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Literature summary 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.21.1.1 soluble
-
Bos taurus
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.21.1.1 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.21.1.1 purification of stable aporptoein Bos taurus

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.21.1.1 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

EC Number Source Tissue Comment Organism Textmining
1.21.1.1 thyroid gland
-
Bos taurus
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.21.1.1 FAD
-
Bos taurus
1.21.1.1 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