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Literature summary extracted from

  • Avilan, L.; Gualdron-Lopez, M.; Quinones, W.; Gonzalez-Gonzalez, L.; Hannaert, V.; Michels, P.A.; Concepcion, J.L.
    Enolase: a key player in the metabolism and a probable virulence factor of trypanosomatid parasites-perspectives for its use as a therapeutic target (2011), Enzyme Res., 2011, 932549.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
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 Trypanosoma brucei
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 Streptococcus pyogenes
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 Trypanosoma cruzi
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 Aeromonas hydrophila
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 japonicum
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 Eimeria tenella
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 infantum
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 Leishmania braziliensis
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 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 Leishmania chagasi
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 Echinostoma caproni

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
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 Trichomonas vaginalis 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 Leishmania donovani 9986
-
4.2.1.11 cell surface associated to the external surface of the parasite Trypanosoma cruzi 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 Leishmania mexicana 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 Leishmania major 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 Fasciola hepatica 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 Lactobacillus crispatus 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 Leishmania chagasi 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 Echinostoma caproni 9986
-
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 secreted enzyme associated to the external surface of the parasite Plasmodium falciparum 9986
-
4.2.1.11 cytosol
-
 Leishmania mexicana 5829
-
4.2.1.11 extracellular secreted enzyme Giardia intestinalis
-
-
4.2.1.11 extracellular secreted enzyme Trichomonas vaginalis
-
-
4.2.1.11 extracellular secreted enzyme Streptococcus pyogenes
-
-
4.2.1.11 extracellular secreted enzyme Leishmania donovani
-
-
4.2.1.11 extracellular secreted enzyme Trypanosoma cruzi
-
-
4.2.1.11 extracellular secreted enzyme Schistosoma japonicum
-
-
4.2.1.11 extracellular secreted enzyme Leishmania mexicana
-
-
4.2.1.11 extracellular secreted enzyme Eimeria tenella
-
-
4.2.1.11 extracellular secreted enzyme Leishmania major
-
-
4.2.1.11 extracellular secreted enzyme Fasciola hepatica
-
-
4.2.1.11 extracellular secreted enzyme Leishmania braziliensis
-
-
4.2.1.11 extracellular secreted enzyme Lactobacillus crispatus
-
-
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 Schistosoma bovis
-
-
4.2.1.11 extracellular secreted enzyme Echinostoma caproni
-
-
4.2.1.11 extracellular secreted enzyme associated to the external surface of the parasite Candida albicans
-
-
4.2.1.11 extracellular secreted enzyme associated to the external surface of the parasite Plasmodium falciparum
-
-
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 Streptococcus pyogenes
-
-
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 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 Leishmania braziliensis
-
-
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 Streptomyces mutans
-
-
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 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 major
-
-
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 chagasi
-
-
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 plasma membrane
-
 Leishmania mexicana 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 enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization Leishmania chagasi 5886
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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 Comment Organism Textmining
4.2.1.11 amastigote
-
 Trichomonas vaginalis
-
4.2.1.11 amastigote
-
 Leishmania donovani
-
4.2.1.11 amastigote
-
 Trypanosoma cruzi
-
4.2.1.11 amastigote
-
 Schistosoma japonicum
-
4.2.1.11 amastigote
-
 Leishmania mexicana
-
4.2.1.11 amastigote
-
 Leishmania major
-
4.2.1.11 amastigote
-
 Schistosoma bovis
-
4.2.1.11 promastigote
-
 Trichomonas vaginalis
-
4.2.1.11 promastigote
-
 Trypanosoma cruzi
-
4.2.1.11 promastigote
-
 Schistosoma japonicum
-
4.2.1.11 promastigote
-
 Leishmania mexicana
-
4.2.1.11 promastigote
-
 Schistosoma bovis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms

EC Number Synonyms Comment Organism
4.2.1.11 enolase
-
 Giardia intestinalis
4.2.1.11 enolase
-
 Trypanosoma brucei
4.2.1.11 enolase
-
 Trichomonas vaginalis
4.2.1.11 enolase
-
 Streptococcus pyogenes
4.2.1.11 enolase
-
 Leishmania donovani
4.2.1.11 enolase
-
 Trypanosoma cruzi
4.2.1.11 enolase
-
 Candida albicans
4.2.1.11 enolase
-
 Aeromonas hydrophila
4.2.1.11 enolase
-
 Plasmodium falciparum
4.2.1.11 enolase
-
 Schistosoma japonicum
4.2.1.11 enolase
-
 Leishmania mexicana
4.2.1.11 enolase
-
 Eimeria tenella
4.2.1.11 enolase
-
 Leishmania major
4.2.1.11 enolase
-
 Leishmania infantum
4.2.1.11 enolase
-
 Fasciola hepatica
4.2.1.11 enolase
-
 Leishmania braziliensis
4.2.1.11 enolase
-
 Lactobacillus crispatus
4.2.1.11 enolase
-
 Streptomyces mutans
4.2.1.11 enolase
-
 Streptomyces pneumoniae
4.2.1.11 enolase
-
 Leishmania chagasi
4.2.1.11 enolase
-
 Schistosoma bovis
4.2.1.11 enolase
-
 Echinostoma caproni

General Information

EC Number General Information Comment 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 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 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 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 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 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 Trypanosoma cruzi
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 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 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 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 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 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 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 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 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 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 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 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 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 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 Echinostoma caproni
4.2.1.11 physiological function enolase can act as a plasminogen-binding protein Candida albicans
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, FYDAEKKEY, is responsible for the plasminogen recognition Aeromonas hydrophila
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
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 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 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 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. Enolase can act as a plasminogen-binding protein, an internal motif, AYDAERKMY, is responsible for the plasminogen recognition Leishmania mexicana