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Literature summary 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

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.6.2.11 0.385
-
 ATP ATPase activity of PotA Escherichia coli

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.11 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.6.2.11 PotA protein Escherichia coli

Substrates and Products (Substrate)

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

Subunits

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