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Literature summary for 5.3.1.1 extracted from

  • Miranda-Ozuna, J.F.; Hernandez-Garcia, M.S.; Brieba, L.G.; Benitez-Cardoza, C.G.; Ortega-Lopez, J.; Gonzalez-Robles, A.; Arroyo, R.
    The glycolytic enzyme triosephosphate isomerase of Trichomonas vaginalis is a surface-associated protein induced by glucose that functions as a laminin- and fibronectin-binding protein (2016), Infect. Immun., 84, 2878-2894 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Trichomonas vaginalis 9986
-
cytoplasm
-
Trichomonas vaginalis 5737
-

Organism

Organism UniProt Comment Textmining
Trichomonas vaginalis A2EGX9
-
-
Trichomonas vaginalis A2FT29
-
-

Synonyms

Synonyms Comment Organism
TIM1
-
Trichomonas vaginalis
TIM2
-
Trichomonas vaginalis

Expression

Organism Comment Expression
Trichomonas vaginalis overexpression under glucose-restricted conditions up
Trichomonas vaginalis overexpression under glucose-rich conditions up

General Information

General Information Comment Organism
physiological function recombinant protein binds to laminin and fibronectin but not to plasminogen. Higher levels of adherence are detected in parasites grown under high-glucose conditions than in those grown under glucose-restricted conditions, and anti-TIM antibody inhibits the binding of Trichomonas vaginalis to laminin and fibronectin Trichomonas vaginalis