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Literature summary extracted from

  • Bobyk, K.D.; Ballou, D.P.; Rokita, S.E.
    Rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid (2015), Biochemistry, 54, 4487-4494.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.21.1.1 additional information
-
 additional information rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid, substrates chloro-, bromo-, and iodotyrosine bind with similar rate constants, overview. Standard two-state model, no intermediate complex accumulates during closure of the active site lid induced by substrate Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.21.1.1 L-tyrosine + 2 NADP+ + 2 iodide Homo sapiens
-
 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.21.1.1 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.21.1.1 thyroid
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.21.1.1 L-tyrosine + 2 NADP+ + 2 bromide halide elimination does not appear to limit reactions of bromo- and iodotyrosine since both fully oxidize the reduced enzyme with nearly equivalent second-order rate constants despite the differing strength of their carbon-halogen bonds Homo sapiens 3,5-dibromo-L-tyrosine + 2 NADPH + 2 H+
-
 r
1.21.1.1 L-tyrosine + 2 NADP+ + 2 chloride chlorotyrosine reacts with the reduced enzyme approximately 20fold more slowly than bromo- and iodotyrosine and reveals a spectral intermediate that forms at approximately the same rate as the bromo- and iodotyrosine reactions Homo sapiens 3,5-dichloro-L-tyrosine + 2 NADPH + 2 H+
-
 r
1.21.1.1 L-tyrosine + 2 NADP+ + 2 iodide
-
 Homo sapiens 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
 ?
1.21.1.1 L-tyrosine + 2 NADP+ + 2 iodide halide elimination does not appear to limit reactions of bromo- and iodotyrosine since both fully oxidize the reduced enzyme with nearly equivalent second-order rate constants despite the differing strength of their carbon-halogen bonds Homo sapiens 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
 r
1.21.1.1 additional information fluorotyrosine is an inert substrate analogue Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.21.1.1 IYD
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.21.1.1 flavin dependent on Homo sapiens
1.21.1.1 NADPH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.21.1.1 metabolism reductive dehalogenation such as that catalyzed by iodotyrosine deiodinase is highly unusual in aerobic organisms but necessary for iodide salvage from iodotyrosine generated during thyroxine biosynthesis Homo sapiens
1.21.1.1 physiological function reductive dehalogenation such as that catalyzed by iodotyrosine deiodinase is highly unusual in aerobic organisms but necessary for iodide salvage from iodotyrosine generated during thyroxine biosynthesis Homo sapiens