Literature summary extracted from

Buettner, C.; Harney, J.W.; Larsen, P.R.
The role of selenocysteine 133 in catalysis by the human type 2 iodothyronine deiodinase (2000), Endocrinology, 141, 4606-4612.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.21.99.4	SeC133A	inactive mutant enzyme	Homo sapiens
1.21.99.4	SeC133C	the Km-value for L-thyroxine is 1500fold higher than the wild-type value, the turnover-number is 10fold lower than the wild-type value	Homo sapiens

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.21.99.4	0.0000014	-	L-thyroxine	wild-type enzyme	Homo sapiens
1.21.99.4	0.0021	-	L-thyroxine	mutant enzyme SeC133C	Homo sapiens

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.21.99.4	Se	enzyme contains selenocysteine in the highly conserved active senter at position 133. Selenium plays a critical role in deiodination	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.21.99.4	Homo sapiens	Q92813	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.21.99.4	L-thyroxine + AH2	-	Homo sapiens	3,3',5-triiodothyronine + iodide + A + H+	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.21.99.4	type 2 iodothyronine deiodinase	-	Homo sapiens

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.21.99.4	additional information	-	additional information	-	Homo sapiens

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Release 2023.1 (January 2023)