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Literature summary for 1.11.1.24 extracted from

  • Zhang, H.; Wang, Z.; Huang, J.; Cao, J.; Zhou, Y.; Zhou, J.
    A novel thioredoxin-dependent peroxiredoxin (TPx-Q) plays an important role in defense against oxidative stress and is a possible drug target in Babesia microti (2020), Front. Vet. Sci., 7, 76 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.24

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Babesia microti

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Babesia microti 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22300
-
 calculated from sequence Babesia microti

Organism

Organism UniProt Comment Textmining
Babesia microti
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Babesia microti

Source Tissue

Source Tissue Comment Organism Textmining
merozoite
-
 Babesia microti
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2 + ferrithiocyanate
-
 Babesia microti H2O + ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 22300, calculated from sequence Babesia microti

Synonyms

Synonyms Comment Organism
BmTPx-Q
-
 Babesia microti

pI Value

Organism Comment pI Value Maximum pI Value
Babesia microti calculated from sequence
-
 9.18

Expression

Organism Comment Expression
Babesia microti when incubated with chloroquine diphosphate salt for 24 h in vitro, the expression of BmTPx-Q shows a marked downward trend with the increase of drug concentration down

General Information

General Information Comment Organism
drug target the enzyme is a possible drug target for the development of strategies to control Babesia microti infection Babesia microti
physiological function the enzyme plays an important role in defense against oxidative stress Babesia microti