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Literature summary for 7.2.2.7 extracted from

  • Anderson, D.S.; Adhikari, P.; Nowalk, A.J.; Chen, C.Y.; Mietzner, T.A.
    The hFbpABC transporter from Haemophilus influenzae functions as a binding-protein-dependent ABC transporter with high specificity and affinity for ferric iron (2004), J. Bacteriol., 186, 6220-6229.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.7

Protein Variants

Protein Variants Comment Organism
Y196I mutation in periplasmic biding protein, FbpA, greatly diminishes iron binding affinity, but has about 35% of wild-type transport activity Haemophilus influenzae

Inhibitors

Inhibitors Comment Organism Structure
Ga3+ exhibis toxicity to Escherichia coli expressing the enzyme Haemophilus influenzae
additional information not inhibitory: carbonyl cyanide m-chlorophenyl hydrazone Haemophilus influenzae
sodium orthovanadate
-
 Haemophilus influenzae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0009
-
 Fe3+ 37°C, wild-type Haemophilus influenzae
0.0012
-
 Fe3+ 37°C, mutant Y196I Haemophilus influenzae

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Fe3+/out high specificity for Fe3+ Haemophilus influenzae ADP + phosphate + Fe3+/in
-
 ?
additional information enzyme has high selectivity for trivalent metals, including Ga3+ and Al3+, over divalent metals Haemophilus influenzae ?
-
 ?

Synonyms

Synonyms Comment Organism
hFbpABC transporter
-
 Haemophilus influenzae