BRENDA - Enzyme Database

Enolase: a key player in the metabolism and a probable virulence factor of trypanosomatid parasites-perspectives for its use as a therapeutic target

Avilan, L.; Gualdron-Lopez, M.; Quinones, W.; Gonzalez-Gonzalez, L.; Hannaert, V.; Michels, P.A.; Concepcion, J.L.; Enzyme Res. 2011, 932549 (2011)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Aeromonas hydrophila
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Candida albicans
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Echinostoma caproni
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Eimeria tenella
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Fasciola hepatica
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Giardia intestinalis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Lactobacillus crispatus
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania braziliensis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania chagasi
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania donovani
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania infantum
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania major
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania mexicana
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Plasmodium falciparum
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Schistosoma bovis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Schistosoma japonicum
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Streptococcus pyogenes
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Streptomyces mutans
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Streptomyces pneumoniae
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Trichomonas vaginalis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Trypanosoma brucei
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Trypanosoma cruzi
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.2.1.11
cell surface
secreted enzyme associated to the external surface of the parasite
Candida albicans
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Echinostoma caproni
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Eimeria tenella
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Fasciola hepatica
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Giardia intestinalis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Lactobacillus crispatus
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania braziliensis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania chagasi
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania donovani
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania infantum
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania major
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania mexicana
9986
-
4.2.1.11
cell surface
secreted enzyme associated to the external surface of the parasite
Plasmodium falciparum
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Schistosoma bovis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Schistosoma japonicum
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Streptococcus pyogenes
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Streptomyces mutans
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Streptomyces pneumoniae
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Trichomonas vaginalis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Trypanosoma cruzi
9986
-
4.2.1.11
cytosol
-
Leishmania mexicana
5829
-
4.2.1.11
extracellular
secreted enzyme associated to the external surface of the parasite
Candida albicans
-
-
4.2.1.11
extracellular
secreted enzyme
Echinostoma caproni
-
-
4.2.1.11
extracellular
secreted enzyme
Eimeria tenella
-
-
4.2.1.11
extracellular
secreted enzyme
Fasciola hepatica
-
-
4.2.1.11
extracellular
secreted enzyme
Giardia intestinalis
-
-
4.2.1.11
extracellular
secreted enzyme
Lactobacillus crispatus
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania braziliensis
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania donovani
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania major
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania mexicana
-
-
4.2.1.11
extracellular
secreted enzyme associated to the external surface of the parasite
Plasmodium falciparum
-
-
4.2.1.11
extracellular
secreted enzyme
Schistosoma bovis
-
-
4.2.1.11
extracellular
secreted enzyme
Schistosoma japonicum
-
-
4.2.1.11
extracellular
secreted enzyme
Streptococcus pyogenes
-
-
4.2.1.11
extracellular
secreted enzyme
Streptomyces mutans
-
-
4.2.1.11
extracellular
secreted enzyme
Streptomyces pneumoniae
-
-
4.2.1.11
extracellular
secreted enzyme
Trichomonas vaginalis
-
-
4.2.1.11
extracellular
secreted enzyme
Trypanosoma cruzi
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Echinostoma caproni
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Eimeria tenella
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Fasciola hepatica
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Giardia intestinalis
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Lactobacillus crispatus
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Leishmania braziliensis
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania chagasi
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania donovani
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania infantum
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania major
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp., no activity in microsomes. Enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
Leishmania mexicana
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Schistosoma japonicum
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Streptococcus pyogenes
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Streptomyces mutans
-
-
4.2.1.11
plasma membrane
enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
Leishmania chagasi
5886
-
4.2.1.11
plasma membrane
enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
Leishmania infantum
5886
-
4.2.1.11
plasma membrane
-
Leishmania mexicana
5886
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Giardia intestinalis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Trypanosoma brucei
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Trichomonas vaginalis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Streptococcus pyogenes
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania donovani
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Trypanosoma cruzi
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Candida albicans
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Aeromonas hydrophila
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Plasmodium falciparum
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Schistosoma japonicum
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania mexicana
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Eimeria tenella
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania major
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania infantum
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Fasciola hepatica
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania braziliensis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Lactobacillus crispatus
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Streptomyces mutans
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Streptomyces pneumoniae
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania chagasi
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Schistosoma bovis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Echinostoma caproni
-
phosphoenolpyruvate + H2O
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Aeromonas hydrophila
-
-
-
4.2.1.11
Candida albicans
-
-
-
4.2.1.11
Echinostoma caproni
-
-
-
4.2.1.11
Eimeria tenella
-
-
-
4.2.1.11
Fasciola hepatica
-
-
-
4.2.1.11
Giardia intestinalis
-
-
-
4.2.1.11
Lactobacillus crispatus
-
-
-
4.2.1.11
Leishmania braziliensis
-
-
-
4.2.1.11
Leishmania chagasi
-
-
-
4.2.1.11
Leishmania donovani
-
-
-
4.2.1.11
Leishmania infantum
-
-
-
4.2.1.11
Leishmania major
-
-
-
4.2.1.11
Leishmania mexicana
-
-
-
4.2.1.11
Plasmodium falciparum
-
-
-
4.2.1.11
Schistosoma bovis
-
-
-
4.2.1.11
Schistosoma japonicum
-
-
-
4.2.1.11
Streptococcus pyogenes
-
-
-
4.2.1.11
Streptomyces mutans
-
-
-
4.2.1.11
Streptomyces pneumoniae
-
-
-
4.2.1.11
Trichomonas vaginalis
-
-
-
4.2.1.11
Trypanosoma brucei
-
-
-
4.2.1.11
Trypanosoma cruzi
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
4.2.1.11
amastigote
-
Leishmania donovani
-
4.2.1.11
amastigote
-
Leishmania major
-
4.2.1.11
amastigote
-
Leishmania mexicana
-
4.2.1.11
amastigote
-
Schistosoma bovis
-
4.2.1.11
amastigote
-
Schistosoma japonicum
-
4.2.1.11
amastigote
-
Trichomonas vaginalis
-
4.2.1.11
amastigote
-
Trypanosoma cruzi
-
4.2.1.11
promastigote
-
Leishmania mexicana
-
4.2.1.11
promastigote
-
Schistosoma bovis
-
4.2.1.11
promastigote
-
Schistosoma japonicum
-
4.2.1.11
promastigote
-
Trichomonas vaginalis
-
4.2.1.11
promastigote
-
Trypanosoma cruzi
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
714875
Giardia intestinalis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Trypanosoma brucei
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Trichomonas vaginalis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Streptococcus pyogenes
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania donovani
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Trypanosoma cruzi
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Candida albicans
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Aeromonas hydrophila
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Plasmodium falciparum
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Schistosoma japonicum
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania mexicana
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Eimeria tenella
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania major
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania infantum
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Fasciola hepatica
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania braziliensis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Lactobacillus crispatus
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Streptomyces mutans
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Streptomyces pneumoniae
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania chagasi
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Schistosoma bovis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Echinostoma caproni
phosphoenolpyruvate + H2O
-
-
-
r
Application (protein specific)
EC Number
Application
Commentary
Organism
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Aeromonas hydrophila
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Candida albicans
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Echinostoma caproni
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Eimeria tenella
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Fasciola hepatica
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Giardia intestinalis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Lactobacillus crispatus
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania braziliensis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania chagasi
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania donovani
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania infantum
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania major
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Leishmania mexicana
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Plasmodium falciparum
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Schistosoma bovis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Schistosoma japonicum
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Streptococcus pyogenes
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Streptomyces mutans
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Streptomyces pneumoniae
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Trichomonas vaginalis
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Trypanosoma brucei
4.2.1.11
drug development
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
Trypanosoma cruzi
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.2.1.11
cell surface
secreted enzyme associated to the external surface of the parasite
Candida albicans
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Echinostoma caproni
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Eimeria tenella
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Fasciola hepatica
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Giardia intestinalis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Lactobacillus crispatus
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania braziliensis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania chagasi
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania donovani
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania infantum
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania major
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Leishmania mexicana
9986
-
4.2.1.11
cell surface
secreted enzyme associated to the external surface of the parasite
Plasmodium falciparum
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Schistosoma bovis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Schistosoma japonicum
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Streptococcus pyogenes
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Streptomyces mutans
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Streptomyces pneumoniae
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Trichomonas vaginalis
9986
-
4.2.1.11
cell surface
associated to the external surface of the parasite
Trypanosoma cruzi
9986
-
4.2.1.11
cytosol
-
Leishmania mexicana
5829
-
4.2.1.11
extracellular
secreted enzyme associated to the external surface of the parasite
Candida albicans
-
-
4.2.1.11
extracellular
secreted enzyme
Echinostoma caproni
-
-
4.2.1.11
extracellular
secreted enzyme
Eimeria tenella
-
-
4.2.1.11
extracellular
secreted enzyme
Fasciola hepatica
-
-
4.2.1.11
extracellular
secreted enzyme
Giardia intestinalis
-
-
4.2.1.11
extracellular
secreted enzyme
Lactobacillus crispatus
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania braziliensis
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania donovani
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania major
-
-
4.2.1.11
extracellular
secreted enzyme
Leishmania mexicana
-
-
4.2.1.11
extracellular
secreted enzyme associated to the external surface of the parasite
Plasmodium falciparum
-
-
4.2.1.11
extracellular
secreted enzyme
Schistosoma bovis
-
-
4.2.1.11
extracellular
secreted enzyme
Schistosoma japonicum
-
-
4.2.1.11
extracellular
secreted enzyme
Streptococcus pyogenes
-
-
4.2.1.11
extracellular
secreted enzyme
Streptomyces mutans
-
-
4.2.1.11
extracellular
secreted enzyme
Streptomyces pneumoniae
-
-
4.2.1.11
extracellular
secreted enzyme
Trichomonas vaginalis
-
-
4.2.1.11
extracellular
secreted enzyme
Trypanosoma cruzi
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Echinostoma caproni
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Eimeria tenella
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Fasciola hepatica
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Giardia intestinalis
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Lactobacillus crispatus
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Leishmania braziliensis
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania chagasi
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania donovani
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania infantum
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp.
Leishmania major
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface of Leishmania spp., no activity in microsomes. Enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
Leishmania mexicana
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Schistosoma japonicum
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Streptococcus pyogenes
-
-
4.2.1.11
additional information
enolase is found both in the secretome and in association with the surface
Streptomyces mutans
-
-
4.2.1.11
plasma membrane
enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
Leishmania chagasi
5886
-
4.2.1.11
plasma membrane
enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
Leishmania infantum
5886
-
4.2.1.11
plasma membrane
-
Leishmania mexicana
5886
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Giardia intestinalis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Trypanosoma brucei
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Trichomonas vaginalis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Streptococcus pyogenes
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania donovani
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Trypanosoma cruzi
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Candida albicans
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Aeromonas hydrophila
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Plasmodium falciparum
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Schistosoma japonicum
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania mexicana
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Eimeria tenella
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania major
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania infantum
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Fasciola hepatica
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania braziliensis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Lactobacillus crispatus
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Streptomyces mutans
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Streptomyces pneumoniae
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Leishmania chagasi
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Schistosoma bovis
-
phosphoenolpyruvate + H2O
-
-
r
4.2.1.11
2-phospho-D-glycerate
Echinostoma caproni
-
phosphoenolpyruvate + H2O
-
-
r
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
4.2.1.11
amastigote
-
Leishmania donovani
-
4.2.1.11
amastigote
-
Leishmania major
-
4.2.1.11
amastigote
-
Leishmania mexicana
-
4.2.1.11
amastigote
-
Schistosoma bovis
-
4.2.1.11
amastigote
-
Schistosoma japonicum
-
4.2.1.11
amastigote
-
Trichomonas vaginalis
-
4.2.1.11
amastigote
-
Trypanosoma cruzi
-
4.2.1.11
promastigote
-
Leishmania mexicana
-
4.2.1.11
promastigote
-
Schistosoma bovis
-
4.2.1.11
promastigote
-
Schistosoma japonicum
-
4.2.1.11
promastigote
-
Trichomonas vaginalis
-
4.2.1.11
promastigote
-
Trypanosoma cruzi
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
714875
Giardia intestinalis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Trypanosoma brucei
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Trichomonas vaginalis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Streptococcus pyogenes
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania donovani
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Trypanosoma cruzi
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Candida albicans
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Aeromonas hydrophila
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Plasmodium falciparum
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Schistosoma japonicum
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania mexicana
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Eimeria tenella
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania major
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania infantum
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Fasciola hepatica
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania braziliensis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Lactobacillus crispatus
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Streptomyces mutans
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Streptomyces pneumoniae
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Leishmania chagasi
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Schistosoma bovis
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
-
714875
Echinostoma caproni
phosphoenolpyruvate + H2O
-
-
-
r
General Information
EC Number
General Information
Commentary
Organism
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Aeromonas hydrophila
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Candida albicans
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Echinostoma caproni
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Eimeria tenella
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Fasciola hepatica
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Giardia intestinalis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Lactobacillus crispatus
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania braziliensis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania chagasi
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania donovani
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania infantum
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania major
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania mexicana
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Plasmodium falciparum
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Schistosoma bovis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Schistosoma japonicum
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Streptococcus pyogenes
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Streptomyces mutans
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Streptomyces pneumoniae
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Trichomonas vaginalis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Trypanosoma brucei
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Trypanosoma cruzi
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein, an internal motif, FYDAEKKEY, is responsible for the plasminogen recognition
Aeromonas hydrophila
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein
Candida albicans
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania chagasi
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania donovani
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania infantum
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania major
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids. Enolase can act as a plasminogen-binding protein, an internal motif, AYDAERKMY, is responsible for the plasminogen recognition
Leishmania mexicana
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein
Plasmodium falciparum
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein
Schistosoma bovis
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein, an internal motif, FYDKERKVYD, is responsible for the plasminogen recognition
Streptomyces pneumoniae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Aeromonas hydrophila
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Candida albicans
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Echinostoma caproni
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Eimeria tenella
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Fasciola hepatica
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Giardia intestinalis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Lactobacillus crispatus
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania braziliensis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania chagasi
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania donovani
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania infantum
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania major
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Leishmania mexicana
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Plasmodium falciparum
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Schistosoma bovis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Schistosoma japonicum
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Streptococcus pyogenes
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Streptomyces mutans
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Streptomyces pneumoniae
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Trichomonas vaginalis
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Trypanosoma brucei
4.2.1.11
metabolism
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
Trypanosoma cruzi
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein, an internal motif, FYDAEKKEY, is responsible for the plasminogen recognition
Aeromonas hydrophila
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein
Candida albicans
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania chagasi
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania donovani
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania infantum
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
Leishmania major
4.2.1.11
physiological function
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids. Enolase can act as a plasminogen-binding protein, an internal motif, AYDAERKMY, is responsible for the plasminogen recognition
Leishmania mexicana
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein
Plasmodium falciparum
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein
Schistosoma bovis
4.2.1.11
physiological function
enolase can act as a plasminogen-binding protein, an internal motif, FYDKERKVYD, is responsible for the plasminogen recognition
Streptomyces pneumoniae