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Literature summary for 1.16.3.1 extracted from

  • Ziegler, L.; Terzulli, A.; Gaur, R.; McCarthy, R.; Kosman, D.J.
    Functional characterization of the ferroxidase, permease high-affinity iron transport complex from Candida albicans (2011), Mol. Microbiol., 81, 473-485.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.16.3.1

Cloned(Commentary)

Cloned (Comment) Organism
functional expression of Fet31 and Fet34 C-terminally fused to YFP or CFP in Saccharomyces cerevisiae enzyme ScFet3p-deficient strain plasma membrane, functional complementation. Other Fet proteins, e.g. CaFet33, from Candida albicans fail to complement the Saccharomyces cerevisiae mutant due to false localization at the vacuolar membrane Candida albicans

Protein Variants

Protein Variants Comment Organism
E184A a Fet34 mutant, that shows altered kinetics compared to the wild-type enzyme Candida albicans
E184A/D408A a Fet34 mutant, that shows altered kinetics compared to the wild-type enzyme Candida albicans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics and steady-state turnover of Fe2+, overview Candida albicans
0.0079
-
 Fe2+ recombinant wild-type CaFet34, pH not specified in the publication, temperature not specified in the publication Candida albicans
0.0108
-
 Fe2+ recombinant E184A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication Candida albicans
1.43
-
 Fe2+ recombinant E184A/D408A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication Candida albicans

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane Fet31 and Fet34, both localize to the yeast plasma membrane Candida albicans 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ Fet31 and Fet34 contain a type 3 Cu2+ pair known as the binuclear Cu-cluster, recombinant soluble Fet34 contains a full complement of 4 Cu atoms per molecule Candida albicans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 Fe2+ + 4 H+ + O2 Candida albicans
-
 4 Fe3+ + 2 H2O
-
 ?
additional information Candida albicans the Fe-uptake proteins Fet31 and Fet34 support a mechanism of Fe-trafficking that involves channelling of the CaFet34-generated Fe3+ directly to CaFtr1 for transport into the cytoplasm ?
-
 ?

Organism

Organism UniProt Comment Textmining
Candida albicans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Fet31 and Fet34 from Saccharomycs cerevisiae by glycosidase EndoH treatment and anion exchange chromatography Candida albicans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 Fe2+ + 4 H+ + O2
-
 Candida albicans 4 Fe3+ + 2 H2O
-
 ?
additional information the Fe-uptake proteins Fet31 and Fet34 support a mechanism of Fe-trafficking that involves channelling of the CaFet34-generated Fe3+ directly to CaFtr1 for transport into the cytoplasm Candida albicans ?
-
 ?
additional information enzymatic activity of sFet34 towards ferrous iron is determined by quantifying the velocity of O2 uptake using standard O2-electrode protocols Candida albicans ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.07
-
 Fe2+ recombinant E184A/D408A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication Candida albicans
0.74
-
 Fe2+ recombinant E184A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication Candida albicans
1.06
-
 Fe2+ recombinant wild-type CaFet34, pH not specified in the publication, temperature not specified in the publication Candida albicans

General Information

General Information Comment Organism
additional information protein localization patterns and metal-enzyme complexes of Candida albicans wild-type and mutant enzymes compared to Saccharomyces cerevisiae enzymes, overview Candida albicans
physiological function the two ferroxidases are likely involved in high-affinity Fe-uptake in Candida albicans, Fet31 and Fet34, both support Fe-uptake along with an Ftr1 protein, either from Candida albicans or from Saccharomyces cerevisiae. CaFtr1 and not CaFtr2 is required for the virulence of the pathogen Candida albicans