KEGG   ENZYME: 1.97.1.10Help
Entry
EC 1.97.1.10                Enzyme                                 

Name
thyroxine 5'-deiodinase;
diiodothyronine 5'-deiodinase [ambiguous];
iodothyronine 5'-deiodinase;
iodothyronine outer ring monodeiodinase;
type I iodothyronine deiodinase;
type II iodothyronine deiodinase;
thyroxine 5-deiodinase [misleading];
L-thyroxine iodohydrolase (reducing)
Class
Oxidoreductases;
Other oxidoreductases;
Sole sub-subclass for oxidoreductases that do not belong in the other subclasses
BRITE hierarchy
Sysname
acceptor:3,5,3'-triiodo-L-thyronine oxidoreductase (iodinating)
Reaction(IUBMB)
3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2 [RN:R03734]
Reaction(KEGG)
Substrate
3,5,3'-triiodo-L-thyronine [CPD:C02465];
iodide [CPD:C00708];
A [CPD:C00028];
H+ [CPD:C00080]
Product
L-thyroxine [CPD:C01829];
AH2 [CPD:C00030]
Comment
The enzyme activity has only been demonstrated in the direction of 5'-deiodination, which renders the thyroid hormone more active. The enzyme consists of type I and type II enzymes, both containing selenocysteine, but with different kinetics. For the type I enzyme the first reaction is a reductive deiodination converting the -Se-H group of the enzyme into an -Se-I group; the reductant then reconverts this into -Se-H, releasing iodide.
Orthology
K01562  
thyroxine 5'-deiodinase
Genes
HSA: 
1733(DIO1) 1734(DIO2)
PTR: 
467521(DIO2) 469331(DIO1)
PPS: 
100972089(DIO2) 100980739(DIO1)
GGO: 
101124806(DIO2) 101154004(DIO1)
PON: 
100440998(DIO1) 100449335(DIO2)
MCC: 
707484(DIO2) 714739(DIO1)
MMU: 
13370(Dio1) 13371(Dio2)
RNO: 
25430(Dio1) 65162(Dio2)
CFA: 
403635(DIO1) 490813(DIO2)
AML: 
FCA: 
101088170(DIO2) 493798(DIO1)
BTA: 
494548(DIO2) 782446(DIO1)
SSC: 
414379(DIO2) 414380(DIO1)
ECB: 
100050359(DIO1) 100052547(DIO2)
MDO: 
SHR: 
100917546(DIO2) 100923092(DIO1)
GGA: 
373903(DIO2) 395940(DIO1)
MGP: 
TGU: 
100224791(DIO2)
ACS: 
XLA: 
733447(dio1)
XTR: 
100036737(dio2) 100497874(dio1)
DRE: 
352937(dio2) 799937(dio1)
TRU: 
100191067(dio1) 100191068(dio2)
OLA: 
TAD: 
 » show all
Taxonomy
Reference
1  [PMID:7053997]
  Authors
Chopra IJ, Chua Teco GN.
  Title
Characteristics of inner ring (3 or 5) monodeiodination of 3,5-diiodothyronine in rat liver: evidence suggesting marked similarities of inner and outer ring deiodinases for iodothyronines.
  Journal
Endocrinology. 110 (1982) 89-97.
  Organism
Rattus norvegicus [GN:rno]
Reference
2  [PMID:6176242]
  Authors
Goswami A, Leonard JL, Rosenberg IN.
  Title
Inhibition by coumadin anticoagulants of enzymatic outer ring monodeiodination of iodothyronines.
  Journal
Biochem. Biophys. Res. Commun. 104 (1982) 1231-8.
  Organism
Rattus norvegicus [GN:rno]
Reference
3  [PMID:7227308]
  Authors
Smallridge RC, Burman KD, Ward KE, Wartofsky L, Dimond RC, Wright FD, Latham KR.
  Title
3',5'-diiodothyronine to 3'-monoiodothyronine conversion in the fed and fasted rat: enzyme characteristics and evidence for two distinct 5'-deiodinases.
  Journal
Endocrinology. 108 (1981) 2336-45.
  Organism
Rattus norvegicus [GN:rno]
Reference
4  [PMID:11898402]
  Authors
Kohrle J.
  Title
Iodothyronine deiodinases.
  Journal
Methods. Enzymol. 347 (2002) 125-67.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
70712-46-8

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