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Literature summary for 1.21.1.1 extracted from

  • Goswami, A.; Rosenberg, I.
    Characterization of a flavoprotein iodotyrosine deiodinase from bovine thyroid. Flavin nucleotide binding and oxidation-reduction properties (1979), J. Biol. Chem., 254, 12326-12330.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Bos taurus
-
-

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of stable aporptoein Bos taurus

Renatured (Commentary)

Renatured (Comment) Organism
apoprotein binds FMN with an almost complete restoration of enzymatic activity. It can also bind FAD with partial restoration of activity, but does not bind riboflavin Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
thyroid gland
-
Bos taurus
-

Cofactor

Cofactor Comment Organism Structure
FAD
-
Bos taurus
FMN enzyme is reduced in two successive 1-electron oxidation-reduction steps. The oxidation-reduction potential of the couple semiquinone/fully reduced enzyme is -0.412 V at pH 7 and 25°C. The value for the oxidized/semiquinone couple is -0.190 V at pH 7 and 25°C Bos taurus