitrate lyase is a persistence factor. ICL is not required for survival within unactivated murine macrophage cells
physiological function
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lack of correlation between ICL gene expression and biological function
physiological function
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the glyoxylate cycle mediated by ICL is unnecessary for virulence
physiological function
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two functional ICLs. ICL has a pivotal role in bacterial persistence in the host. ICL activity is essential for survival in the host. ICL and to a lesser extent AceA are required for the growth on propionate and on odd-chain fatty acids as a carbon source. The organism possesses dual ICL/MICL activity and can support growth on acetate and propionate
physiological function
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involved in a novel pathway for pyruvate dissimilation (GAS pathway: utilizes the glyoxylate shunt, anaplerotic fixation of carbon from CO2 and succinyl CoA synthetase for the generation of succinyl CoA)
physiological function
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involved in a novel pathway for pyruvate dissimilation (GAS pathway: utilizes the glyoxylate shunt, anaplerotic fixation of carbon from CO2 and succinyl CoA synthetase for the generation of succinyl CoA)
physiological function
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isocitrate lyase plays a key role for survival of Mycobacterium tuberculosis in the latent form during a chronic stage of infection. The enzyme is important during steady stage growth when it converts isocitrate to succinate and glyoxylate
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
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Mycobacterium tuberculosis isocitrate lyases are catalytically bifunctional isocitrate and methylisocitrate lyases required for growth on even and odd chain fatty acids
physiological function
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the enzyme catalyzes the first committed step in the glyoxylate cycle, it is essential in Mycobacterium tuberculosis for cell survival during chronic infection
physiological function
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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
physiological function
isocitrate lyase is a key enzyme of the glyoxylate shunt crucial for the survival of Mycobacterium tuberculosis in macrophages during persistent infection
physiological function
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the enzyme plays a key role during Puccinia striiformis f. sp. tritici germination
physiological function
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the enzyme plays a key role during Puccinia striiformis f. sp. tritici germination
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physiological function
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the enzyme catalyzes the first committed step in the glyoxylate cycle, it is essential in Mycobacterium tuberculosis for cell survival during chronic infection
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physiological function
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involved in a novel pathway for pyruvate dissimilation (GAS pathway: utilizes the glyoxylate shunt, anaplerotic fixation of carbon from CO2 and succinyl CoA synthetase for the generation of succinyl CoA)
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physiological function
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isocitrate lyase is a key enzyme of the glyoxylate shunt crucial for the survival of Mycobacterium tuberculosis in macrophages during persistent infection
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physiological function
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ICL gene is required for non-growing survival in the Loebel model (nutrient deprivation in oxygen-rich medium)
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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
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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