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Literature summary for 7.6.2.11 extracted from

  • Kashiwagi, K.; Endo, H.; Kobayashi, H.; Igarashi, K.
    Spermidine-preferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membranes (1995), J. Biol. Chem., 270, 25377-25382.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C26A no loss of ATPase activity Escherichia coli
C276A no loss of ATPase activity Escherichia coli
C54T mutated PotA protein loses both ATPase and spermidine uptake activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NEM inhibits ATPase activity of Pot A Escherichia coli
PCMB inhibits ATPase activity of Pot A Escherichia coli
spermidine inhibits ATPase activity of Pot A Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.385
-
ATP ATPase activity of PotA Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ ATPase activity of PotA is dependent on Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
PotA protein Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
spermidine/out + ATP + H2O
-
Escherichia coli spermidine/in + ADP + phosphate
-
?

Subunits

Subunits Comment Organism
More the enzyme is a ATP-binding cassette transporter Escherichia coli