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Literature summary for 1.16.3.1 extracted from

  • Brito, C.; Matias, C.; Gonzalez-Nilo, F.D.; Watt, R.K.; Yevenes, A.
    The C-terminal regions have an important role in the activity of the ferroxidase center and the stability of Chlorobium tepidum ferritin (2014), Protein J., 33, 211-220 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene ftn, sequence comparisons, recombinant expression of wild-type enzyme and mutant A19Y in Escherichia coli strain BL21(DE3) Chlorobaculum tepidum

Protein Variants

Protein Variants Comment Organism
A19Y site-directed mutagenesis, introduction of a stop codon at position 166 and replacment of Ala19 by a Tyr residue. The mutant is able to bind, oxidize and store iron, and its activity is inhibited by Zn(II) as described for other ferritins. The mutant enzymes shows reduced activity and protein stability compared to the wild-type enzyme Chlorobaculum tepidum
additional information deletion of 38 amino acid of the C-terminal region of rCtFtn decreases the enzyme stability Chlorobaculum tepidum

Inhibitors

Inhibitors Comment Organism Structure
GdnHCl recombinant wild-type rCtFtn and mutant A19Y are stable at up to 2 M GdnHCl. At 2.5 M GdnHCl both proteins start to loose structural stability Chlorobaculum tepidum
Zn2+
-
Chlorobaculum tepidum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of Fe(II) oxidation of wild-type and mutant enzymes Chlorobaculum tepidum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 Fe(II) + 4 H+ + O2 Chlorobaculum tepidum
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
4 Fe(III) + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Chlorobaculum tepidum Q8KBP5 i.e. Chlorobaculum tepidum
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS Q8KBP5 i.e. Chlorobaculum tepidum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 Fe(II) + 4 H+ + O2
-
Chlorobaculum tepidum 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity Chlorobaculum tepidum 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS 4 Fe(III) + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
CT1740
-
Chlorobaculum tepidum
CtFtn
-
Chlorobaculum tepidum
ferritin
-
Chlorobaculum tepidum
Ftn
-
Chlorobaculum tepidum
More cf. EC 1.16.3.2 Chlorobaculum tepidum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Chlorobaculum tepidum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Chlorobaculum tepidum

General Information

General Information Comment Organism
metabolism the initial step in the iron store mechanism occurs when the Fe(II) is oxidize to Fe(III) at the ferroxidase center (FC) found in the H-chain from mammalian ferritins, bacterial ferritins and Bfr subunits Chlorobaculum tepidum
additional information the recombinant Chlorobium tepidum ferritin (rCtFtn) has an unusual C-terminal region composed of 12 histidine residues, as well as aspartate and glutamate residues. These residues act as potential metal ion ligands, and the rCtFtn homology model predicts that this region projects inside the protein cage. The rCtFtn also lacks a conserved Tyr residue in position 19. The C-terminal region plays an important role in the activity of the ferroxidase center and the stability of rCtFtn. Homology modeling of the subunit of rCtFtn shows that the protein acquires the typical 5 alpha-helix bundle observed for other ferritin subunits Chlorobaculum tepidum
physiological function the recombinant Chlorobium tepidum ferritin (rCtFtn) is able to oxidize iron with a moderate ferroxidase activity Chlorobaculum tepidum