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Literature summary for 7.4.2.6 extracted from

  • Hopfe, M.; Henrich, B.
    OppA, the substrate-binding subunit of the oligopeptide permease, is the major Ecto-ATPase of Mycoplasma hominis (2004), J. Bacteriol., 186, 1021-1928.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K875R Oppa, decrease in ATPhydrolysis to 15% of wild-tpe Mycoplasma hominis
additional information OppA, exchange of P-loop motif GKDSSGKS to THASSSAH, no ATP-binding observed, decrease in ATP hydrolysis to 6% of wild-type Mycoplasma hominis

Inhibitors

Inhibitors Comment Organism Structure
4',4'-diisothiocyanostylbene-2',2'-disulfonic acid 0.5 mM, about 25% residual activity Mycoplasma hominis
5'-fluorosulfonyl-benzoyladenosine 1 mM, about 25% residual activity Mycoplasma hominis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
ATP pH 7.5, 37°C Mycoplasma hominis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface substrate binding protein OppA of the permease complex Mycoplasma hominis 9986
-

Organism

Organism UniProt Comment Textmining
Mycoplasma hominis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + oligopeptide/out
-
Mycoplasma hominis ADP + phosphate + oligopeptide/in
-
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