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Literature summary for 3.1.3.2 extracted from

  • Schell, D.; Stierhof, Y.D.; Overath, P.
    Purification and characterization of a tartrate-sensitive acid phosphatase of Trypanosoma brucei (1990), FEBS Lett., 271, 67-70.
    View publication on PubMed
Search for more literature for 3.1.3.2

Inhibitors

Inhibitors Comment Organism Structure
Tartrate one membrane-bound enzyme is sensitive the other is resistant Trypanosoma brucei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 p-nitrophenyl phosphate tartrate-sensitive enzyme Trypanosoma brucei

Localization

Localization Comment Organism GeneOntology No. Textmining
flagellar pocket
-
 Trypanosoma brucei
-
-
membrane at least 2 membrane-bound enzymes Trypanosoma brucei 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 x * 70000, tartrate-sensitive enzyme, SDS-PAGE Trypanosoma brucei

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Trypanosoma brucei

Purification (Commentary)

Purification (Comment) Organism
-
 Trypanosoma brucei

Source Tissue

Source Tissue Comment Organism Textmining
bloodstream form
-
 Trypanosoma brucei
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
43.4
-
 tartrate-sensitive enzyme Trypanosoma brucei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl phosphate + H2O
-
 Trypanosoma brucei p-nitrophenol + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 70000, tartrate-sensitive enzyme, SDS-PAGE Trypanosoma brucei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 tartrate-sensitive enzyme Trypanosoma brucei