Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.11 extracted from

  • Das, S.; Shevade, S.; LaCount, D.J.; Jarori, G.K.
    Plasmodium falciparum enolase complements yeast enolase functions and associates with the parasite food vacuole (2011), Mol. Biochem. Parasitol., 179, 8-17.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.11

Cloned(Commentary)

Cloned (Comment) Organism
ability of Pfeno to complement a mutant Saccharomyces cervisiae strain R11258 deficient in enolase activity. In this strain Tetr-Eno2, the enolase 1 gene is deleted and expression of the enolase 2 gene is under the control of a tetracycline repressible promoter. Pfeno is able to restore all three phenotypic effects fully or partially, i.e. growth retardation, vacuolar fragmentation and altered expression of certain vacuolar proteins, overview Plasmodium falciparum

Localization

Localization Comment Organism GeneOntology No. Textmining
cell membrane
-
 Plasmodium falciparum
-
-
cytoskeleton
-
 Plasmodium falciparum 5856
-
cytosol
-
 Plasmodium falciparum 5829
-
food vacuole association of enolase with the food vacuole Plasmodium falciparum 20020
-
nucleus
-
 Plasmodium falciparum 5634
-

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme partially by preparation of food vacuoles Plasmodium falciparum

Subunits

Subunits Comment Organism
dimer the dimeric structure of Pfeno is required for the optimal vacuolar functions Plasmodium falciparum

Synonyms

Synonyms Comment Organism
enolase
-
 Plasmodium falciparum
Pfeno
-
 Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Plasmodium falciparum