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Literature summary for 1.16.3.1 extracted from

  • Masuda, T.; Goto, F.; Yoshihara, T.; Mikami, B.
    The universal mechanism for iron translocation to the ferroxidase site in ferritin, which is mediated by the well conserved transit site (2010), Biochem. Biophys. Res. Commun., 400, 94-99.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant H ferritin, 10 mg/ml protein in 10 mM Tris,HCl, pH 7.5, and 0.15 M NaCl, is mixed at equal volumes with crystallization solution containing 0.1 M BICINE-Na, pH 9.0, and 1.9-2.0 M MgCl2, 20°C, 1 week, X-ray diffraction structure determination and analysis at 1.52-1.97 A resolution Homo sapiens

Protein Variants

Protein Variants Comment Organism
E140A site-directed mutagenesis, the initial velocity of iron oxidization is reduced in the mutant Homo sapiens
E140Q site-directed mutagenesis, the initial velocity of iron oxidization is highly reduced in the mutant. The side chain of the mutated Gln140 is fixed by a hydrogen bond, whereas that of native Glu140 is flexible Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information stopped-flow kinetics and initial velocities of iron oxidation of wild-type and mutant enzymes, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P02794 ferritin heavy chain
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heat treatment at 60°C for 10 min, followed by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme metal binding structure, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional structural analysis of wild-type and mutant H ferritins, overview Homo sapiens

Synonyms

Synonyms Comment Organism
H ferritin
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Homo sapiens

General Information

General Information Comment Organism
additional information ferritin is a ubiquitous iron storage protein that possesses ferroxidase activity Homo sapiens