Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Details on Person TPO combines Diiodo-Tyr and I-Tyr on TG to form T3

Class:Id	Reaction:9961637
_displayName	TPO combines Diiodo-Tyr and I-Tyr on TG to form T3
_timestamp	2025-09-25 08:50:29
authored	[InstanceEdit:9961677] Stephan, Ralf, 2025-07-10
catalystActivity	[CatalystActivity:9961543] transferase activity of p-DUOX1,2:DUOXA1,2:TPO:CAV1:TXNDC11 [plasma membrane]
compartment	[Compartment:984] extracellular region [Compartment:876] plasma membrane
created	[InstanceEdit:9961392] Stephan, Ralf, 2025-07-25
crossReference	[DatabaseIdentifier:9961350] RHEA:48969
goBiologicalProcess	[GO_BiologicalProcess:19403] thyroid hormone generation
input	[SimpleEntity:351629] H2O2 [extracellular region] [SimpleEntity:351629] H2O2 [extracellular region] [SimpleEntity:351629] H2O2 [extracellular region] [SimpleEntity:351629] H2O2 [extracellular region] [SimpleEntity:351629] H2O2 [extracellular region] [SimpleEntity:351629] H2O2 [extracellular region] [Complex:9961502] I(1,2)Y-TG dimer [extracellular region] [Homo sapiens]
internalReviewed	[InstanceEdit:9967044] D'Eustachio, Peter, 2025-09-25
literatureReference	[LiteratureReference:350851] Formation of molecular iodine during oxidation of iodide by the peroxidase/H2O2 system. Implications for antithyroid therapy [LiteratureReference:9961618] Cryo-electron microscopy structures of human thyroid peroxidase (TPO) in complex with TPO antibodies [LiteratureReference:9961675] Factors influencing the study of peroxidase-generated iodine species and implications for thyroglobulin synthesis [LiteratureReference:9961572] Iodination and oxidation of thyroglobulin catalyzed by thyroid peroxidase [LiteratureReference:9961636] Thyroid peroxidase as a dual active site enzyme: Focus on biosynthesis, hormonogenesis and thyroid disorders of autoimmunity and cancer [LiteratureReference:9961534] Mutation analysis of thyroid peroxidase gene in Chinese patients with total iodide organification defect: identification of five novel mutations [LiteratureReference:9961575] Genetics of specific phenotypes of congenital hypothyroidism: a population-based approach [LiteratureReference:9961687] The mechanism of iodination reactions in thyroid glands [LiteratureReference:9961360] Mechanism of simultaneous iodination and coupling catalyzed by thyroid peroxidase [LiteratureReference:9961602] The structure of human thyroglobulin
modified	[InstanceEdit:9966171] Stephan, Ralf, 2025-09-11 [InstanceEdit:9966179] Stephan, Ralf, 2025-09-11 [InstanceEdit:9966620] Stephan, Ralf, 2025-09-23 [InstanceEdit:9967043] Stephan, Ralf, 2025-09-25 [InstanceEdit:9967045] Stephan, Ralf, 2025-09-25
name	TPO combines Diiodo-Tyr and I-Tyr on TG to form T3 DIT and MIT combine to form triiodothyronine
negativePrecedingEvent	[NegativePrecedingEvent:9966173] Incorrect Order: Iodinated TG is released from storage
output	[SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [SimpleEntity:109276] H2O [extracellular region] [Complex:9961569] T3-TG dimer [extracellular region] [Homo sapiens]
precedingEvent	[Reaction:209815] Tyrosine is monoiodinated [Homo sapiens] [Reaction:350901] Iodide is organified [Homo sapiens] [Reaction:209921] Monoiodinated tyrosine can be deiodinated [Homo sapiens] [Reaction:5693681] DUOX1 reduces O2 to H2O2 [Homo sapiens] [Reaction:9961403] DUOX2 reduces O2 to H2O2 [Homo sapiens] [Reaction:9961567] TPO incompletely iodinates I-Tyr on TG [Homo sapiens] [Reaction:350901] Iodide is organified [Homo sapiens] [Reaction:9961427] ANO1 dimer exports I- to follicular lumen [Homo sapiens] [Reaction:5693681] DUOX1 reduces O2 to H2O2 [Homo sapiens] [Reaction:9961403] DUOX2 reduces O2 to H2O2 [Homo sapiens] [Reaction:5627802] SLC26A4 exports I- to follicular lumen [Homo sapiens] [Reaction:9961331] TPO iodinates Tyr on TG [Homo sapiens]
regulatedBy	[PositiveRegulation:1449716] Positive regulation by 'Thyrotropin [extracellular region]'
reviewStatus	[ReviewStatus:9821383] three stars
species	[Species:48887] Homo sapiens
stableIdentifier	[StableIdentifier:9961763] R-HSA-9961637.1
summation	[Summation:352312] A small fraction of TG tyrosines are incompletely iodinated,...
(hasEvent)	[Pathway:9961413] UNRELEASED: Thyroxine metabolism and iodide transport [Homo sapiens]
(precedingEvent)	[BlackBoxEvent:9961335] P4HB oligomerizes iodinated TG [Homo sapiens] [BlackBoxEvent:9961402] T3,T4-TG dimers are imported and move to lysosomes [Homo sapiens] [BlackBoxEvent:9966621] TPO oligomerizes iodinated TG [Homo sapiens]
[Change default viewing format]

No pathways have been reviewed or authored by TPO combines Diiodo-Tyr and I-Tyr on TG to form T3 (9961637)