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Literature summary for 7.6.2.11 extracted from

  • Igarashi, K.; Kashiwagi, K.
    Polyamine transport in bacteria and yeast (1999), Biochem. J., 344, 633-642.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
PotF-putrescine complex Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information dissociation constant of spermidine and putrescine of the spermidine-preferential uptake system in presence of 1 mM Mg2+ and 100 mM K+ at pH 7.5 are 0.0032 mM and 0.1 mM Escherichia coli
0.385
-
ATP ATPase activity of PotA Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane PotB and PotC contain six putative transmembrane segments linked by hydrophobic segments of variable length Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus
-
-
-
Borreliella burgdorferi
-
-
-
Escherichia coli
-
-
-
Haemophilus influenzae
-
-
-
Mycoplasma genitalium
-
-
-
Mycoplasma pneumoniae
-
-
-
Treponema pallidum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
PotD protein Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229 Escherichia coli ?
-
?
additional information PotA protein is involved in the energy-coupling step Escherichia coli ?
-
?
putrescine/out + ATP + H2O two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system Escherichia coli putrescine/in + ADP + phosphate
-
?
spermidine/out + ADP + H2O the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP Escherichia coli spermidine/in + ?
-
?
spermidine/out + ATP + H2O two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system.The nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP Escherichia coli spermidine/in + ADP + phosphate
-
?
spermidine/out + CTP + H2O the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP Escherichia coli spermidine/in + CDP + phosphate
-
?
spermidine/out + GTP + H2O the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP Escherichia coli spermidine/in + GDP + phosphate
-
?
spermidine/out + UTP + H2O the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP Escherichia coli spermidine/in + UDP + phosphate
-
?
spermine/out + ATP + H2O two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system Escherichia coli spermine/in + ADP + phosphate
-
?

Subunits

Subunits Comment Organism
More the spermidine-preferential uptake system consists of 4 proteins, that are all necessary for spermidine uptake: PotA, PotB, PotC and PotD. The calculated molecular weights are 43000 Da for PotA, 31000 Da for PotB, 29000 Da for PotC and 39000 Da for PotD. The putrescine-uptake system consists of the 4 proteins: PotF, PotG, PotH and PotI. All 4 proteins are necessary for maximal putrescine transport. PotF is a 38000 Da putrescine binding protein, PotG is a 45000 Da membrane-associated ATPase, PotH and PotI are 31000-35000 Da channel-forming proteins Escherichia coli
More the enzyme is a ATP-binding cassette transporter Haemophilus influenzae
More the enzyme is a ATP-binding cassette transporter Mycoplasma genitalium
More the enzyme is a ATP-binding cassette transporter Escherichia coli
More the enzyme is a ATP-binding cassette transporter Archaeoglobus fulgidus
More the enzyme is a ATP-binding cassette transporter Mycoplasma pneumoniae
More the enzyme is a ATP-binding cassette transporter Treponema pallidum
More the enzyme is a ATP-binding cassette transporter Borreliella burgdorferi