Information on EC 4.1.3.1 - isocitrate lyase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.1.3.1
-
RECOMMENDED NAME
GeneOntology No.
isocitrate lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isocitrate = succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate = succinate + glyoxylate
show the reaction diagram
kinetic mechanism is the same in microgravity and in standard g controls
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
condensation
-
-
-
-
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
-
glyoxylate cycle
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
TCA cycle IV (2-oxoglutarate decarboxylase)
-
TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
-
SYSTEMATIC NAME
IUBMB Comments
isocitrate glyoxylate-lyase (succinate-forming)
The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate [3].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acuD
Penicillium marneffei
-
citrate lyase encoding gene
acuD
Penicillium marneffei CBS 119456
-
citrate lyase encoding gene
-
citrate lyase
-
-
citrate lyase
-
-
citrate lyase
Debaryomyces hansenii Y7426
-
-
-
citrate lyase
Penicillium marneffei
-
-
citrate lyase
Penicillium marneffei CBS 119456
-
-
-
EgGCE
Q8LPA6
bifunctional enzyme: isocitrate lyase and malate synthase
EgGCE
Euglena gracilis SM-ZK
Q8LPA6
bifunctional enzyme: isocitrate lyase and malate synthase
-
FPICL1
Q58A52
-
FPICL1
Fomitopsis palustris TYP-6137
Q58A52
-
-
ICL
-
-
-
-
ICL
Aspergillus fumigatus ATCC46645
-
-
-
ICL
Aspergillus niger N402
-
-
-
ICL
Colwellia psychrerythraea NRC 1004
A8C5K8
-
-
ICL
Debaryomyces hansenii Y7426
-
-
-
ICL
Escherichia coli K-12 W3110
-
-
-
ICL
Q8LPA6
-
ICL
Euglena gracilis SM-ZK
Q8LPA6
-
-
ICL
Fomitopsis palustris TYP-6137
Q58A52
-
-
ICL
-
key enzyme in the glyoxylate cycle
ICL
Magnaporthe grisea Guy 11
-
key enzyme in the glyoxylate cycle
-
ICL
Mycobacterium smegmatis 1-2c
-
-
-
ICL
-
ICL1 with isocitrate and 2-methylisocitrate lyase activity
ICL
Pseudomonas fluorescens 13525
-
-
-
ICL
Sinorhizobium meliloti Rm5000
-
-
-
ICL
-
-
ICL1
-
isoenzyme, has both isocitrate lyase and 2-methylisocitrate lyase activity
ICL2
-
isoenzyme, has no 2-methylisocitrate lyase activity
isocitrase
-
-
-
-
isocitratase
-
-
-
-
isocitrate lyase
-
-
isocitrate lyase
-
-
isocitrate lyase
Aspergillus niger N402
-
-
-
isocitrate lyase
-
-
isocitrate lyase
-
-
isocitrate lyase
Candida albicans ATCC 10231
-
;
-
isocitrate lyase
-
-
isocitrate lyase
Q8LPA6
activity of a bifunctional protein named glyoxylate cycle enzyme (malate synthase and isocitrate lyase activity)
isocitrate lyase
-
-
isocitrate lyase
Mycobacterium smegmatis 1-2c
-
-
-
isocitrate lyase
P0A5H3
-
isocitrate lyase
-
-
isocitrate lyase
Q5YLB6
-
isocitrate lyase
Penicillium marneffei
-
-
isocitrate lyase
-
-
isocitrate lyase
-
-
isocitrate lyase
-
-
isocitrate lyase 1
-
relative electrophoretic mobility Rf 0.28
isocitrate lyase 2
-
relative electrophoretic mobility Rf 0.44
isocitrate lyase 2
-
-
isocitric lyase
-
-
-
-
isocitritase
-
-
-
-
lyase, isocitrate
-
-
-
-
petal death protein
Q05957
-
SSO1333
Q97YI8
gene name
threo-DS-Isocitrate glyoxylate-lyase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9045-78-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC46645
-
-
Manually annotated by BRENDA team
Aspergillus fumigatus ATCC46645
strain ATCC46645
-
-
Manually annotated by BRENDA team
strain N402
-
-
Manually annotated by BRENDA team
Aspergillus niger N402
strain N402
-
-
Manually annotated by BRENDA team
thermophilic
-
-
Manually annotated by BRENDA team
strains 1026b and DD503
-
-
Manually annotated by BRENDA team
ATCC 10231
-
-
Manually annotated by BRENDA team
Candida albicans ATCC 10231
-
-
-
Manually annotated by BRENDA team
Candida brassicae
-
-
-
Manually annotated by BRENDA team
strain NRC 1004
UniProt
Manually annotated by BRENDA team
Colwellia psychrerythraea NRC 1004
strain NRC 1004
UniProt
Manually annotated by BRENDA team
Debaryomyces hansenii Y7426
Y7426
-
-
Manually annotated by BRENDA team
strain K-12 W3110
-
-
Manually annotated by BRENDA team
strains BW2952, BW3767, BW3709, BW3480, BW3708, BW3782, MG1655
-
-
Manually annotated by BRENDA team
Escherichia coli K-12 W3110
strain K-12 W3110
-
-
Manually annotated by BRENDA team
-
Q8LPA6
Swissprot
Manually annotated by BRENDA team
SM-ZK
Q8LPA6
Swissprot
Manually annotated by BRENDA team
Euglena gracilis SM-ZK
SM-ZK
Q8LPA6
Swissprot
Manually annotated by BRENDA team
strain TYP-6137, formerly named Tyromyces palustris
EMBL
Manually annotated by BRENDA team
Fomitopsis palustris TYP-6137
strain TYP-6137, formerly named Tyromyces palustris
EMBL
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
Klicl1 deletion mutant
-
-
Manually annotated by BRENDA team
Lupinus sp.
-
-
-
Manually annotated by BRENDA team
strain Guy 11
-
-
Manually annotated by BRENDA team
Magnaporthe grisea Guy 11
strain Guy 11
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis 1-2c
1-2c
-
-
Manually annotated by BRENDA team
H37Rv, ATCC 25618, without functional ICL2 gene (aceA) because gene is split into two ORFs (aceAa and aceAb)
-
-
Manually annotated by BRENDA team
ssp. indica cv Guangluai
-
-
Manually annotated by BRENDA team
Penicillium marneffei
-
-
-
Manually annotated by BRENDA team
Penicillium marneffei
CBS 119456
-
-
Manually annotated by BRENDA team
Penicillium marneffei CBS 119456
CBS 119456
-
-
Manually annotated by BRENDA team
strain PAO1
UniProt
Manually annotated by BRENDA team
strain PAO1
-
-
Manually annotated by BRENDA team
strain 13525
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens 13525
strain 13525
-
-
Manually annotated by BRENDA team
wild-type: KT2442, mutant: KT217, poly(3-hydroxyalkanoate)-overproducing mutant in which aceA gene is knocked out
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
strain Rm5000
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti Rm5000
strain Rm5000
-
-
Manually annotated by BRENDA team
Streptomyces clavuligerus NRRL 3585
NRRL 3585
SwissProt
Manually annotated by BRENDA team
strain DSM 639
-
-
Manually annotated by BRENDA team
isolate ATCC 95640
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
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
-
a mutant deleted of the ICL gene (acuD) is fully virulent in a murine model
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
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
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
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
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
malfunction
-
ICL (aceA) mutant displays reduced virulence on alfalfa seedlings and a reduction in histopathology in rat lungs
malfunction
-
population of an ICL-deficient strain increases in macrophages after 12 h but then decline significantly
malfunction
-
mutations in the sole ICL gene (aceA) prevent growth on acetate but do not affect pathogenesis in a mouse model
malfunction
P0A5H3
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
metabolism
-
participation of isoforms in metabolic regulation of the glyoxylate cycle, organic acid metabolism during photorespiration in leaves and acidosis in corn seeds
metabolism
-
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
-, Q5YLB6
glyoxylate cycle key enzyme
metabolism
-
high activity in isolates from cystic fibrosis patients
metabolism
Aspergillus niger N402
-
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
-
physiological function
-
isocitrate lyase is a persistence factor. ICL is not required for survival within unactivated murine macrophage cells
physiological function
-
the glyoxylate cycle mediated by ICL is unnecessary for virulence
physiological function
-
ICL1 contributes to virulence but is not essential for systemic infection. Role for the beta-oxidation pathway in virulence
physiological function
-
lack of correlation between ICL gene expression and biological function
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
physiological function
-
ICL is essential for full virulence in the organism
physiological function
-
two functional ICLs
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
physiological function
-
ICL is essential for long-term survival and proliferation in macrophages
physiological function
-
ICL is required for persistence during chronic infection, but not for acute lethal infection in mice
physiological function
-
the organism constitutively produces ICL
physiological function
P0A5H3
ICL gene is required for non-growing survival in the Loebel model (nutrient deprivation in oxygen-rich medium)
physiological function
-
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)
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate
succinate + glyoxylate
show the reaction diagram
-
reversible aldol cleavage
glyoxylate shunt
-
r
(2R)-2-ethyl malate
acetate + 2-oxobutanoate
show the reaction diagram
-, Q05957
-
-
-
?
(2R)-2-methyl malate
pyruvate + acetate
show the reaction diagram
-, Q05957
-
-
-
?
(2R)-ethyl-(3S)-methyl malate
2-oxobutanoate + propanoate
show the reaction diagram
-, Q05957
-
-
-
?
(2R)-isobutyl-(3S)-methyl malate
4-methyl-2-oxopentanoate + propanoate
show the reaction diagram
-, Q05957
-
-
-
?
(2R)-propyl-(3S)-methyl malate
4-methyl-2-oxopentanoate + propanoate
show the reaction diagram
-, Q05957
-
-
-
?
(2R,3R:2S,3S)-2-methyl-isocitrate
succinate + pyruvate
show the reaction diagram
-, Q05957
-
-
-
?
(2R,3S)-2,3-dimethyl malate
pyruvate + propanoate
show the reaction diagram
-, Q05957
-
-
-
?
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
-
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-, Q05957
-
-
-
?
(2R,3S:2S,3R)-2-methyl-isocitrate
succinate + pyruvate
show the reaction diagram
-, P0A5H3
-
-
-
?
(2R,3S:2S,3R)-2-methyl-isocitrate
succinate + pyruvate
show the reaction diagram
-, Q05957
-
-
-
?
(2S)-2-methyl malate
pyruvate + acetate
show the reaction diagram
-, Q05957
kcat below 1x10-5
-
-
?
(R)-malate
glyoxylate + acetate
show the reaction diagram
-, Q05957
kcat below 1x10-5
-
-
?
(S)-malate
glyoxylate + acetate
show the reaction diagram
-, Q05957
kcat below 1x10-5
-
-
?
acetyl-CoA + glyoxylate + H2O
malate + CoA
show the reaction diagram
Euglena gracilis, Euglena gracilis SM-ZK
Q8LPA6
-
-
-
?
D,L-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
DL-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Lupinus sp.
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
Lupinus sp.
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
Lupinus sp.
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
P0A5H3
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-, P17069
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
Candida brassicae
-
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Q8RPZ0, -
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Q8LPA6
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Q8LPA6
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Q5XTP4, -
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-, Q58A52
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
A8C5K8
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-, Q9I0K4
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Q97YI8
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
Mg-isocitrate is the true substrate
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
first enzyme of glyoxylate shunt
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
first step in glyoxylate-bypass pathway
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
rate-limiting enzyme of the citric acid cycle
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
regulatory enzyme playing a crucial role in fungal growth
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
30C, pH 7.5, HEPES containing phenylhydrazine HCl
absorbance of glyoxylate phenylhydrazone at 334 nm
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
pH 7.3, cell-free extracts, in presence of MgCl2 and 2,4-dinitrophenylhydrazine
analysis based on absorbance at 450 nm
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
ICL1, ICL2 and ICL
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Colwellia psychrerythraea NRC 1004
A8C5K8
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Debaryomyces hansenii Y7426
-
pH 7.3, cell-free extracts, in presence of MgCl2 and 2,4-dinitrophenylhydrazine
analysis based on absorbance at 450 nm
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Escherichia coli K-12 W3110
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Fomitopsis palustris TYP-6137
Q58A52
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Streptomyces clavuligerus NRRL 3585
Q8RPZ0
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Aspergillus fumigatus ATCC46645
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Aspergillus niger N402
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Sinorhizobium meliloti Rm5000
-
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Euglena gracilis SM-ZK
Q8LPA6
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Magnaporthe grisea Guy 11
-
-
-
-
?
isocitrate
?
show the reaction diagram
-
-
-
-
-
isocitrate
?
show the reaction diagram
-
assimilation of one-carbon compounds in the icl+ serine pathway
-
-
-
isocitrate
?
show the reaction diagram
Lupinus sp.
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-, P17069
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
Candida brassicae
-
glyoxylate cycle
-
-
-
isocitrate
glyoxylate + succinate
show the reaction diagram
P0A9G6
-
-
-
?
isocitrate
glyoxylate + succinate
show the reaction diagram
-
-
-
-
?
isocitrate
glyoxylate + succinate
show the reaction diagram
-
-
-
-
?
isocitrate
glyoxylate + succinate
show the reaction diagram
-, Q5YLB6
-
-
-
?
isocitrate
glyoxylate + succinate
show the reaction diagram
-
blue-native SDS-PAGE
coupling glyoxylate formation to lactate dehydrogenase type II activity (10 U) in presence of NAD
-
?
oxalacetate
oxalate + acetate
show the reaction diagram
-, Q05957
-
-
-
?
isocitrate + phenylhydrazine
? + glyoxylate phenylhydrazone
show the reaction diagram
-
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate
succinate + glyoxylate
show the reaction diagram
-
reversible aldol cleavage
glyoxylate shunt
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
r
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
Q8RPZ0, -
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
first enzyme of glyoxylate shunt
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
first step in glyoxylate-bypass pathway
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
rate-limiting enzyme of the citric acid cycle
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
-
regulatory enzyme playing a crucial role in fungal growth
-
?
isocitrate
?
show the reaction diagram
-
-
-
-
-
isocitrate
?
show the reaction diagram
-
assimilation of one-carbon compounds in the icl+ serine pathway
-
-
-
isocitrate
?
show the reaction diagram
Lupinus sp.
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-, P17069
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
-
isocitrate
?
show the reaction diagram
Candida brassicae
-
glyoxylate cycle
-
-
-
isocitrate
succinate + glyoxylate
show the reaction diagram
Streptomyces clavuligerus NRRL 3585
Q8RPZ0
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
Ba2+ less effective activator than Mg2+
Ba2+
-
partial reactivation after thermal inactivation
Ba2+
-
no activation
Ba2+
-
no activation
Ba2+
Candida brassicae
-
Ba2+ less effective activator than Mg2+
Ba2+
-
Ba2+ less effective activator than Mg2+
Cd2+
-
5 mM, 90% inhibition of Mg2+-activated enzyme, interaction with catalytic domain induces partial unfolding (revealed by thermal denaturation, far-UV circular dichroism, fluorescence spectra, and glutaraldehyde crosslinking)
Co2+
-
Co2+ 17% as effective as Mg2+; no activity in absence of exogenous cation
Co2+
-
Co2+ 29% as effective as Mg2+; no activity in absence of exogenous cation
Co2+
-
Co2+ 12% as effective as Mg2+; no activity in absence of exogenous cation
Co2+
-
Co2+ 18% as effective as Mg2+; no activity in absence of exogenous cation
Co2+
-
can partly replace Mg2+
Co2+
-
can replace Mg2+
Co2+
Q05957
activating
Fe2+
-
no activity in absence of exogenous cation, Fe2+ 7% as effective as Mg2+
Fe2+
Q05957
activating
Mg2+
-
no activity in absence of exogenous cation, Mg2+ most effective
Mg2+
-
essential for activity, optimal concentration 3 mM
Mg2+
-
reactivation after thermal inactivation, Mg2+-isocitrate complex is true substrate, 2 Mg2+-binding sites: catalytic and activator site
Mg2+
-
increase of activity
Mg2+
Lupinus sp.
-
increase of activity
Mg2+
Lupinus sp.
-
-
Mg2+
-
-
Mg2+
-
absolute requirement
Mg2+
-
increase of activity
Mg2+
-
increase of activity
Mg2+
-
maximal activity at 5-6 mM
Mg2+
-
increase of activity
Mg2+
-
increase of activity; maximal activity at 3.7 mM
Mg2+
Lupinus sp.
-
increase of activity; maximal activity at 5 mM
Mg2+
-
maximal activity at 6 mM
Mg2+
-
increase of activity
Mg2+
-
increase of activity
Mg2+
-
increase of activity
Mg2+
-
required for full activity, optimal concentration 5 mM
Mg2+
-
activity of demetallized enzyme: 0.5%
Mg2+
-
increase of activity
Mg2+
Candida brassicae
-
maximal activity at 8 mM
Mg2+
-
non-essential activator
Mg2+
-
requirement, optimal concentration: 2 mM, Km value: 0.092 at pH 7
Mg2+
-
10 mM, dependent
Mg2+
-
Icl enzyme: most effective cation, optimal concentration: 5 mM
Mg2+
-
dependent
Mg2+
-
activity dependent on Mg2+
Mg2+
Q05957
activating oxalacetate hydrolase activity
Mg2+
-
dependent on Mg2+
Mg2+
P0A5H3
required
Mg2+
-
5 mM, essential for catalytic activity, 100% activity, binds and stabilizes non-catalytic alpha/beta barrel core without structural alterations (revealed by thermal, urea and GdnHCL denaturation and far-UV CD)
Mg2+
-
ICL1, dependent on
Mn2+
-
Mn2+ 54% as effective as Mg2+; no activity in absence of exogenous cation
Mn2+
-
Mn2+ less effective activator than Mg2+
Mn2+
-
partial reactivation after thermal inactivation
Mn2+
-
Mn2+ 24% as effective as Mg2+; no activity in absence of exogenous cation
Mn2+
-
Mn2+ 14% as effective as Mg2+; no activity in absence of exogenous cation
Mn2+
-
Mn2+ 31% as effective as Mg2+; no activity in absence of exogenous cation
Mn2+
-
Mn2+ 30% as effective as Mg2+
Mn2+
-
Mn2+ 27% as effective as Mg2+; no activity in absence of exogenous cation
Mn2+
Candida brassicae
-
Mn2+ less effective activator than Mg2+
Mn2+
-
Mn2+ less effective activator than Mg2+
Mn2+
-
can replace Mg2+ with 24% of the activity of Mg2+
Mn2+
-
can partly replace Mg2+
Mn2+
-
Icl enzyme: can replace Mg2+, yielding 39% of the activity obtained with Mg2+
Mn2+
Q05957
activating oxalacetate hydrolase activity
Mn2+
-
5 mM, 45% activity, binds and stabilizes non-catalytic alpha/beta barrel core without structural alterations (revealed by thermal, urea and GdnHCL denaturation and far-UV CD)
Ni2+
-
no activity in absence of exogenous cation, Ni2+ 7% as effective as Mg2+
Ni2+
-
less efficient activator than Mg2+
Ni2+
-
can partly replace Mg2+
Sr2+
-
no activity in absence of exogenous cation, Sr2+ 3% as effective as Mg2+
Sr2+
-
no activation
Sr2+
-
no activation
Zn2+
-
5 mM, 90% inhibition of Mg2+-activated enzyme, interaction with catalytic domain induces partial unfolding (revealed by thermal denaturation, far-UV circular dichroism, ANS fluorescence spectra, and glutaraldehyde crosslinking)
Mn2+
-
ICL2 and ICL, dependent on
additional information
-
no significant change in enzyme activity after incubation with Co2+, Pb2+, Fe2+, Cu2+, Cd2+, Na+, K+, Cl-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R,2R,6E)-8-(2,5-dihydroxyphenyl)-2-hydroxy-6-methyl-1-[[(1S,4aS,8aS)-2,5,5,8a-tetramethyl-1,4,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]methyl]oct-6-en-1-yl hydrogen sulfate
-
-
(1S,4bS,10aR,12aS)-10a-[(acetyloxy)methyl]-1-formyl-4b,7,7,12a-tetramethyl-1,4,4a,4b,5,6,6a,7,8,9,10,10a,10b,11,12,12a-hexadecahydrochrysene-2-carboxylic acid
-
scarlarane sesterterpene, isolated from Smenospongia sp.
(2-bromo-4,5-dihydroxybenzyl)(2,3-dibromo-4,5-dihydroxybenzyl) ether
-
-
-
(2-bromo-4,5-dihydroxyphenyl)(3,4-dihydroxyphenyl) ether
-
-
-
(2E,6E)-9-[(2R)-6-hydroxy-2,8-dimethyl-3,4-dihydro-2H-chromen-2-yl]-2,6-dimethylnona-2,6-dienal
-
-
(2E,7E)-10-[(2R)-6-hydroxy-2,8-dimethyl-3,4-dihydro-2H-chromen-2-yl]-3,7-dimethyl-2-(2-methylprop-1-en-1-yl)deca-2,7-dienal
-
-
(2R)-2-[(3E,7E)-9-(hydroxymethyl)-4,8,11-trimethyldodeca-3,7,10-trien-1-yl]-2,8-dimethyl-3,4-dihydro-2H-chromen-6-ol
-
-
(3-bromo-4,5-dihydroxyphenyl)(2,3-dibromo-4,5-dihydroxyphenyl)methanone
-
-
-
(4R,5R)-4-[(2E)-5-[(2R)-6-hydroxy-2,8-dimethyl-3,4-dihydro-2H-chromen-2-yl]-2-methylpent-2-en-1-yl]-2-methyl-5-(2-methylprop-1-en-1-yl)cyclopent-2-en-1-one
-
-
(4S,5bR,11aS,13aS,13bR)-4-hydroxy-5b,8,8,11a,13a-pentamethyl-1,4,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1-yl acetate
-
scarlarane sesterterpene, isolated from Smenospongia sp.
(4S,5bS,11aR,13aS,13bR)-11a-formyl-4-hydroxy-5b,8,8,13a-tetramethyl-1,4,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1-yl acetate
-
scarlarane sesterterpene, isolated from Smenospongia sp.
(4S,5bS,11aR,13aS,13bR)-11a-[(acetyloxy)methyl]-5b,8,8,13a-tetramethyl-1,4,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1,4-diyl diacetate
-
scarlarane sesterterpene, isolated from Smenospongia sp.
(5bS,11aR,13aS,13bR)-11a-(hydroxymethyl)-5b,8,8,13a-tetramethyl-3-oxo-1,3,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1-yl acetate
-
scarlarane sesterterpene, isolated from Smenospongia sp.
(5E)-5-[(2R,6E,10E)-13-furan-3-yl-2,6,10-trimethyltrideca-6,10-dien-1-ylidene]-4-hydroxy-3-methylfuran-2(5H)-one
-
linear furanosesterterpene, isolated from Smenospongia sp.
(5Z)-5-[(2R,5Z,9Z)-13-furan-3-yl-2,6,10-trimethyltrideca-5,9-dien-1-ylidene]-4-hydroxy-3-methylfuran-2(5H)-one
-
linear furanosesterterpene, isolated from Smenospongia sp.
(E)-2-(3-methylnon-2-enyl)benzene-1,4-diol
-
-
(E)-2-(4-hydroxy-3-methylbut-2-enyl)benzene-1,4-diol
-
-
(E)-2-(9-hydroxy-3-methylnon-2-enyl)benzene-1,4-diol
-
-
1,2-bis(5-hydroxy-1H-indol-3-yl)ethane-1,2-dione
-
-
1-(2-aminoethyl)-1H-indol-6-ol
-
-
1-(3-methoxyphenyl)-2,3,4,9-tetrahydro-1H-b-carboline
-
-
1-(4-ethylpiperazin-1-yl)-3-nitropropan-1-one
-
-
1-(4-methoxyphenyl)-2,3,4,9-tetrahydro-1H-b-carboline
-
-
1-(naphthalen-2-yl)-2,3,4,9-tetrahydro-1H-b-carboline
-
-
1-carboxy-6-hydroxy-3,4-dihydro-beta-carboline
-
weak inhibition, isolated from marine sponge Hyrtios sp. (Thorectidae family)
1-cyclopropyl-6-fluoro-7-[4-(3-nitropropanoyl)piperazin-1-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
-
1-cyclopropyl-7-(3,5-dimethyl-4-(3-nitropropanoyl)piperazin-1-yl)-6-fluoro-8-methoxy-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
-
-
1-ethyl-6,8-difluoro-7-[3-methyl-4-(3-nitropropanoyl)piperazin-1-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
-
1-ethyl-6-fluoro-7-[4-(3-nitropropanoyl)piperazin-1-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
-
12-deacetoxy-23-acetoxy-19-O-acetylscalarin
-
cytotoxic, isolated from Smenospongia sp.
12-deacetoxy-23-acetoxyscalarin
-
cytotoxic, isolated from Smenospongia sp.
12-deacetoxy-23-hydroxyheteronemin
-
cytotoxic, isolated from Smenospongia sp.
2,2',3,3'-tetrabromo-4,4',5,5'-tetrahydroxydiphenylmethane
-
-
2,2',3-tribromo-3',4,4',5-tetrahydroxy-6'-hydroxymethyldiphenylmethane
-
-
2,2',3-tribromo-4,4',5,5'-tetrahydroxybibenzyl
-
-
-
2,2'-dibromo-4,4',5,5'-tetrahydroxybibenzyl
-
-
-
2,3-dibromo-4,5-dihydroxybenzyl alcohol
-
-
2,3-dibromo-4,5-dihydroxybenzyl methyl ether
-
-
2-(3-methylbut-2-enyl)benzene-1,4-diol
-
-
2-allylbenzene-1,4-diol
-
-
2-hydroxy-1-(5-hydroxy-1H-indol-3-yl)ethanone
-
-
2-mercaptoethanol
-
-
2-mercaptoethanol
-
increase of activity
2-mercaptoethanol
Candida brassicae
-
increase of activity
2-oxoglutarate
-
-
2-oxoglutarate
-
19% inhibition at 5 mM
2-oxoglutarate
-
-
2-oxoglutarate
-
-
2-[(2E,7R,8R)-7,8-dihydroxy-3-methyl-9-[(1S,4aS,8aS)-2,5,5,8a-tetramethyl-1,4,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]non-2-en-1-yl]benzene-1,4-diol
-
-
3,5-dibromo-4-hydroxyphenylethylamine
-
-
3-bromo-4-(2,3-dibromo-4,5-dihydroxybenzyl)-5-methoxymethylpyrocatechol
-
-
3-nitro-1-(4-phenylpiperazin-1-yl)propan-1-one
-
-
3-nitro-1-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]propan-1-one
-
-
3-nitropropionate
-
50% inhibition at 0.04 mM
3-nitropropionate
-
-
3-nitropropionate
-
irreversible inactivation
3-nitropropionate
-
no growth of Mycobacterium tuberculosis on fatty acids after addition of 3-nitropropionate
3-nitropropionate
-
-
3-nitropropionate
-
0.133 mM, complete inhibition
3-nitropropionate
-
-
3-nitropropionate
-
-
3-nitropropionate
-
0.1 mM, inhibition of bacterial growth on and metabolisation of proprionate as sole carbon in absence of Vitamin B12
3-nitropropionic acid
-
-
3-phosphoglycerate
-
-
3-phosphoglycerate
-
29% inhibition at 1 mM
4,4'-(oxydimethanediyl)bis(5,6-dibromobenzene-1,2-diol)
-
-
4,4'-ethane-1,2-diyldibenzene-1,2-diol
-
-
4,4'-methanediylbis(5,6-dibromobenzene-1,2-diol)
-
-
4,4'-methanediylbis(5-bromobenzene-1,2-diol)
-
-
4-chloromercuribenzoate
-
complete inactivation at 0.001 mM
4-hydroxy-9-deoxoidiadione
-
cytotoxic, linear furanosesterterpene, isolated from Smenospongia sp.
5-hydroxy-1H-indole-3-carbaldehyde
-
-
5-hydroxy-1H-indole-3-carboxylic acid methyl ester
-
weak inhibition, isolated from marine sponge Hyrtios sp. (Thorectidae family)
5-hydroxyindole-3-carbaldehyde
-
moderate inhibition, isolated from marine sponge Hyrtios sp. (Thorectidae family)
6-hydroxy-4,9-dihydro-3H-beta-carboline-1-carboxylic acid
-
-
ADP
-
20% inhibition at 2 mM
ADP
-
activation by ADP
ascorbate
-
enzyme is inhibited by an ascorbate plus Fe2+ system under aerobic conditions,16% residual activity at 2 mM ascorbate/0.02 mM Fe2+. Inactivation requires hydrogen peroxide, and can be prevented by catalase, EDTA, Mg2+, isocitrate, 20 mM glutathione, 20 mM dithiothreitol or 40 mM L-cysteine
ATP
-
35% inhibition at 2 mM
Ba2+
-
no inhibition
bis(2,3-dibromo-4,5-dihydroxyphenyl) ether
-
-
-
bis(2-bromo-4,5-dihydroxyphenyl) ether
-
-
-
bis(3,4-dihydroxyphenyl)methanone
-
-
-
bis(3-bromo-4,5-dihydroxyphenyl)methanone
-
-
-
Ca2+
-
no inhibition
citrate
-
22% inhibition at 5 mM
citrate
-
no inhibition at 0.1 mM
D-fructose-6-phosphate
-
-
D-Glucose-6-phosphate
-
-
Dithionitrobenzoate
-
-
dithiothreitol
-
-
Fe2+
-
enzyme is inhibited by an ascorbate plus Fe2+ system under aerobic conditions,16% residual activity at 2 mM ascorbate/0.02 mM Fe2+. Inactivation requires hydrogen peroxide, and can be prevented by catalase, EDTA, Mg2+, isocitrate, 20 mM glutathione, 20 mM dithiothreitol or 40 mM L-cysteine
-
fructose-1,6-bisphosphate
-
39% inhibition at 5 mM
fructose-1,6-bisphosphate
-
-
fructose-1,6-bisphosphate
-
-
fumarate
-
no inhibition at 0.1 mM
Glucose-1-phosphate
-
-
glucose-6-phosphate
-
44% inhibition at 5 mM
glucose-6-phosphate
-
-
glutathione
-
-
glutathione
Candida brassicae
-
increase of activity
glycolate
-
50% inhibition at 5 mM
glycolate
-
-
glycolate
-
20% inhibition at 1 mM
glycolate
Candida brassicae
-
-
glyoxylate
Lupinus sp.
-
-
glyoxylate
-
-
glyoxylate
-
linear competitive inhibitor
GSSG
-
ICL can be inactivated by glutathionylation and reactivated by glutaredoxin after reduced dithiothreitol treatment, whereas thioredoxin does not appear to regulate ICL activity
H2O2
-
inhibits enzyme activity with increased concentrations, no activity above 1.3 mM
H2O2
-
incubation with 0.1 mM H2O2 and 0.5mM GSH for 30 min results in a decrease of protein activity comparable with that obtained in the presence of GSSG. The addition of reduced dithiothreitol provides full reactivation of enzyme activity. Exposure to 1 mM H2O2 for 30 min results in an almost complete inactivation of the enzyme, whereas in the presence of a 10fold lower concentration of H2O2 (0.1 mM), ICL retains 20% of total activity after 30 min of incubation. GSH, reacting with sulfenic acid, can protect the protein from H2O2-mediated irreversible inactivation by glutathionylation
halisulfate 1
-
-
halisulfate 5
-
-
HgCl2
-
100% inhibition at 0.01 mM
HgCl2
-
30% inhibition at 0.1 mM
hydrohalisulfate 1
-
-
Hydroxymalonate
-
50% inhibition at 0.5 mM
hyrtiosin A
-
moderate inhibition, isolated from marine sponge Hyrtios sp. (Thorectidae family)
hyrtiosin B
-
strong inhibition, isolated from marine sponge Hyrtios sp. (Thorectidae family)
iodoacetate
-
70% inhibition at 10 mM
iodoacetate
-
isocitrate protects
Itaconate
-
89% inhibition at 1 mM
Itaconate
-
uncompetitive with respect to isocitrate
Itaconic acid
-
potent competitive inhibitor of ICL, 1 mg/ml reduces the activity to 42% of the uninhibited control. Inhibition of ICL enzymatic activity during chronic infection of rats forces the infection into an acute phase
KCl
-
strong activation by KCl
KCl
-
at pH-values above 8.6 inhibition, below pH 8.6 activation by KCl
malate
-
no inhibition at 0.1 mM
malate
Lupinus sp., Ricinus communis
-
-
malate
-
Icl enzyme, 50% inhibition at 5 mM
malate
-
competitive mode
Maleate
-
66% inhibition at 0.5 mM
-
Maleate
-
condensation reaction
-
malonate
-
condensation reaction
malonate
Lupinus sp.
-
-
malonate
Candida brassicae
-
-
methyl (1R,4bS,10aR,12aS)-10a-[(acetyloxy)methyl]-1-formyl-4b,7,7,12a-tetramethyl-1,4,4a,4b,5,6,6a,7,8,9,10,10a,10b,11,12,12a-hexadecahydrochrysene-2-carboxylate
-
scarlarane sesterterpene, isolated from Smenospongia sp.
methyl (1S,4bS,10aR,12aS)-10a-[(acetyloxy)methyl]-1-formyl-4b,7,7,12a-tetramethyl-1,4,4a,4b,5,6,6a,7,8,9,10,10a,10b,11,12,12a-hexadecahydrochrysene-2-carboxylate
-
scarlarane sesterterpene, isolated from Smenospongia sp.
methylenesuccinate
-
87% inhibition at 0.03 mM
methylenesuccinate
-
-
methylenesuccinate
-
condensation reaction
methylenesuccinate
-
-
methylenesuccinate
-
-
methylenesuccinate
-
-
Methylmalonate
-
50% inhibition at 15 mM
N'1-[(4-nitrophenyl)methylene]-2-[3-(4-bromo-2-fluorobenzyl)-4-oxo-1,2,3,4-tetrahydro-1-phthalazinyl]ethanohydrazide
-
is the most active compound
N-(4-bromo-3-methylphenyl)-3-nitropropanamide
-
-
-
N-(4-bromophenyl)-3-nitropropanamide
-
-
-
N-(4-chlorophenyl)-3-nitropropanamide
-
-
-
N-ethylmaleimide
Lupinus sp.
-
-
N-ethylmaleimide
-
40% inhibition at 1 mM
NaCl
-
activation by NaCl
oxalacetate
-
50% inhibition at 5 mM
oxalate
-
71% inhibition at 0.5 mM
oxalate
Lupinus sp.
-
-
oxalate
-
77% inhibition at 1 mM
oxalate
-
86% inhibition at 10 mM
oxalate
-
Icl enzyme, 50% inhibition at 5 mM
oxaloacetate
-
89% inhibition at 10 mM
p-chloromercuribenzoate
-
reversible by cysteine
p-chloromercuribenzoate
Lupinus sp.
-
-
p-chloromercuribenzoate
-
100% inhibition at 0.02 mM, reversible by 2-mercaptoethanol
p-chloromercuribenzoate
-
70% inhibition at 0.1 mM
p-hydroxymercuribenzoate
-
complete inhibition at 0.016 mM
phosphate
-
nonlinear competitive inhibitor, inhibition model
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
53% inhibition at 1 mM
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
Lupinus sp.
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
uncompetitive inhibitor
pyruvate
-
58% inhibition at 5 mM
pyruvate
-
87% inhibition at 10 mM
serotonin
-
moderate inhibition, isolated from marine sponge Hyrtios sp. (Thorectidae family)
sodium (2S)-5-furan-3-yl-2-[(1R)-1-hydroxy-2-[(1S,2R,4aR,8aR)-2-methyl-5-methylidenedecahydronaphthalen-1-yl]ethyl]pentyl sulfate
-
-
Sr2+
-
no inhibition
succinate
-
21% inhibition at 5 mM
succinate
-
7% inhibition at 0.5 mM
succinate
-
-
succinate
Lupinus sp.
-
-
succinate
-
38% inhibition at 1 mM
succinate
Candida brassicae
-
-
succinate
-
AceA enzyme, 50% inhibition at 5 mM
succinate
-
competitive mode
succinate
-
33% inhibition at 10 mM
sulfhydryl compounds
-
-
sulfhydryl compounds
-
increase of activity
sulfhydryl compounds
-
increase of activity
Tartrate
-
33% inhibition at 0.5 mM
Tartrate
Lupinus sp.
-
-
threo-DL-homoisocitrate
-
-
-
Urea
-
partial inactivation
XHD-1
-
extract of Illicium verum
-
XHD-2
-
extract of Zingiber officinale
-
Zn2+
Candida brassicae
-
-
[(5bS,11aR,13aS)-5b,8,8,13a-tetramethyl-5,5a,5b,6,7,7a,8,9,10,11,11b,12,13,13a-tetradecahydrochryseno[1,2-c]furan-11a(4H)-yl]methanol
-
scarlarane sesterterpene, isolated from Smenospongia sp.
[(5bS,11aR,13aS)-5b,8,8,13a-tetramethyl-5,5a,5b,6,7,7a,8,9,10,11,11b,12,13,13a-tetradecahydrochryseno[1,2-c]furan-11a(4H)-yl]methyl acetate
-
scarlarane sesterterpene, isolated from Smenospongia sp.
[(5bS,11aR,13aS,13bR)-1-methoxy-5b,8,8,13a-tetramethyl-1,5,5a,5b,6,7,7a,8,9,10,11,11b,12,13,13a,13b-hexadecahydrochryseno[1,2-c]furan-11a(3H)-yl]methanol
-
scarlarane sesterterpene, isolated from Smenospongia sp.
Mn2+
Candida brassicae
-
inhibition in presence of Mg2+, activation in absence of Mg2+
additional information
-
not inhibited by bromopyruvate
-
additional information
-
6-hydroxy-3,4-dihydro-1-oxo-beta-carboline, isolated from marine sponge Hyrtios sp. (Thorectidae family), defined inactive as inhibitor since IC50 is higher than 0.989 mM at a concentration of 2 mg/ml
-
additional information
-
some 2-[3-(4-bromo-2-fluorobenzyl)-4-oxo-3,4-dihydro-1-phthalazinyl]acetic acid hydrazones show 45-61% inhibition at 10 mM
-
additional information
-
natural glyoxylate cycle inhibitors such 5-hydroxyindole-type alkaloids are potent inhibitors
-
additional information
-
halisulfates from the tropical sponge Hippospongia sp. are able to inhibit ICL activity, appressorium formation and C2 utilization
-
additional information
-
extracts of Illicium verum and Zingiber officinale inhibit ICL
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
increase of activity
2-mercaptoethanol
Candida brassicae
-
increase of activity
2-mercaptoethanol
-
41% increase of activity at 1 mM
acetate
-
activity of the ICL promoter is significantly upregulated during growth on acetate
acetyl-CoA
Q8LPA6
more than 4fold increased enzyme activity in the presence of 150 microM acetyl-CoA
acetyl-CoA
Q8LPA6
increases the substrate binding affinities isocitrate and succinate, but had little effect on the affinity for glyoxylate
cysteine
-
increase of activity
cysteine
-
increase of activity
cysteine
Candida brassicae
-
increase of activity
dithioerythritol
Candida brassicae
-
increase of activity
dithiothreitol
-
increase of activity; optimal concentration 5 mM
dithiothreitol
Lupinus sp.
-
increase of activity
dithiothreitol
-
increase of activity; optimal concentration 1 mM
dithiothreitol
Candida brassicae
-
increase of activity
dithiothreitol
-
65% increase of activity at 1 mM
glutaredoxin 1
-
reactivation of GSSG-treated ICL in the presence of glutaredoxin 1 within 20 min
-
glutathione
Candida brassicae
-
increase of activity
glutathione
-
35% increase of activity at 1 mM
Na2S2O4
Lupinus sp.
-
increase of activity
Reducing agents
Lupinus sp.
-
increase of activity
-
sulfhydryl compounds
-
increase of activity
sulfhydryl compounds
-
increase of activity
thioglycolate
Lupinus sp.
-
increase of activity
thiol compounds
-
increase of activity
thiol compounds
-
increase of activity
thiol compounds
Candida brassicae
-
increase of activity
L-cysteine
-
45% increase of activity at 1 mM
additional information
-
no evidence that isocitrate lyase contains coenzyme
-
additional information
-
no significant change in enzyme activity after incubation with serine, glycine, aspartic and glutamic acids
-
additional information
-
no reactivation of GSSG-treated ICL in the presence of thioredoxin 1
-
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
-
additional information
-
ICL activity increases in pellicles in synthetic media as a consequence of fatty acid degradation as well as under microaerophilic growth conditions
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.1
-
(2R)-2-ethyl malate
Q05957
pH 7.5, 25C
0.29
-
(2R)-2-methyl malate
Q05957
pH 7.5, 25C
0.45
-
(2R)-ethyl-(3S)-methyl malate
Q05957
pH 7.5, 25C
0.53
-
(2R)-ethyl-(3S)-methyl malate
Q05957
pH 7.5, 25C
8
-
(2R)-isobutyl-(3S)-methyl malate
Q05957
pH 7.5, 25C
0.098
-
(2R)-propyl-(3S)-methyl malate
Q05957
pH 7.5, 25C
0.104
-
(2R,3R:2S,3S)-2-methyl-isocitrate
Q05957
pH 7.5, 25C
0.026
-
(2R,3S)-2,3-dimethyl malate
Q05957
pH 7.5, 25C
0.029
-
(2R,3S)-2,3-dimethyl malate
Q05957
pH 7.5, 25C
0.042
-
(2R,3S)-isocitrate
Q05957
pH 7.5, 25C
0.069
-
(2R,3S:2S,3R)-2-methyl-isocitrate
Q05957
pH 7.5, 25C
0.718
-
(2R,3S:2S,3R)-2-methyl-isocitrate
P0A5H3
ICL1, in 50 mM MOPS pH 6.8, 5 mM MgCl2
0.025
-
acetyl-CoA
Q8LPA6
pH 8.0, 30C
0.015
-
DL-isocitrate
-
-
0.087
0.096
DL-isocitrate
-
-
0.093
-
DL-isocitrate
-
-
0.136
-
DL-isocitrate
-
-
0.51
-
DL-isocitrate
-
20C, pH 6.8
0.6
-
DL-isocitrate
-
-
0.62
-
DL-isocitrate
Candida brassicae
-
imidazole-HCl buffer pH 6.85
0.633
-
DL-isocitrate
-
15C, pH 6.8, Km increases with elevating temperature
1.2
1.7
DL-isocitrate
-
-
1.532
-
DL-isocitrate
Candida brassicae
-
sodium phosphate buffer, pH 6.85
1.6
-
DL-isocitrate
-
pH 7
0.018
-
DS-isocitrate
-
pH 6.8
-
0.033
-
DS-isocitrate
-
HEPES, pH 7.0
-
0.062
-
DS-isocitrate
-
pH 7.3
-
0.066
-
DS-isocitrate
-
-
-
0.25
-
DS-isocitrate
-
-
-
0.014
-
glyoxylate
-
-
0.04
-
glyoxylate
Q8LPA6
pH 8.0, 30C
0.05
-
glyoxylate
Lupinus sp.
-
-
0.088
-
glyoxylate
-
pH 7, microgravity, condensation reaction
0.092
-
glyoxylate
-
pH 7, standard g, condensation reaction
0.13
-
glyoxylate
-
-
0.96
-
glyoxylate
Q8LPA6
D475N mutant protein, 0.15 mM acetyl-CoA, 10 mM succinate, pH 6.5, 30C
1.3
-
glyoxylate
Q8LPA6
D475N mutant protein, 10 mM succinate, pH 6.5, 30C
0.0157
-
Isocitrate
-
pH 6.5
0.016
-
Isocitrate
-
pH 7.5, 25C
0.032
-
Isocitrate
-
phosphate, pH 6.0
0.035
-
Isocitrate
Lupinus sp.
-
imidazole, pH 7.0
0.039
-
Isocitrate
-
MOPS, pH 6.8
0.039
-
Isocitrate
-
pH 7, standard g, cleavage reaction
0.043
-
Isocitrate
-
pH 7, microgravity, cleavage reaction
0.05
-
Isocitrate
-
pH 7.5, 25C
0.056
-
Isocitrate
-
ICL1
0.06
-
Isocitrate
-
100 mM Hepes, pH 7.0
0.07
-
Isocitrate
-
-
0.083
-
Isocitrate
-
ICL2
0.1
0.2
Isocitrate
Lupinus sp.
-
Tris, triethanolamine or imidazole buffer
0.1
-
Isocitrate
-
ICL
0.11
-
Isocitrate
-
TRA, pH 7.0
0.159
-
Isocitrate
-
in 50 mM potassium phosphate, 4 mM MgCl2, 4 mM phenylhydrazine, 12 mM cysteine, pH 7.0, at 37C
0.188
-
Isocitrate
P0A5H3
ICL1, in 50 mM MOPS pH 6.8, 5 mM MgCl2
0.25
-
Isocitrate
-
MOPS, pH 7.5
0.25
-
Isocitrate
P0A9G6
10C
0.26
-
Isocitrate
-
mutant Q217K, 10C
0.29
-
Isocitrate
-
phosphate, pH 7.5
0.3
-
Isocitrate
-
phosphate, pH 7.0
0.33
-
Isocitrate
-
wild-type, 10C
0.47
-
Isocitrate
-
wild-type, 20C
0.5
-
Isocitrate
-
mutant Q217K, 30C
0.51
-
Isocitrate
-
50 mM MOPS buffer, pH 7.5, with 1 mM MgCl2, 10 mM 2-mercaptoethanol, and 2.7 mM O-nitrophenyl-beta-D-galactopyranoside
0.52
-
Isocitrate
-
60 mM potassium phosphate, pH 7.5
0.65
-
Isocitrate
P0A9G6
40C
0.66
-
Isocitrate
-
Tris, pH 7.6
0.67
-
Isocitrate
-
phosphate, pH 7.5
0.72
-
Isocitrate
-
-
0.76
-
Isocitrate
-
60 mM triethanolamine, pH 7.5
0.76
-
Isocitrate
-
mutant Q207H, 10C
0.96
-
Isocitrate
Q97YI8
pH 7.5, 70C, recombinant enzyme
1
-
Isocitrate
Lupinus sp.
-
phosphate buffer, pH 6.8 or 7.5
1
-
Isocitrate
-
phosphate, pH 6.8
1.14
-
Isocitrate
P0A5H3
ICL2, in Tricine-HCl pH 7.5, 5 mM MgCl2
1.4
-
Isocitrate
-
pH 7.5, 25C
2.07
-
Isocitrate
-
mutant Q207H, 30C
6.7
-
Isocitrate
Q8LPA6
when acetyl-CoA is present at concentrations higher than 5 mM, the Km value for isocitrate decreased by about one-third and the Vmax value increased about 2-fold, pH not specified in the publication, temperature not specified in the publication
7.6
-
Isocitrate
Q8LPA6
pH 6.5, 30C
0.092
-
Mg2+
-
pH 7
0.13
-
oxalacetate
Q05957
pH 7.5, 25C
0.044
-
succinate
-
-
0.053
-
succinate
-
pH 7, microgravity, condensation reaction
0.063
-
succinate
-
pH 7, standard g, condensation reaction
0.2
-
succinate
Lupinus sp.
-
-
0.59
-
succinate
-
-
1.1
-
succinate
-
-
6
-
succinate
Q8LPA6
D475N mutant protein, 1.5 mM glyoxylate, sharply decreased with increasing acetyl-CoA concentration, pH 6.5, 30C
0.145
-
threo D-(s)-isocitrate
-
Icl enzyme, 37C
1.3
-
threo D-(s)-isocitrate
-
AceA enzyme, Tricine buffer, 37C, pH 7.5
0.008
-
threo-Ds-isocitrate
-
-
0.018
-
threo-Ds-isocitrate
-
-
0.02
-
threo-Ds-isocitrate
-
25 mM imidazole buffer, pH 6.8
0.021
-
threo-Ds-isocitrate
-
-
0.04
-
threo-Ds-isocitrate
-
-
0.05
-
threo-Ds-isocitrate
-
-
0.05
-
threo-Ds-isocitrate
-
-
0.051
-
threo-Ds-isocitrate
-
-
0.1
-
threo-Ds-isocitrate
-
Hepes, pH 7.4
0.2
-
threo-Ds-isocitrate
-
0.4 M KCl, 25 mM imidazole buffer, pH 6.8
0.26
-
threo-Ds-isocitrate
-
Hepes, pH 7.4, 60 mM Cl-
0.3
-
threo-Ds-isocitrate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.25
-
(2R,3S:2S,3R)-2-methyl-isocitrate
P0A5H3
ICL1, in 50 mM MOPS pH 6.8, 5 mM MgCl2
18.1
-
DL-isocitrate
-
20C, pH 6.8
32
-
DL-isocitrate
-
pH 7
1.38
-
Isocitrate
P0A5H3
ICL2, in Tricine-HCl pH 7.5, 5 mM MgCl2
5.24
-
Isocitrate
P0A5H3
ICL1, in 50 mM MOPS pH 6.8, 5 mM MgCl2
8.43
-
Isocitrate
-
in 50 mM MOPS buffer, pH 7.5, with 1 mM MgCl2, 10 mM 2-mercaptoethanol, and 2.7 mM O-nitrophenyl-beta-D-galactopyranoside
13.3
-
Isocitrate
A8C5K8
mutant enzyme A341N, at 25C
26.6
-
Isocitrate
A8C5K8
mutant enzyme Q47K, at 25C
28.5
-
Isocitrate
A8C5K8
wild type enzyme, at 25C
44.5
-
Isocitrate
-
-
122
-
Isocitrate
-
-
800
-
Isocitrate
-
-
24
-
threo-Ds-isocitrate
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.003
-
3-nitropropionate
-
Icl enzyme, 37C
0.015
-
3-nitropropionate
-
-
0.04
-
3-nitropropionate
-
-
0.11
-
3-nitropropionate
-
AceA enzyme, 37C
0.12
-
Bromopyruvate
-
Icl enzyme, 37C
0.71
-
Bromopyruvate
-
AceA enzyme, 37C
0.06
-
D-fructose-6-phosphate
-
-
0.3
-
D-Glucose-6-phosphate
-
-
0.5
-
Hydroxymalonate
-
-
0.0119
-
Itaconate
-
pH 6.5
0.068
-
Itaconate
-
pH 7
0.12
-
Itaconate
-
Icl enzyme, 37C
0.22
-
Itaconate
-
AceA enzyme, 37C
0.19
-
itaconic anhydride
-
Icl enzyme, 37C
0.48
-
itaconic anhydride
-
AceA enzyme, 37C
15
-
Methylmalonate
-
-
5
-
oxalacetate
-
-
0.037
-
oxalate
-
pH 7
0.893
-
phosphoenolpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.1), 10 mM MgCl2, 12 mM cysteine
1.8
-
succinate
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0126
-
(1R,2R,6E)-8-(2,5-dihydroxyphenyl)-2-hydroxy-6-methyl-1-[[(1S,4aS,8aS)-2,5,5,8a-tetramethyl-1,4,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]methyl]oct-6-en-1-yl hydrogen sulfate
-
-
0.01561
-
(2-bromo-4,5-dihydroxybenzyl)(2,3-dibromo-4,5-dihydroxybenzyl) ether
-
pH not specified in the publication, temperature not specified in the publication
-
0.06819
-
(2-bromo-4,5-dihydroxyphenyl)(3,4-dihydroxyphenyl) ether
-
pH not specified in the publication, temperature not specified in the publication
-
0.185
-
(2E,6E)-9-[(2R)-6-hydroxy-2,8-dimethyl-3,4-dihydro-2H-chromen-2-yl]-2,6-dimethylnona-2,6-dienal
-
pH 7.0, 37C
0.1729
-
(2E,7E)-10-[(2R)-6-hydroxy-2,8-dimethyl-3,4-dihydro-2H-chromen-2-yl]-3,7-dimethyl-2-(2-methylprop-1-en-1-yl)deca-2,7-dienal
-
pH 7.0, 37C
0.1184
-
(2R)-2-[(3E,7E)-9-(hydroxymethyl)-4,8,11-trimethyldodeca-3,7,10-trien-1-yl]-2,8-dimethyl-3,4-dihydro-2H-chromen-6-ol
-
pH 7.0, 37C
0.00265
-
(3-bromo-4,5-dihydroxyphenyl)(2,3-dibromo-4,5-dihydroxyphenyl)methanone
-
pH not specified in the publication, temperature not specified in the publication
-
0.4
-
(E)-2-(3-methylnon-2-enyl)benzene-1,4-diol
-
-
0.29
-
(E)-2-(4-hydroxy-3-methylbut-2-enyl)benzene-1,4-diol
-
-
0.28
-
(E)-2-(9-hydroxy-3-methylnon-2-enyl)benzene-1,4-diol
-
-
0.089
-
1,2-bis(5-hydroxy-1H-indol-3-yl)ethane-1,2-dione
-
pH not specified in the publication, temperature not specified in the publication
0.301
-
1-(2-aminoethyl)-1H-indol-6-ol
-
pH not specified in the publication, temperature not specified in the publication
0.075
-
1-(3-methoxyphenyl)-2,3,4,9-tetrahydro-1H-b-carboline
-
pH not specified in the publication, temperature not specified in the publication
0.0126
-
1-(4-ethylpiperazin-1-yl)-3-nitropropan-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.18
-
1-(4-methoxyphenyl)-2,3,4,9-tetrahydro-1H-b-carboline
-
pH not specified in the publication, temperature not specified in the publication
0.137
-
1-(naphthalen-2-yl)-2,3,4,9-tetrahydro-1H-b-carboline
-
pH not specified in the publication, temperature not specified in the publication
0.379
-
1-carboxy-6-hydroxy-3,4-dihydro-beta-carboline
-
0.874 mg/ml
0.00012
-
1-cyclopropyl-6-fluoro-7-[4-(3-nitropropanoyl)piperazin-1-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0001
-
1-cyclopropyl-7-(3,5-dimethyl-4-(3-nitropropanoyl)piperazin-1-yl)-6-fluoro-8-methoxy-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.00146
-
1-ethyl-6,8-difluoro-7-[3-methyl-4-(3-nitropropanoyl)piperazin-1-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.002
-
2,2',3,3'-tetrabromo-4,4',5,5'-tetrahydroxydiphenylmethane
-
in 20 mM sodium phosphate buffer (pH 7.0), with 3.75 mM MgCl2 and 4.1 mM phenylhydrazine, at 37C
0.0028
-
2,2',3-tribromo-3',4,4',5-tetrahydroxy-6'-hydroxymethyldiphenylmethane
-
in 20 mM sodium phosphate buffer (pH 7.0), with 3.75 mM MgCl2 and 4.1 mM phenylhydrazine, at 37C
0.01477
-
2,2',3-tribromo-4,4',5,5'-tetrahydroxybibenzyl
-
pH not specified in the publication, temperature not specified in the publication
-
0.02121
-
2,2'-dibromo-4,4',5,5'-tetrahydroxybibenzyl
-
pH not specified in the publication, temperature not specified in the publication
-
0.0926
-
2,3-dibromo-4,5-dihydroxybenzyl alcohol
-
in 20 mM sodium phosphate buffer (pH 7.0), with 3.75 mM MgCl2 and 4.1 mM phenylhydrazine, at 37C
0.1256
-
2,3-dibromo-4,5-dihydroxybenzyl methyl ether
-
in 20 mM sodium phosphate buffer (pH 7.0), with 3.75 mM MgCl2 and 4.1 mM phenylhydrazine, at 37C
0.61
-
2-(3-methylbut-2-enyl)benzene-1,4-diol
-
-
1.02
-
2-allylbenzene-1,4-diol
-
-
0.318
-
2-hydroxy-1-(5-hydroxy-1H-indol-3-yl)ethanone
-
pH not specified in the publication, temperature not specified in the publication
0.015
-
2-[(2E,7R,8R)-7,8-dihydroxy-3-methyl-9-[(1S,4aS,8aS)-2,5,5,8a-tetramethyl-1,4,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]non-2-en-1-yl]benzene-1,4-diol
-
-
0.116
-
3,5-dibromo-4-hydroxyphenylethylamine
-
in 20 mM sodium phosphate buffer (pH 7.0), with 3.75 mM MgCl2 and 4.1 mM phenylhydrazine, at 37C
0.0021
-
3-bromo-4-(2,3-dibromo-4,5-dihydroxybenzyl)-5-methoxymethylpyrocatechol
-
in 20 mM sodium phosphate buffer (pH 7.0), with 3.75 mM MgCl2 and 4.1 mM phenylhydrazine, at 37C
0.04121
-
3-nitro-1-(4-phenylpiperazin-1-yl)propan-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0348
-
3-nitropropionate
-
pH 7.0, 37C
0.0507
-
3-nitropropionate
-
pH not specified in the publication, temperature not specified in the publication
0.051
-
3-nitropropionate
-
pH not specified in the publication, temperature not specified in the publication
0.0924
-
3-nitropropionate
-
-
0.0924
-
3-nitropropionate
-
in 20 mM sodium phosphate buffer (pH 7.0), with 3.75 mM MgCl2 and 4.1 mM phenylhydrazine, at 37C
0.116
-
3-nitropropionic acid
-
pH not specified in the publication, temperature not specified in the publication
0.02806
-
4,4'-(oxydimethanediyl)bis(5,6-dibromobenzene-1,2-diol)
-
pH not specified in the publication, temperature not specified in the publication
0.05847
-
4,4'-ethane-1,2-diyldibenzene-1,2-diol
-
pH not specified in the publication, temperature not specified in the publication
0.01844
-
4,4'-methanediylbis(5,6-dibromobenzene-1,2-diol)
-
pH not specified in the publication, temperature not specified in the publication
0.247
-
5-hydroxy-1H-indole-3-carbaldehyde
-
pH not specified in the publication, temperature not specified in the publication
0.799
-
5-hydroxy-1H-indole-3-carboxylic acid methyl ester
-
0.153 mg/ml
0.247
-
5-hydroxyindole-3-carbaldehyde
-
0.0398 mg/ml
0.38
-
6-hydroxy-4,9-dihydro-3H-beta-carboline-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.01163
-
bis(2,3-dibromo-4,5-dihydroxyphenyl) ether
-
pH not specified in the publication, temperature not specified in the publication
-
0.03088
-
bis(2-bromo-4,5-dihydroxyphenyl) ether
-
pH not specified in the publication, temperature not specified in the publication
-
0.02258
-
bis(3,4-dihydroxyphenyl)methanone
-
pH not specified in the publication, temperature not specified in the publication
-
0.00889
-
bis(3-bromo-4,5-dihydroxyphenyl)methanone
-
pH not specified in the publication, temperature not specified in the publication
-
0.318
-
hyrtiosin A
-
0.061 mg/ml
0.089
-
hyrtiosin B
-
0.285 mg/ml
0.06
-
Itaconate
-
-
0.0368
-
N-(4-bromo-3-methylphenyl)-3-nitropropanamide
-
pH not specified in the publication, temperature not specified in the publication
-
0.03246
-
N-(4-bromophenyl)-3-nitropropanamide
-
pH not specified in the publication, temperature not specified in the publication
-
0.02132
-
N-(4-chlorophenyl)-3-nitropropanamide
-
pH not specified in the publication, temperature not specified in the publication
-
0.301
-
serotonin
-
0.053 mg/ml
0.0674
-
sodium (2S)-5-furan-3-yl-2-[(1R)-1-hydroxy-2-[(1S,2R,4aR,8aR)-2-methyl-5-methylidenedecahydronaphthalen-1-yl]ethyl]pentyl sulfate
-
-
5
-
succinate
-
in 50 mM MOPS buffer, pH 7.5, with 1 mM MgCl2, 10 mM 2-mercaptoethanol, and 2.7 mM O-nitrophenyl-beta-D-galactopyranoside
0.0477
-
XHD-1
-
in 50 mM potassium phosphate, 4 mM MgCl2, 4 mM phenylhydrazine, 12 mM cysteine, pH 7.0, at 37C
-
0.0182
-
XHD-2
-
in 50 mM potassium phosphate, 4 mM MgCl2, 4 mM phenylhydrazine, 12 mM cysteine, pH 7.0, at 37C
-
0.141
-
(4R,5R)-4-[(2E)-5-[(2R)-6-hydroxy-2,8-dimethyl-3,4-dihydro-2H-chromen-2-yl]-2-methylpent-2-en-1-yl]-2-methyl-5-(2-methylprop-1-en-1-yl)cyclopent-2-en-1-one
-
pH 7.0, 37C
additional information
-
(4S,5bR,11aS,13aS,13bR)-4-hydroxy-5b,8,8,11a,13a-pentamethyl-1,4,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1-yl acetate
-
> 0.1 mg/ml
additional information
-
(4S,5bS,11aR,13aS,13bR)-11a-formyl-4-hydroxy-5b,8,8,13a-tetramethyl-1,4,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1-yl acetate
-
> 0.1 mg/ml
additional information
-
(4S,5bS,11aR,13aS,13bR)-11a-[(acetyloxy)methyl]-5b,8,8,13a-tetramethyl-1,4,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1,4-diyl diacetate
-
> 0.1 mg/ml
additional information
-
(5bS,11aR,13aS,13bR)-11a-(hydroxymethyl)-5b,8,8,13a-tetramethyl-3-oxo-1,3,5,5a,5b,6,7,7a,8,9,10,11,11a,11b,12,13,13a,13b-octadecahydrochryseno[1,2-c]furan-1-yl acetate
-
> 0.1 mg/ml
additional information
-
(5E)-5-[(2R,6E,10E)-13-furan-3-yl-2,6,10-trimethyltrideca-6,10-dien-1-ylidene]-4-hydroxy-3-methylfuran-2(5H)-one
-
0.027 mg/ml
additional information
-
(5Z)-5-[(2R,5Z,9Z)-13-furan-3-yl-2,6,10-trimethyltrideca-5,9-dien-1-ylidene]-4-hydroxy-3-methylfuran-2(5H)-one
-
0.0312 mg/ml
0.0002
-
1-ethyl-6-fluoro-7-[4-(3-nitropropanoyl)piperazin-1-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
additional information
-
12-deacetoxy-23-acetoxy-19-O-acetylscalarin
-
> 0.1 mg/ml
additional information
-
12-deacetoxy-23-acetoxyscalarin
-
0.0672 mg/ml
additional information
-
12-deacetoxy-23-hydroxyheteronemin
-
> 0.1 mg/ml
0.03018
-
3-nitro-1-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]propan-1-one
-
pH not specified in the publication, temperature not specified in the publication
additional information
-
3-nitropropionate
-
0.006 mg/ml
0.04615
-
4,4'-methanediylbis(5-bromobenzene-1,2-diol)
-
pH not specified in the publication, temperature not specified in the publication
additional information
-
4-hydroxy-9-deoxoidiadione
-
> 0.1 mg/ml
0.0033
-
itaconic anhydride
-
in 50 mM potassium phosphate, 4 mM MgCl2, 4 mM phenylhydrazine, 12 mM cysteine, pH 7.0, at 37C
additional information
-
methyl (1R,4bS,10aR,12aS)-10a-[(acetyloxy)methyl]-1-formyl-4b,7,7,12a-tetramethyl-1,4,4a,4b,5,6,6a,7,8,9,10,10a,10b,11,12,12a-hexadecahydrochrysene-2-carboxylate
-
0.055 mg/ml
additional information
-
methyl (1S,4bS,10aR,12aS)-10a-[(acetyloxy)methyl]-1-formyl-4b,7,7,12a-tetramethyl-1,4,4a,4b,5,6,6a,7,8,9,10,10a,10b,11,12,12a-hexadecahydrochrysene-2-carboxylate
-
> 0.1 mg/ml
additional information
-
[(5bS,11aR,13aS)-5b,8,8,13a-tetramethyl-5,5a,5b,6,7,7a,8,9,10,11,11b,12,13,13a-tetradecahydrochryseno[1,2-c]furan-11a(4H)-yl]methanol
-
0.0457 mg/ml
additional information
-
[(5bS,11aR,13aS)-5b,8,8,13a-tetramethyl-5,5a,5b,6,7,7a,8,9,10,11,11b,12,13,13a-tetradecahydrochryseno[1,2-c]furan-11a(4H)-yl]methyl acetate
-
> 0.1 mg/ml
additional information
-
[(5bS,11aR,13aS,13bR)-1-methoxy-5b,8,8,13a-tetramethyl-1,5,5a,5b,6,7,7a,8,9,10,11,11b,12,13,13a,13b-hexadecahydrochryseno[1,2-c]furan-11a(3H)-yl]methanol
-
0.042 mg/ml
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.002
-
-
knock-out mutant enzyme after growth on gluconate, crude extract
0.0029
-
-
in cell-free extracts after cell growth in YPD medium
0.003
-
-
knock-out mutant enzyme after growth on gluconate + heptanoate, crude extract
0.004
-
-
strain BW3782, 0.02% glucose (chemostat); strain BW3782, 0.2% glucose (batch)
0.0048
-
-
in cell-free extracts after cell growth in YPD medium containing 1 M NaCl
0.005
-
-
in cell-free extracts after cell growth in YPD medium containing 1 M KCl
0.011
-
-
control cells, pH 7.3
0.022
-
-
strain BW3709, 0.2% glucose (batch)
0.023
-
-
strain BW3767, 0.2% glucose (batch)
0.034
-
-
strain BW2952, 0.2% glucose (batch)
0.04
-
-
homogenate
0.043
-
-
wild-type enzyme after growth on gluconate, crude extract
0.053
-
-
Al-stressed cells, pH 7.3
0.088
-
-
strain BW3480, 0.02% glucose (chemostat)
0.138
-
-
recombinant enzyme in crude extract
0.138
-
-
in 50 mM MOPS buffer (pH 7.3), 5 mM MgCl2, 1 mM EDTA, 4 mM phenylhydrazine HCl
0.155
-
-
strain MG1655, 0.2% glucose (batch)
0.19
-
-
strain BW3708, 0.2% glucose (batch)
0.22
-
-
crude cell extract
0.248
-
-
strain BW2952, 0.02% glucose (chemostat)
0.321
-
-
wild-type enzyme after growth on gluconate + heptanoate, crude extract
0.471
-
-
strain BW3767, 0.02% glucose (chemostat)
0.538
-
-
strain BW3709, 0.02% glucose (chemostat)
0.586
-
Q5XTP4, -
37C, wild type
0.636
-
Q8LPA6
isocitrate lyase activity
1.066
-
-
strain BW2952, 0.2% acetate (batch)
1.227
-
-
strain BW3767, 0.2% acetate (batch)
1.3
-
-
Icl enzyme
1.656
-
-
strain BW3709, 0.2% acetate (batch)
1.674
-
-
strain MG1655, 0.02% glucose (chemostat)
1.778
-
-
strain BW3708, 0.02% glucose (chemostat)
1.83
-
Lupinus sp.
-
-
2.084
-
-
strain MG1655, 0.2% acetate (batch)
2.23
-
Q8RPZ0, -
-
2.9
-
-
-
3.075
-
-
strain BW3708, 0.2% acetate (batch)
3.68
-
Lupinus sp.
-
-
3.85
-
-, Q5YLB6
pH and temperature not specified in the publication
4.4
-
-
ICL2, 1003fold purified
4.45
-
-
-
4.52
-
-
-
4.9
-
-
ICL1, 123fold purified
4.96
-
-
-
5.19
-
Q8LPA6
malate synthase activity
5.28
-
-
pH 7.5, 25C
5.5
-
-
pH 7.5, 25C
5.81
-
-
pH 7.5, 25C
6.17
-
-
-
7.9
-
-
after 30fold purification
8.01
-
Candida brassicae
-
-
8.4
-
-
after 38.2fold purification
8.8
10.9
-
-
9.48
-
-
-
9.5
-
-
purified ICL
10.1
-
-
-
10.5
-
-
mutant Q217K
14.5
-
-
mutant Q207H
14.6
-
-
wild-type
37.5
-
-
-
54
-
P0A9G6
-
additional information
-
-
-
additional information
-
-
increased enzyme activity in seedlings submerged for more than 12 h, indicating the activation of the glyoxylate cycle under low oxygen conditions
additional information
-
Q5XTP4, -
37C, mutant Ace-21 no activity
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
ICL2
6.5
-
Q8LPA6
isocitrate lyase
6.5
-
-
-
6.8
-
Lupinus sp.
-
-
6.8
-
Candida brassicae
-
-
6.8
-
-
Icl enzyme
6.8
-
-
wild-type
6.85
-
-
mutants Q207H and Q217k
6.9
-
P0A9G6
-
7
-
Lupinus sp.
-
triethanolamine buffer
7
-
Q05957
(2R,3S)-2-ethyl-3-methyl malate
7.2
7.3
-
-
7.2
7.6
-
-
7.2
-
-
-
7.3
7.5
-
-
7.35
7.6
-
-
7.5
8.5
Q8LPA6
malate synthase
7.5
-
Lupinus sp.
-
phosphate, Tris or imidazole buffer
7.5
-
-
presence of 0.3 M KCl
7.5
-
-
phosphate, Tris or imidazole buffer
7.5
-
-
AceA enzyme
7.5
-
-
ICL1
7.5
-
Q97YI8
assay at
8
-
-
absence of KCl
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8.5
-
50% activity at pH 5, 22% activity at pH 8.5, no activity at pH 9
6.9
7.9
-
50% of optimal activity at pH 6.9 and 7.9
7
9
-
30% of optimal activity at pH 7 and pH 9
7.2
8.2
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
25
-
wild type
27.5
30
-
mutant Q207H
30
32.5
-
mutant Q217K
37
-
Candida brassicae
-
-
50
-
-
-
70
-
Q97YI8
assay at
additional information
-
P0A9G6
optimum temperature above 40C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
-
-
half maximal enzyme activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
calculated from amino acid sequence
6.79
-
-, Q5YLB6
predicted
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Penicillium marneffei
-
higher expression levels than in mycelium and yeast, increased expression level two hours after macrophage internalization (coordinated with downregulation of gene encoding glyceraldehyde-3-phosphate dehydrogenase), Northern blot
Manually annotated by BRENDA team
Penicillium marneffei CBS 119456
-
higher expression levels than in mycelium and yeast, increased expression level two hours after macrophage internalization (coordinated with downregulation of gene encoding glyceraldehyde-3-phosphate dehydrogenase), Northern blot
-
Manually annotated by BRENDA team
Lupinus sp.
-
-
Manually annotated by BRENDA team
-
0.02% glucose (chemostat); 0.2% glucose (batch)
Manually annotated by BRENDA team
Fomitopsis palustris TYP-6137
-
-
-
Manually annotated by BRENDA team
Penicillium marneffei
-
lower expression levels than in conidium and yeast, Northern blot
Manually annotated by BRENDA team
Aspergillus fumigatus ATCC46645
-
-
-
Manually annotated by BRENDA team
Penicillium marneffei CBS 119456
-
lower expression levels than in conidium and yeast, Northern blot
-
Manually annotated by BRENDA team
-
ICL1 and and ICL2
Manually annotated by BRENDA team
Lupinus sp.
-
-
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
Penicillium marneffei
-
higher expression levels than in mycelium and lower expression than in conidium, Northern blot
Manually annotated by BRENDA team
Penicillium marneffei CBS 119456
-
higher expression levels than in mycelium and lower expression than in conidium, Northern blot
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Pseudomonas fluorescens 13525
-
-
-
Manually annotated by BRENDA team
-
membrane fraction (3 h, 180000xg) of cell-free extract, increased expression level upon oxidative stress induced by 8 h treatment with 100 microM menadione
Manually annotated by BRENDA team
Fomitopsis palustris TYP-6137
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Burkholderia pseudomallei (strain K96243)
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
13800
-
-
gel filtration
46830
-
-
mutant C247S mass spectrometry
46850
-
-
calculated from amino acid sequence
46860
-
-
mutant C178S mass spectrometry
46870
-
-
mutant C178S mass spectrometry, after 1 h of GSSG-treated ICL; wild-type, mass spectrometry
46890
-
-
mutant C178S mass spectrometry, after 24 h of GSSG-treated ICL; mutant C178S mass spectrometry, after 5 h of GSSG-treated ICL
47120
-
-
mutant C247S mass spectrometry, after 1 h of GSSG-treated ICL
47140
-
-
mutant C247S mass spectrometry, after 24 h of GSSG-treated ICL
47160
-
-
mutant C247S mass spectrometry, after 5 h of GSSG-treated ICL
47170
-
-
wild-type, mass spectrometry, after 1 h of GSSG-treated ICL
47190
-
-
wild-type, mass spectrometry, after 5 h of GSSG-treated ICL
47510
-
-
wild-type, mass spectrometry, after 24 h of GSSG-treated ICL
48000
-
-
single peak in ESI-MS
50000
-
-
calculated from amino acid sequence
59740
-
-, Q58A52
calculated from sequence of cDNA
60000
-
-, Q9I0K4
SDS-PAGE
60230
-
-
calculated from amino acid sequence
61000
-
-
SDS-PAGE
61600
-
-
calculation from sequence of DNA
64620
-
-
calculation from sequence of DNA
64740
-
P17069
calculation from sequence of DNA
114000
-
-
-
130000
-
-
gel filtration
130000
-
-
gel filtration
133000
-
-
blue native PAGE
133000
-
Q05957
gel filtration
140000
-
-
gel filtration
145000
170000
Lupinus sp.
-
gel filtration
145000
-
-
gel filtration
164000
-
-
gel filtration, ICL1
177000
-
-
gel filtration
180000
-
-
sedimentation equilibrium centrifugation
180000
-
-
gel filtration
180000
-
-
sedimentation equilibrium centrifugation, gel filtration
186000
-
-
gel filtration
188000
-
-
gel filtration
190000
-
Q97YI8
-
200000
210000
-
gel filtration
200000
-
-
gel filtration, glycerol density gradient
200000
-
-
gel filtration
207000
-
-
gel filtration, ICL2
208000
-
-
gel filtration
208000
-
-
gel filtration, ICL
215000
-
-
gel filtration
222000
-
-
calculation from sedimentation and diffusion data
240000
-
-
gel filtration
240000
-
-
gel filtration
240000
-
-
gel filtration
240000
-
-
gel-filtration
240000
-
A8C5K8
gel filtration
246000
-
-
gel filtration
250000
-
-
gel filtration
250000
-
-
gel filtration
250000
-
-
gel filtration
252000
-
-
gel filtration
255000
-
-
gel filtration
260000
-
Lupinus sp.
-
-
264000
-
-
gel filtration
264000
-
-
gel filtration
270000
-
-
gel filtration
272000
-
-
gel filtration
277000
-
-
gel filtration
290000
-
Candida brassicae
-
gel filtration
420000
-
Q8LPA6
gel filtration
475000
-
Q8RPZ0, -
calculated from amino acid sequence
480000
-
-
gel filtration
530000
-
Q8LPA6
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q5YLB6
x * 60000, SDS-PAGE
dimer
-
2 * 65000, SDS-PAGE
dimer
-
2 * 63000, calculation from amino acid sequence; 2 * 64000, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
homotetramer
A8C5K8
4 * 58131, calculated from amino acid sequence; 4 * 60000, gel filtration
homotetramer
-
4 * 46000, SDS-PAGE; 4 * 53750, gel filtration
homotetramer
P0A5H3
x-ray crystallography
homotetramer
-
4 * 66000, SDS-PAGE, gel filtration
homotetramer
Q97YI8
-
homotetramer
Q8LPA6
4 * 131000, gel filtration, calculated subunit molecular mass
homotetramer
Colwellia psychrerythraea NRC 1004
-
4 * 58131, calculated from amino acid sequence; 4 * 60000, gel filtration
-
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
4 * 44700, SDS-PAGE
tetramer
-
4*60000, SDS-PAGE
tetramer
-
4 * 64000, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 64000, SDS-PAGE
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
4 * 123000, SDS-PAGE
tetramer
-
4 * 28500
tetramer
Lupinus sp.
-
4 * 66000, SDS-PAGE
tetramer
-
4 * 66000, SDS-PAGE
tetramer
-
-
tetramer
-
4*67000, SDS-PAGE
tetramer
-
4 * 64000, SDS-PAGE
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
4 * 64000, SDS-PAGE
tetramer
-
4 * 62000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
Candida brassicae
-
4*71000, SDS-PAGE
tetramer
-
subunits of 62500 and 64000, SDS-PAGE
tetramer
-
4 * 62000, SDS-PAGE
tetramer
-
4 * 64700, SDS-PAGE
tetramer
-
monomers are identical, crystallization experiments
tetramer
-
4 * 64000, SDS-PAGE
tetramer
-
crystallization experiments
tetramer
Q8LPA6
4 * 110000, SDS-PAGE
tetramer
-
4 * 34000, SDS-PAGE
tetramer
Q05957
4 * 35000, SDS-PAGE
tetramer
-
4 * 48000, gel filtration
tetramer
-
gel filtration, ICL1, ICL2 and ICL
tetramer
-
-
tetramer
Euglena gracilis SM-ZK
-
4 * 110000, SDS-PAGE
-
tetramer
Pseudomonas fluorescens 13525
-
4 * 34000, SDS-PAGE
-
trimer
-
3 * 65000, SDS-PAGE
trimer
-
3 * 60000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
non-covalently bound carbohydrate
side-chain modification
-
2% neutral sugar
phosphoprotein
-, Q5YLB6
inactivation by phosphorylation
no modification
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
complexed with glyoxylate and a divalent cation
-
hanging drop vapor diffusion method
-
vapour diffusion with 0.1 M Tris-HCl, 0.2 M sodium acetate, 20-30% (w/v) PEG 4000, pH 8.0
P0A5H3
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7
Candida brassicae
-
stable
7.5
9
-
at 15C stable for 30 min
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
no loss of activity after 30 min
30
-
-
16% loss of activity after 30 min
30
-
-
enzyme is rapidly inactivated above, NaCl, 10% glycerol and 1 mM dithiothreitol protects
30
-
-
complete inactivation after 2 min
30
-
-
mutant Q207H, half time of thermal inactivation 58.4 s; mutant Q217K, half time of thermal inactivation 120.3 s; wild-type, half time of thermal inactivation 88.2 s
30
-
A8C5K8
the enzyme is rapidly inactivated at 30C
35
-
-
no enzyme activity
40
50
-
stable for 1 h
40
-
-
30% loss of activity after 30 min
40
-
-
stable at temperatures up to 40C, rapid decrease of activity at higher temperatures
40
-
P0A9G6
half time of thermal inactivation 161.8 s
50
-
-
completely inactivated after 5 min
50
-
-
completely inactive at temperatures above 50C
50
-
-
82% loss of activity after 30 min
50
-
-
heating to temperatures above caused loss of activity
50
-
-
low stability at temperatures above
50
-
-
5 mM ZnCl2, sigmoidal thermal denaturation curve, loss of 35% of helicity
51
-
-
native enzyme, apparent melting temperature (Tm), far-UV CD (222 nm), major part of enzyme resistant to thermal unfolding despite almost complete loss of activity above 50C, catalytic domain unfolded
55
-
-
50% activity lost after 4 h
55
-
-
2.5 mM MgCl2, first Tm of biphasic thermal denaturation curve (far-UV CD (222 nm)), loss of secondary structure similar to native enzyme, catalytic domain unfolded
55.5
-
-
50% activity lost after 43 min, in presence of 0.4 M KCl 50% activity lost after 129 min
56
-
-
1 mM MgCl2, first Tm of biphasic thermal denaturation curve (far-UV CD (222 nm)), loss of secondary structure similar to native enzyme, catalytic domain unfolded
60
-
-
50% activity lost after 3 min
60
-
-
50% activity lost after 5 min, in presence of 0.4 M KCl 50% activity lost after 4 min
60
-
-
100% loss of activity after 30 min
65
-
-
40% activity lost after 15 min
66
-
-
2.5 mM MgCl2, second Tm of biphasic thermal denaturation curve (far-UV CD (222 nm)), almost complete loss of secondary structure, noncatalytic alpha/beta barrel unfolded
90
-
-
1 mM MgCl2, second Tm of biphasic thermal denaturation curve (far-UV CD (222 nm)), almost complete loss of secondary structure, noncatalytic alpha/beta barrel unfolded
additional information
-
-
more heat labile at low concentrations
additional information
-
-
oxalate protects
additional information
-
-
biphasic kinetics of thermal inactivation
additional information
-
-
KCl, MgCl2, CaCl2 stabilize
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
most isocitrases very unstable, bacterial enzyme more stable than plant enzyme
-
unstable, loses its activity within a couple of hours on ice, AceA enzyme
-
extremely unstable in absence of Mg2+ or EDTA, glycerol or sucrose could not stabilize
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
reducing agent necessary for maintenance of enzyme activity
Lupinus sp.
-
33131
dithiothreitol very effective in protecting enzyme from loss of activity
-
33124
H2O2 inactivates isocitrate lyase and degrades its product glyoxylate. Gel filtration, cross-linking and co-immunoprecipitation studies indicate association of isocitrate lyase with catalase, this would afford protection from H2O2.
-
663767
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, at least 3 months, stable
-
-35C, more than 80% of the activity remains after more than 1 year
-
-20C, several weeks, stable
-
-20C, at least 6 months, stable
-
-12C, 20% glycerol, 21 days, 20% loss of activity
-
-12C, 20% glycerol, 7 days, 20% loss of activity
-
-12C, without glycerol, 4 h, 100% loss of activity
-
-20C, Tris-HCl-buffer, pH 7.5, 50% loss of activity after 3 days, 100% loss of activity after 6 days
-
-70C, Tris-HCl-buffer, pH 7.5, 5% loss of activity after 1 day, 10% loss of activity for each following day
-
-70C, Tris-HCl-buffer, pH 7.5, 80% activity by the tenth day of storage in the presence of 5 mM Mg2+ and 25% of activity when 5 mM Mn2+ are used for stabilization, the following storage conditions are optimal: low temperature (-70C), 25% glycerol in the medium and the presence of 5 mM MgCl2
-
-70C, Tris-HCl-buffer, pH 7.5, 85% activity by the tenth day of storage in the presence of 5 mM Mn2+ and 30% of activity when 5 mM Mg2+ are used for stabilization, the following storage conditions are optimal: low temperature (-70C), 25% glycerol in the medium and the presence of 5 mM MnCl2
-
4C, 20% glycerol, 7 days, 30% loss of activity
-
4C, without glycerol, 7 days, 50% loss of activity
-
room temperature, Tris-HCl-buffer, pH 7.5, 80% loss of activity in 24 hours
-
storage in glycerol-containing medium (25% glycerol) results in a 30% higher activity than storage in the absence of glycerol
-
-30C, 0.3 mM dithiothreitol, 12 days, 50% loss of activity
Lupinus sp.
-
-30C, 12 days, almost all activity lost
Lupinus sp.
-
-80C, stable for several months when frozen in liquid nitrogen and stored at -80C, Icl enzyme
-
4C, 50 mM NaH2PO4, 300 mM NaCl, 10 mM imidazole, pH 8.0, 2 months, no loss of activity
-
4C, after thawing and storage at 4C the loss of activity after 2 months is minimal in the presence of glycerol and a reducing agent, Icl enzyme
-
-80C, 6 months, stable
-
4C, 0.1 M Tris-HCl (pH 7.5), 3 mM 2-mercaptoethanol or 6 mM DTT, 5 mM MgCl2, 25% glycerol, 5 days, 10% loss of activity, 30 days, 75% loss of activity
-
removal of dithiothreitol during storage leads to spontaneous and slow inactivation
-
-20C, 4 weeks, 25-30% loss of activity
-
-20C, phosphate buffer, pH 6.0, 3 mM MgCl2, 10% glycerol, two months, 8% loss of activity
-
-20C, phosphate buffer, pH 6.0, 3 mM MgCl2, one week, 90% loss of activity
-
4C, phosphate buffer, pH 6.0, 3 mM MgCl2, one week, 50% loss of activity
-
-70C, concentrated to 2.4 mg/ml, 10 mM triethanolamine buffer, 12 mM MgCl2, 14 mM 2-mercaptoethanol, pH 7.6, 50% v/v glycerol, several months, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, phenyl-Sepharose column chromatography, and Resource Q column chromatography
-
thermophilic
-
-
Candida brassicae
-
to homogeneity, by Ni2+ affinity chromatography
-
from overproducing strain
-
anion exchange chromatography (DEAE), immobilized metal ion affinity chromatography (Ni2+), gel filtration
Q8LPA6
ammonium sulfate frationation, gel filtration, ion exchange chromatography (DEAE-cellulose)
-
-
Lupinus sp.
-
Ni-NTA column chromatography
-
HiTrap Q FF ion exchange column chromatography, Superdex S-200 gel filtration, and HiTrap Q HP ion exchange column chromatography
P0A5H3
Ni-Sepharose chromatography
-
recombinant protein from cell lysate by Ni-NTA metal-affinity chromatography (elution: 400 mM imidazole) and gel filtration on Superdex 200HR 10/300 column
-
immobilized metal ion affinity chromatography (Ni2+), tags removed
-, Q5YLB6
Macro-Prep High Q Support column chromatography
-, Q9I0K4
90% homogeneity
Q8RPZ0, -
copurified with aconitase
-
to homogeneity, purification of ICL1 is 123fold with a yield of 5.7%, purification degree and yield of ICL2 are 110 and 5.7%, respectively
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into vector pCR2.1-AfpyrG and overexpressed in the pyrA-strain AB4.1
-
pGSV3-lux ICL mutant
-
from genomic DNA
-
wild-type and mutants cloned by the pET-3c-HIS/Escherichia coli BL21 expression system
-
expression in Escherichia coli
-
expressed in Escherichia coli Top10 cells
A8C5K8
expresssion in Escherichia coli
Q05957
expression in Escherichia coli
P0A9G6
His-tagged version (without signal peptide (amino acid residue 1-12)) expressed in Escherichia coli BL21(DE3)
Q8LPA6
expression in Escherichia coli
-
expression in Saccharomyces cerevisiae
-
expressed in Escherichia coli strain BLR (DE3)
-
from genomic DNA into pQE30 for sequencing and subcloning into Escherichia coli-Mycobacterium shuttle plasmid pUV15(10) for expression in Mycobacterium smegmatis also after infection of and phagocytosis by mouse macrophage cell line RAW264.7, amplified sequence carried non-sense mutation at position 681 (C to G)
-
expressed in Escherichia coli BL21(DE3) cells
P0A5H3
expressed in Escherichia coli strain JM 109
-
from genomic DNA from strain H37Rv in pET21d for inducible expression in Escherichia coli C41
-
from genomic DNA into pQE30 for sequencing and subcloning into Escherichia coli-Mycobacterium shuttle plasmid pUV15(10) for expression as single protein of GFP fusion in Mycobacterium smegmatis also after infection of and phagocytosis by mouse macrophage cell line RAW264.7
-
Icl and AceA are different open reading frames, both with isocitrate lyase activity
-
ICL loss-of-function mutant strain DELTAicl complemented with the functional ICL gene using the integrative vector pMV306
P0A5H3
a thioredoxin/His-tagged version expressed in Escherichia coli BL21(DE3)
-, Q5YLB6
expressed in Escherichia coli
-, Q9I0K4
lacZ fusion expressed Pseudomonas aeruginosa
-
expressed in Escherichia coli
-
expressed in Escherichia coli
Q8RPZ0, -
expression in Escherichia coli
Q97YI8
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in bloodstream infection, ICL is downregulated in the initial stages of infection (10 min)
-
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
-
ICL in a rabbit meningitis model is upregulated after 7 days in the subarachnoid space
-
during infection, significant ICL gene expression in conidia, appressoria, mycelia and hyphae
-
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
-
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
-
expressed in macrophages
Penicillium marneffei
-
regulated by carbon sources
-
induced during growth on acetate but not on xylose
-
Ca2+, K+, and Na+ have little effect on the regulation of activity of ICL isoforms
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C165S
-
behaves as the wild-type
C165S/C247S
-
is inactivated by 5 mM GSSG and reactivated by treatment with either 20 mM reduced dithiothreitol or reduced glutaredoxin 1 as the wild-type protein. Complete shift in molecular mass corresponding to one glutathione adduct after 5 h of incubation, but prolonged incubation does not induce any additional glutathionylation
C165S/C247S/C301S
-
is inactivated by 5 mM GSSG and reactivated by treatment with either 20 mM reduced dithiothreitol or reduced glutaredoxin 1 as the wild-type protein. Complete shift in molecular mass corresponding to one glutathione adduct after 5 h of incubation, but prolonged incubation does not induce any additional glutathionylation
C178S
-
is totally inactive
C247S
-
behaves as the wild-type. Complete shift in molecular mass corresponding to one glutathione adduct after 5 h of incubation, but prolonged incubation does not induce any additional glutathionylation
C301S
-
behaves as the wild-type
Q207H
-
mutant with decreased activity between 10C and 25C
Q217K
-
mutant with decreased activity between 10C and 25C
A214S
A8C5K8
increased thermostability and low specific activity at low temperature
A231E
A8C5K8
more thermolabile than the wild type enzyme
A341N
A8C5K8
decreased activity compared to the wild type enzyme
F333L
A8C5K8
very low activity
Q47K
A8C5K8
activity similar to the wild type enzyme
A214S
Colwellia psychrerythraea NRC 1004
-
increased thermostability and low specific activity at low temperature
-
A231E
Colwellia psychrerythraea NRC 1004
-
more thermolabile than the wild type enzyme
-
A341N
Colwellia psychrerythraea NRC 1004
-
decreased activity compared to the wild type enzyme
-
F333L
Colwellia psychrerythraea NRC 1004
-
very low activity
-
Q47K
Colwellia psychrerythraea NRC 1004
-
activity similar to the wild type enzyme
-
C144A
Q05957
mutant with no enzyme activity
D79A
Q05957
mutant with 1000fold reduced turnover rate
A219C
-
similar catalytic properties as the wild-type enzyme
R187K
Q8LPA6
putative acetyl-CoA binding site of malate synthase, no malate synthase activity, but isocitrate lyase activity
C191A
P0A5H3
unable to form the closed conformation crystal form
C195A
P0A5H3
reduced activity
D475N
Q8LPA6
putative acetyl-CoA binding site of malate synthase, no malate synthase activity, but isocitrate lyase activity
additional information
Q8LPA6
truncated mutants: 13-573 (no isocitrate lyase activity, malate synthase activity), 566-1165 (no malate synthase activity), 20-573 (no isocitrate lyase activity, malate synthase activity), 38-573 (no isocitrate lyase activity), 20-1165 (isocitrate lyase activity and malate synthase activity), 38-1165
C195S
P0A5H3
reduced activity
additional information
-, Q9I0K4
transposition mutant PAO1SM::Himar1GmR is unable to grow on citronellol, n-octanol, leucine and acetate, and shows totally abolished ICL activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
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isocitrate lyase inhibitors can be developed for chronic infections but only for use in combination with effective antibiotics
drug development
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isocitrate lyase inhibitor design, substitution of a functional group at position C3 in 5-hydroxyindole-type alkaloids by hydrophilic group increases inhibitory activity
molecular biology
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cell growth in presence of high salt concentrations (1 M NaCl or KCl) leads to increase in enzyme activity consisting with higher levels of succinate and decreased levels of isocitrate
molecular biology
Debaryomyces hansenii Y7426
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cell growth in presence of high salt concentrations (1 M NaCl or KCl) leads to increase in enzyme activity consisting with higher levels of succinate and decreased levels of isocitrate
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medicine
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enzyme provides a potential target for drug design aimed at the control of parasitic infections
medicine
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overexpression of ICL from Mycobacterium smegmatis (MS-ICL) in Mycobacterium smegmatis (MS) does not suppress apoptosis induced in mouse macrophages upon infection by these recombinant bacteria (rMS-pMS-icl) compared to infection by control MS or MS overexpressing ICL from Mycobacterium tuberculosis
medicine
Mycobacterium smegmatis 1-2c
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overexpression of ICL from Mycobacterium smegmatis (MS-ICL) in Mycobacterium smegmatis (MS) does not suppress apoptosis induced in mouse macrophages upon infection by these recombinant bacteria (rMS-pMS-icl) compared to infection by control MS or MS overexpressing ICL from Mycobacterium tuberculosis
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medicine
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isocitrate lyase inhibitors as possible antituberculosis drugs
medicine
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overexpression of ICL from Mycobacterium tuberculosis (MTB-ICL) in Mycobacterium smegmatis (MS) suppresses apoptosis induced in mouse macrophages upon infection by these recombinant bacteria (rMS-pMTB-icl) compared to infection by control MS
medicine
Penicillium marneffei
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cytoplasm of macrophages possibly glucose-deficient, thus internalized Penicillium marneffei depends on glyoxylate pathway
medicine
Penicillium marneffei CBS 119456
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cytoplasm of macrophages possibly glucose-deficient, thus internalized Penicillium marneffei depends on glyoxylate pathway
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molecular biology
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glyoxylate shunt crucial for NADH/NADPH conversion cycle
additional information
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constitutive enzymic activity can be used to identify Yersinia pestis in humans, animals, water, soil and food