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Literature summary for 4.1.3.1 extracted from

  • Dunn, M.F.; Ramirez-Trujillo, J.A.; Hernandez-Lucas, I.
    Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis (2009), Microbiology, 155, 3166-3175.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information high enzymic activity of ICL in strains isolated from diabetic patients suffering from vulvovaginal candidiasis. Specific activation of ICL1 when the pathogen is exposed to neutrophils or macrophages Candida albicans
additional information ICL activity increases in pellicles in synthetic media as a consequence of fatty acid degradation as well as under microaerophilic growth conditions Mycobacterium tuberculosis

Application

Application Comment Organism
additional information constitutive enzymic activity can be used to identify Yersinia pestis in humans, animals, water, soil and food Yersinia pestis

Inhibitors

Inhibitors Comment Organism Structure
additional information natural glyoxylate cycle inhibitors such 5-hydroxyindole-type alkaloids are potent inhibitors Candida albicans
additional information extracts of Illicium verum and Zingiber officinale inhibit ICL Mycobacterium tuberculosis
additional information halisulfates from the tropical sponge Hippospongia sp. are able to inhibit ICL activity, appressorium formation and C2 utilization Pyricularia grisea

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Colletotrichum lagenaria 5777
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
-
Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus
-
-
-
Aspergillus nidulans
-
-
-
Brucella suis
-
-
-
Candida albicans
-
-
-
Colletotrichum lagenaria
-
-
-
Cryptococcus neoformans
-
-
-
Escherichia coli
-
-
-
Leptosphaeria maculans
-
-
-
Mycobacterium avium
-
-
-
Mycobacterium tuberculosis
-
-
-
Paracoccidioides brasiliensis
-
-
-
Pseudomonas aeruginosa
-
-
-
Pyricularia grisea
-
-
-
Rhizobium tropici
-
-
-
Rhodococcus equi
-
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
Sinorhizobium meliloti
-
-
-
Talaromyces marneffei
-
-
-
Yersinia enterocolitica
-
-
-
Yersinia pestis
-
-
-
Yersinia pseudotuberculosis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
appressorium
-
Pyricularia grisea
-
appressorium
-
Colletotrichum lagenaria
-
conidium
-
Pyricularia grisea
-
conidium
-
Colletotrichum lagenaria
-
conidium
-
Aspergillus fumigatus
-
hypha
-
Pyricularia grisea
-
hypha
-
Colletotrichum lagenaria
-
hypha
-
Aspergillus fumigatus
-
mycelium
-
Pyricularia grisea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate
-
Pseudomonas aeruginosa succinate + glyoxylate
-
?
additional information Lys-193, Cys-195, His-197 and His-356 are catalytic, active-site residues, while His-184 is involved in the assembly of the tetrameric enzyme Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
tetramer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
AceA
-
Pseudomonas aeruginosa
AceA
-
Mycobacterium avium
AceA
-
Mycobacterium tuberculosis
AceA
-
Yersinia pestis
acuD
-
Aspergillus fumigatus
acuD
-
Paracoccidioides brasiliensis
ICL
-
Salmonella enterica subsp. enterica serovar Typhimurium
ICL
-
Sinorhizobium meliloti
ICL
-
Escherichia coli
ICL
-
Aspergillus nidulans
ICL
-
Pseudomonas aeruginosa
ICL
-
Mycobacterium avium
ICL
-
Yersinia pseudotuberculosis
ICL
-
Yersinia pestis
ICL
-
Rhodococcus equi
ICL
-
Aspergillus fumigatus
ICL
-
Yersinia enterocolitica
ICL
-
Rhizobium tropici
ICL
-
Paracoccidioides brasiliensis
ICL
-
Brucella suis
ICL
-
Talaromyces marneffei
ICL1
-
Mycobacterium tuberculosis
ICL1
-
Candida albicans
ICL1
-
Cryptococcus neoformans
ICL1
-
Pyricularia grisea
ICL1
-
Colletotrichum lagenaria
ICL1
-
Leptosphaeria maculans
ICL2
-
Mycobacterium tuberculosis
isocitrate lyase
-
Salmonella enterica subsp. enterica serovar Typhimurium
isocitrate lyase
-
Sinorhizobium meliloti
isocitrate lyase
-
Escherichia coli
isocitrate lyase
-
Aspergillus nidulans
isocitrate lyase
-
Pseudomonas aeruginosa
isocitrate lyase
-
Mycobacterium avium
isocitrate lyase
-
Mycobacterium tuberculosis
isocitrate lyase
-
Candida albicans
isocitrate lyase
-
Yersinia pseudotuberculosis
isocitrate lyase
-
Yersinia pestis
isocitrate lyase
-
Cryptococcus neoformans
isocitrate lyase
-
Rhodococcus equi
isocitrate lyase
-
Pyricularia grisea
isocitrate lyase
-
Colletotrichum lagenaria
isocitrate lyase
-
Aspergillus fumigatus
isocitrate lyase
-
Leptosphaeria maculans
isocitrate lyase
-
Yersinia enterocolitica
isocitrate lyase
-
Rhizobium tropici
isocitrate lyase
-
Paracoccidioides brasiliensis
isocitrate lyase
-
Brucella suis
isocitrate lyase
-
Talaromyces marneffei

Expression

Organism Comment Expression
Candida albicans in bloodstream infection, ICL is downregulated in the initial stages of infection (10 min) down
Pyricularia grisea during infection, significant ICL gene expression in conidia, appressoria, mycelia and hyphae up
Talaromyces marneffei expressed in macrophages up
Cryptococcus neoformans ICL in a rabbit meningitis model is upregulated after 7 days in the subarachnoid space up
Mycobacterium tuberculosis increased aceA (icl) mRNA expression in response to human macrophages. ICL mRNA levels markedly increase in lungs of mice and in human lung granulomas, as well as in the lymphocyte region of necrotic granulomas up
Yersinia pseudotuberculosis induced during growth on acetate but not on xylose up
Yersinia enterocolitica induced during growth on acetate but not on xylose up
Candida albicans is induced in Candida albicans exposed to human neutrophils. In bloodstream infection, ICL is upregulated beginning about 20 min after infection and reaches a 20fold increase after 60 min. ICL expression is detected during growth on Casamino acids, glutamate or peptone, and under starvation conditions up
Paracoccidioides brasiliensis transcript level of the ICL gene increases following phagocytosis by murine macrophages. After macrophage internalization of conidia the ICL-encoding gene (acuD) is highly expressed up

General Information

General Information Comment Organism
malfunction a mutant deleted of the ICL gene (acuD) is fully virulent in a murine model Aspergillus fumigatus
malfunction 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 Candida albicans
malfunction 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 Cryptococcus neoformans
malfunction 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 Pyricularia grisea
malfunction ICL (aceA) mutant displays reduced virulence on alfalfa seedlings and a reduction in histopathology in rat lungs Pseudomonas aeruginosa
malfunction 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 Colletotrichum lagenaria
malfunction mutations in the sole ICL gene (aceA) prevent growth on acetate but do not affect pathogenesis in a mouse model Yersinia pestis
malfunction population of an ICL-deficient strain increases in macrophages after 12 h but then decline significantly Rhodococcus equi
malfunction 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 Mycobacterium tuberculosis
physiological function ICL is essential for full virulence in the organism Pyricularia grisea
physiological function ICL is essential for long-term survival and proliferation in macrophages Rhodococcus equi
physiological function ICL is required for persistence during chronic infection, but not for acute lethal infection in mice Salmonella enterica subsp. enterica serovar Typhimurium
physiological function ICL1 contributes to virulence but is not essential for systemic infection. Role for the beta-oxidation pathway in virulence Candida albicans
physiological function 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 Leptosphaeria maculans
physiological function lack of correlation between ICL gene expression and biological function Cryptococcus neoformans
physiological function the glyoxylate cycle mediated by ICL is unnecessary for virulence Brucella suis
physiological function the organism constitutively produces ICL Yersinia pestis
physiological function two functional ICLs Mycobacterium avium
physiological function 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 Mycobacterium tuberculosis