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Information on EC 4.1.3.1 - isocitrate lyase and Organism(s) Escherichia coli and UniProt Accession P0A9G6

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.1 isocitrate lyase
IUBMB Comments
The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate .
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This record set is specific for:
Escherichia coli
UNIPROT: P0A9G6
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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isocitrate
=
succinate
+
glyoxylate
=
+
Synonyms
icl, isocitrate lyase, citrate lyase, mtbicl, eggce, isocitritase, isocitratase, isocitric lyase, fpicl1, petal death protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isocitrase
-
-
-
-
isocitratase
-
-
-
-
isocitrate lyase
-
-
isocitric lyase
-
-
-
-
isocitritase
-
-
-
-
lyase, isocitrate
-
-
-
-
threo-DS-Isocitrate glyoxylate-lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
isocitrate glyoxylate-lyase (succinate-forming)
The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9045-78-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
isocitrate
glyoxylate + succinate
show the reaction diagram
-
-
-
?
(2R,3S)-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
DL-isocitrate
succinate + glyoxylate
show the reaction diagram
-
-
-
-
?
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
?
isocitrate
succinate + glyoxylate
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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
isocitrate
?
show the reaction diagram
-
glyoxylate cycle
-
-
?
isocitrate
succinate + glyoxylate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
no activity in absence of exogenous cation, Mg2+ most effective
Ni2+
-
no activity in absence of exogenous cation, Ni2+ 7% as effective as Mg2+
Sr2+
-
no activity in absence of exogenous cation, Sr2+ 3% as effective as Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
-
3-Bromopyruvate
-
-
3-nitropropionate
-
50% inhibition at 0.04 mM
3-phosphoglycerate
-
-
Dithionitrobenzoate
-
-
glycolate
glyoxylate
-
linear competitive inhibitor
HgCl2
-
100% inhibition at 0.01 mM
Hydroxymalonate
-
50% inhibition at 0.5 mM
malonate
-
-
methylmalonate
-
50% inhibition at 15 mM
oxalate
-
-
phosphate
-
-
phosphoenolpyruvate
succinate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 0.65
isocitrate
0.015 - 0.096
DL-isocitrate
0.018 - 0.062
Ds-isocitrate
0.13
glyoxylate
-
-
0.59
succinate
-
-
0.008
threo-Ds-isocitrate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
3-nitropropionate
-
-
0.5
Hydroxymalonate
-
-
15
methylmalonate
-
-
0.893
phosphoenolpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.1), 10 mM MgCl2, 12 mM cysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
0.022
-
strain BW3709, 0.2% glucose (batch)
0.023
-
strain BW3767, 0.2% glucose (batch)
0.034
-
strain BW2952, 0.2% glucose (batch)
0.088
-
strain BW3480, 0.02% glucose (chemostat)
0.155
-
strain MG1655, 0.2% glucose (batch)
0.19
-
strain BW3708, 0.2% glucose (batch)
0.248
-
strain BW2952, 0.02% glucose (chemostat)
0.471
-
strain BW3767, 0.02% glucose (chemostat)
0.538
-
strain BW3709, 0.02% glucose (chemostat)
1.066
-
strain BW2952, 0.2% acetate (batch)
1.227
-
strain BW3767, 0.2% acetate (batch)
1.656
-
strain BW3709, 0.2% acetate (batch)
1.674
-
strain MG1655, 0.02% glucose (chemostat)
1.778
-
strain BW3708, 0.02% glucose (chemostat)
2.084
-
strain MG1655, 0.2% acetate (batch)
3.075
-
strain BW3708, 0.2% acetate (batch)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
177000
-
gel filtration
180000
-
sedimentation equilibrium centrifugation
188000
-
gel filtration
208000
-
gel filtration
44700
-
4 * 44700, SDS-PAGE
48000
-
4 * 48000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A219C
-
similar catalytic properties as the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
half time of thermal inactivation 161.8 s
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, at least 6 months, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robertson, E.F.; Reeves, H.C.
Purification and characterization of isocitrate lyase from Escherichia coli
Curr. Microbiol.
14
347-350
1987
Escherichia coli
-
Manually annotated by BRENDA team
Mackintosh, C.; Nimmo, H.G.
Purification and properties of Escherichia coli isocitrate lyase
Biochem. Soc. Trans.
14
320-321
1986
Escherichia coli
-
Manually annotated by BRENDA team
Hoyt, J.C.; Robertson, E.F.; Berlyn, K.A.; Reeves, H.C.
Escherichia coli isocitrate lyase: properties and comparisons
Biochim. Biophys. Acta
966
30-35
1988
Escherichia coli
Manually annotated by BRENDA team
Mackintosh, C.; Nimmo, H.G.
Purification and regulatory properties of isocitrate lyase from Escherichia coli ML308
Biochem. J.
250
25-31
1988
Escherichia coli
Manually annotated by BRENDA team
Zarembinski, C.M.; Hoyt, J.C.; Reeves, H.C.
Properties of isocitrate lyase from Escherichia coli K12 grown on acetate or glycolate
Curr. Microbiol.
22
65-68
1991
Escherichia coli
-
Manually annotated by BRENDA team
Ko, Y.H.; McFadden, B.A.
The inhibition of isocitrate lyase from Escherichia coli by glyoxylate
Curr. Microbiol.
21
313-315
1990
Escherichia coli
-
Manually annotated by BRENDA team
Britton, K.L.; Abeysinghe, I.S.B.; Baker, P.J.; Barynin, V.; Diehl, P.; Langridge, S.J.; McFadden, B.A.; Sedelnikova, S.E.; Stillman, T.J.; Weeradechapon, K.; Rice, D.W.
The structure and domain organization of Escherichia coli isocitrate lyase
Acta Crystallogr. Sect. D
D57
1209-1218
2001
Escherichia coli
Manually annotated by BRENDA team
Watanabe, S.; Takada, Y.
Amino acid residues involved in cold adaptation of isocitrate lyase from a psychrophilic bacterium, Colwellia maris
Microbiology
150
3393-3403
2004
Colwellia maris, Escherichia coli (P0A9G6), Escherichia coli
Manually annotated by BRENDA team
Prasad Maharjan, R.; Yu, P.L.; Seeto, S.; Ferenci, T.
The role of isocitrate lyase and the glyoxylate cycle in Escherichia coli growing under glucose limitation
Res. Microbiol.
156
178-183
2005
Escherichia coli
Manually annotated by BRENDA team
Ogawa, T.; Murakami, K.; Mori, H.; Ishii, N.; Tomita, M.; Yoshin, M.
Role of phosphoenolpyruvate in the NADP-isocitrate dehydrogenase and isocitrate lyase reaction in Escherichia coli
J. Bacteriol.
189
1176-1178
2007
Escherichia coli, Escherichia coli K-12 W3110
Manually annotated by BRENDA team
Dunn, M.F.; Ramirez-Trujillo, J.A.; Hernandez-Lucas, I.
Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis
Microbiology
155
3166-3175
2009
Aspergillus fumigatus, Aspergillus nidulans, Candida albicans, Colletotrichum lagenaria, Rhodococcus equi, Cryptococcus neoformans, Escherichia coli, Leptosphaeria maculans, Pyricularia grisea, Mycobacterium tuberculosis, Mycobacterium avium, Yersinia pestis, Yersinia pseudotuberculosis, Pseudomonas aeruginosa, Sinorhizobium meliloti, Rhizobium tropici, Salmonella enterica subsp. enterica serovar Typhimurium, Yersinia enterocolitica, Paracoccidioides brasiliensis, Brucella suis, Talaromyces marneffei
Manually annotated by BRENDA team
Lee, Y.V.; Wahab, H.A.; Choong, Y.S.
Potential inhibitors for isocitrate lyase of Mycobacterium tuberculosis and non-M. tuberculosis a summary
BioMed Res. Int.
2015
895453
2015
Acinetobacter calcoaceticus, Ricinus communis, Escherichia coli, Pyricularia grisea, Mycobacterium tuberculosis, Neurospora crassa, Vogesella indigofera, Candida albicans (Q9P8Q7)
Manually annotated by BRENDA team