Metabolism of amine-derived hormones (Homo sapiens)

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9, 10, 24232211, 18648132, 16, 1967111, 1817, 2120561251463, 15secretory granulecytosolAscH-I-DBH tetramerI-T3ASMTDIO3O2DDC dimerH+DIO2 BH4NADPHDEHAL1:FMNTPH2 AANATI-TSHB T4I2CGA Fe2+ O2ADRH2OH+Na+PNMTL-TrpDIO1 TH:Fe2+MLTNa+PQQ 4aOH-BH4CO2Ac5HTL-TyrThyrotropin5HTDBH(40-617) H2O2L-AlaDeHANADPHAdoMetDAH+HITPOT4DUOX1 AdoHcyTH L-TyrT3TPH:Fe++H2OL-DopaTPH1 DUOX1,2Ac-CoADITAdoHcyMITNADP+DUOX2 H+Cu2+ DIO dimerNADPHSLC5A5NADPHL-TyrDANADP+O2NADP+PXLP-DDC H2ONADP+H+L-AlaFe2+ CoA-SHNADP+NAdNAdFMN AdoMetIYD O2H+5HTP


Description

Catecholamines and thyroxine are synthesized from tyrosine, and serotonin and melatonin from tryptophan. View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 209776
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Jassal, Bijay

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Bibliography

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  1. Rodriguez IR, Mazuruk K, Schoen TJ, Chader GJ.; ''Structural analysis of the human hydroxyindole-O-methyltransferase gene. Presence of two distinct promoters.''; PubMed Europe PMC Scholia
  2. Kobayashi K, Morita S, Mizuguchi T, Sawada H, Yamada K, Nagatsu I, Fujita K, Nagatsu T.; ''Functional and high level expression of human dopamine beta-hydroxylase in transgenic mice.''; PubMed Europe PMC Scholia
  3. Walther DJ, Peter JU, Bashammakh S, Hörtnagl H, Voits M, Fink H, Bader M.; ''Synthesis of serotonin by a second tryptophan hydroxylase isoform.''; PubMed Europe PMC Scholia
  4. Salvatore D, Low SC, Berry M, Maia AL, Harney JW, Croteau W, St Germain DL, Larsen PR.; ''Type 3 lodothyronine deiodinase: cloning, in vitro expression, and functional analysis of the placental selenoenzyme.''; PubMed Europe PMC Scholia
  5. Gnidehou S, Lacroix L, Sezan A, Ohayon R, Noël-Hudson MS, Morand S, Francon J, Courtin F, Virion A, Dupuy C.; ''Cloning and characterization of a novel isoform of iodotyrosine dehalogenase 1 (DEHAL1) DEHAL1C from human thyroid: comparisons with DEHAL1 and DEHAL1B.''; PubMed Europe PMC Scholia
  6. Degroot LJ, Niepomniszcze H.; ''Biosynthesis of thyroid hormone: basic and clinical aspects.''; PubMed Europe PMC Scholia
  7. Lagorce JF, Thomes JC, Catanzano G, Buxeraud J, Raby M, Raby C.; ''Formation of molecular iodine during oxidation of iodide by the peroxidase/H2O2 system. Implications for antithyroid therapy.''; PubMed Europe PMC Scholia
  8. Lewis DA, Melchitzky DS, Haycock JW.; ''Four isoforms of tyrosine hydroxylase are expressed in human brain.''; PubMed Europe PMC Scholia
  9. Flatmark T.; ''Catecholamine biosynthesis and physiological regulation in neuroendocrine cells.''; PubMed Europe PMC Scholia
  10. Ruddick JP, Evans AK, Nutt DJ, Lightman SL, Rook GA, Lowry CA.; ''Tryptophan metabolism in the central nervous system: medical implications.''; PubMed Europe PMC Scholia
  11. Ichinose H, Kurosawa Y, Titani K, Fujita K, Nagatsu T.; ''Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase.''; PubMed Europe PMC Scholia
  12. Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR.; ''The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression.''; PubMed Europe PMC Scholia
  13. Smanik PA, Liu Q, Furminger TL, Ryu K, Xing S, Mazzaferri EL, Jhiang SM.; ''Cloning of the human sodium lodide symporter.''; PubMed Europe PMC Scholia
  14. Kaneda N, Ichinose H, Kobayashi K, Oka K, Kishi F, Nakazawa A, Kurosawa Y, Fujita K, Nagatsu T.; ''Molecular cloning of cDNA and chromosomal assignment of the gene for human phenylethanolamine N-methyltransferase, the enzyme for epinephrine biosynthesis.''; PubMed Europe PMC Scholia
  15. Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC.; ''Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin.''; PubMed Europe PMC Scholia
  16. Ishii A, Kobayashi K, Kiuchi K, Nagatsu T.; ''Expression of two forms of human dopamine-beta-hydroxylase in COS cells.''; PubMed Europe PMC Scholia
  17. Ameziane-El-Hassani R, Morand S, Boucher JL, Frapart YM, Apostolou D, Agnandji D, Gnidehou S, Ohayon R, Noël-Hudson MS, Francon J, Lalaoui K, Virion A, Dupuy C.; ''Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity.''; PubMed Europe PMC Scholia
  18. Sumi-Ichinose C, Ichinose H, Takahashi E, Hori T, Nagatsu T.; ''Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis.''; PubMed Europe PMC Scholia
  19. Lamouroux A, Vigny A, Faucon Biguet N, Darmon MC, Franck R, Henry JP, Mallet J.; ''The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme.''; PubMed Europe PMC Scholia
  20. Glatt CE, Wahner AD, White DJ, Ruiz-Linares A, Ritz B.; ''Gain-of-function haplotypes in the vesicular monoamine transporter promoter are protective for Parkinson disease in women.''; PubMed Europe PMC Scholia
  21. Edens WA, Sharling L, Cheng G, Shapira R, Kinkade JM, Lee T, Edens HA, Tang X, Sullards C, Flaherty DB, Benian GM, Lambeth JD.; ''Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox.''; PubMed Europe PMC Scholia
  22. Cleary S, Brouwers FM, Eisenhofer G, Pacak K, Christie DL, Lipski J, McNeil AR, Phillips JK.; ''Expression of the noradrenaline transporter and phenylethanolamine N-methyltransferase in normal human adrenal gland and phaeochromocytoma.''; PubMed Europe PMC Scholia
  23. Mandel SJ, Berry MJ, Kieffer JD, Harney JW, Warne RL, Larsen PR.; ''Cloning and in vitro expression of the human selenoprotein, type I iodothyronine deiodinase.''; PubMed Europe PMC Scholia
  24. Köhrle J, Brabant G, Hesch RD.; ''Metabolism of the thyroid hormones.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114805view16:30, 25 January 2021ReactomeTeamReactome version 75
113249view11:31, 2 November 2020ReactomeTeamReactome version 74
112467view15:42, 9 October 2020ReactomeTeamReactome version 73
101752view12:37, 5 November 2018EgonwCHEBI:29036 is the identifier for Cu2+
101376view11:26, 1 November 2018ReactomeTeamreactome version 66
100914view21:01, 31 October 2018ReactomeTeamreactome version 65
100455view19:36, 31 October 2018ReactomeTeamreactome version 64
100002view16:19, 31 October 2018ReactomeTeamreactome version 63
99555view14:53, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93982view13:49, 16 August 2017ReactomeTeamreactome version 61
93584view11:28, 9 August 2017ReactomeTeamreactome version 61
87081view14:23, 18 July 2016MkutmonOntology Term : 'amino acid metabolic pathway' added !
86690view09:24, 11 July 2016ReactomeTeamreactome version 56
83438view12:25, 18 November 2015ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
4aOH-BH4MetaboliteCHEBI:15374 (ChEBI)
5HTMetaboliteCHEBI:28790 (ChEBI)
5HTPMetaboliteCHEBI:17780 (ChEBI)
AANATProteinQ16613 (Uniprot-TrEMBL)
ADRMetaboliteCHEBI:28918 (ChEBI)
ASMTProteinP46597 (Uniprot-TrEMBL)
Ac-CoAMetaboliteCHEBI:15351 (ChEBI)
Ac5HTMetaboliteCHEBI:17697 (ChEBI)
AdoHcyMetaboliteCHEBI:16680 (ChEBI)
AdoMetMetaboliteCHEBI:15414 (ChEBI)
AscH-MetaboliteCHEBI:38290 (ChEBI)
BH4MetaboliteCHEBI:15372 (ChEBI)
CGA ProteinP01215 (Uniprot-TrEMBL)
CO2MetaboliteCHEBI:16526 (ChEBI)
CoA-SHMetaboliteCHEBI:15346 (ChEBI)
Cu2+ MetaboliteCHEBI:28694 (ChEBI)
DAMetaboliteCHEBI:18243 (ChEBI)
DBH tetramerComplexR-HSA-209957 (Reactome)
DBH(40-617) ProteinP09172 (Uniprot-TrEMBL)
DDC dimerComplexR-HSA-209895 (Reactome)
DEHAL1:FMNComplexR-HSA-209777 (Reactome)
DIO dimerComplexR-HSA-350846 (Reactome)
DIO1 ProteinP49895 (Uniprot-TrEMBL)
DIO2 ProteinQ92813 (Uniprot-TrEMBL)
DIO3ProteinP55073 (Uniprot-TrEMBL)
DITMetaboliteCHEBI:15768 (ChEBI)
DUOX1 ProteinQ9NRD9 (Uniprot-TrEMBL)
DUOX1,2ComplexR-HSA-5693689 (Reactome)
DUOX2 ProteinQ9NRD8 (Uniprot-TrEMBL)
DeHAMetaboliteCHEBI:58539 (ChEBI)
FMN MetaboliteCHEBI:17621 (ChEBI)
Fe2+ MetaboliteCHEBI:29033 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2O2MetaboliteCHEBI:16240 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HIMetaboliteCHEBI:43451 (ChEBI)
I-MetaboliteCHEBI:16382 (ChEBI)
I2MetaboliteCHEBI:17606 (ChEBI)
IYD ProteinQ6PHW0 (Uniprot-TrEMBL)
L-AlaMetaboliteCHEBI:57972 (ChEBI)
L-DopaMetaboliteCHEBI:15765 (ChEBI)
L-TrpMetaboliteCHEBI:57912 (ChEBI)
L-TyrMetaboliteCHEBI:58315 (ChEBI)
MITMetaboliteCHEBI:27847 (ChEBI)
MLTMetaboliteCHEBI:16796 (ChEBI)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
NAdMetaboliteCHEBI:18357 (ChEBI)
Na+MetaboliteCHEBI:29101 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
PNMTProteinP11086 (Uniprot-TrEMBL)
PQQ MetaboliteCHEBI:18315 (ChEBI)
PXLP-DDC ProteinP20711 (Uniprot-TrEMBL)
SLC5A5ProteinQ92911 (Uniprot-TrEMBL)
T3MetaboliteCHEBI:28774 (ChEBI)
T4MetaboliteCHEBI:18332 (ChEBI)
TH ProteinP07101 (Uniprot-TrEMBL)
TH:Fe2+ComplexR-HSA-209926 (Reactome)
TPH1 ProteinP17752 (Uniprot-TrEMBL)
TPH2 ProteinQ8IWU9 (Uniprot-TrEMBL)
TPH:Fe++ComplexR-HSA-976249 (Reactome)
TPOProteinP07202 (Uniprot-TrEMBL)
TSHB ProteinP01222 (Uniprot-TrEMBL)
ThyrotropinComplexR-HSA-378994 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
4aOH-BH4ArrowR-HSA-209823 (Reactome)
4aOH-BH4ArrowR-HSA-209828 (Reactome)
5HTArrowR-HSA-209859 (Reactome)
5HTPArrowR-HSA-209828 (Reactome)
5HTPR-HSA-209859 (Reactome)
5HTR-HSA-209792 (Reactome)
AANATmim-catalysisR-HSA-209792 (Reactome)
ADRArrowR-HSA-209903 (Reactome)
ASMTmim-catalysisR-HSA-209821 (Reactome)
Ac-CoAR-HSA-209792 (Reactome)
Ac5HTArrowR-HSA-209792 (Reactome)
Ac5HTR-HSA-209821 (Reactome)
AdoHcyArrowR-HSA-209821 (Reactome)
AdoHcyArrowR-HSA-209903 (Reactome)
AdoMetR-HSA-209821 (Reactome)
AdoMetR-HSA-209903 (Reactome)
AscH-R-HSA-209891 (Reactome)
BH4R-HSA-209823 (Reactome)
BH4R-HSA-209828 (Reactome)
CO2ArrowR-HSA-209859 (Reactome)
CO2ArrowR-HSA-209924 (Reactome)
CoA-SHArrowR-HSA-209792 (Reactome)
DAArrowR-HSA-209924 (Reactome)
DAArrowR-HSA-351596 (Reactome)
DAR-HSA-209891 (Reactome)
DAR-HSA-351596 (Reactome)
DBH tetramermim-catalysisR-HSA-209891 (Reactome)
DDC dimermim-catalysisR-HSA-209859 (Reactome)
DDC dimermim-catalysisR-HSA-209924 (Reactome)
DEHAL1:FMNmim-catalysisR-HSA-209921 (Reactome)
DEHAL1:FMNmim-catalysisR-HSA-209960 (Reactome)
DIO dimermim-catalysisR-HSA-209772 (Reactome)
DIO3mim-catalysisR-HSA-350869 (Reactome)
DITArrowR-HSA-209973 (Reactome)
DITR-HSA-209840 (Reactome)
DITR-HSA-209925 (Reactome)
DITR-HSA-209960 (Reactome)
DUOX1,2mim-catalysisR-HSA-5693681 (Reactome)
DeHAArrowR-HSA-209891 (Reactome)
H+ArrowR-HSA-209821 (Reactome)
H+ArrowR-HSA-209903 (Reactome)
H+R-HSA-209772 (Reactome)
H+R-HSA-209973 (Reactome)
H+R-HSA-350869 (Reactome)
H+R-HSA-350901 (Reactome)
H+R-HSA-5693681 (Reactome)
H2O2ArrowR-HSA-5693681 (Reactome)
H2O2R-HSA-209973 (Reactome)
H2O2R-HSA-350901 (Reactome)
H2OArrowR-HSA-209891 (Reactome)
H2OArrowR-HSA-209973 (Reactome)
H2OArrowR-HSA-350901 (Reactome)
HIArrowR-HSA-209815 (Reactome)
I-ArrowR-HSA-209772 (Reactome)
I-ArrowR-HSA-209910 (Reactome)
I-ArrowR-HSA-209921 (Reactome)
I-ArrowR-HSA-209960 (Reactome)
I-ArrowR-HSA-350869 (Reactome)
I-R-HSA-209910 (Reactome)
I-R-HSA-209973 (Reactome)
I-R-HSA-350901 (Reactome)
I2ArrowR-HSA-350901 (Reactome)
I2R-HSA-209815 (Reactome)
L-AlaArrowR-HSA-209840 (Reactome)
L-AlaArrowR-HSA-209925 (Reactome)
L-DopaArrowR-HSA-209823 (Reactome)
L-DopaR-HSA-209924 (Reactome)
L-TrpR-HSA-209828 (Reactome)
L-TyrArrowR-HSA-209921 (Reactome)
L-TyrArrowR-HSA-209960 (Reactome)
L-TyrR-HSA-209815 (Reactome)
L-TyrR-HSA-209823 (Reactome)
L-TyrR-HSA-209973 (Reactome)
MITArrowR-HSA-209815 (Reactome)
MITR-HSA-209921 (Reactome)
MITR-HSA-209925 (Reactome)
MLTArrowR-HSA-209821 (Reactome)
NADP+ArrowR-HSA-209772 (Reactome)
NADP+ArrowR-HSA-209921 (Reactome)
NADP+ArrowR-HSA-209960 (Reactome)
NADP+ArrowR-HSA-209973 (Reactome)
NADP+ArrowR-HSA-350869 (Reactome)
NADP+ArrowR-HSA-350901 (Reactome)
NADP+ArrowR-HSA-5693681 (Reactome)
NADPHR-HSA-209772 (Reactome)
NADPHR-HSA-209921 (Reactome)
NADPHR-HSA-209960 (Reactome)
NADPHR-HSA-209973 (Reactome)
NADPHR-HSA-350869 (Reactome)
NADPHR-HSA-350901 (Reactome)
NADPHR-HSA-5693681 (Reactome)
NAdArrowR-HSA-209891 (Reactome)
NAdArrowR-HSA-351604 (Reactome)
NAdR-HSA-209903 (Reactome)
NAdR-HSA-351604 (Reactome)
Na+ArrowR-HSA-209910 (Reactome)
Na+R-HSA-209910 (Reactome)
O2R-HSA-209823 (Reactome)
O2R-HSA-209828 (Reactome)
O2R-HSA-209891 (Reactome)
O2R-HSA-5693681 (Reactome)
PNMTmim-catalysisR-HSA-209903 (Reactome)
R-HSA-209772 (Reactome) Iodothyronine deiodinases 1 and 2 (DIO1/2) are the vertebrate enzymes responsible for the deiodination of the prohormone thyroxine (T4; 3,5,3',5'-tetraiodothyronine) into the biologically active hormone T3 (3,5,3'-triiodothyronine). DIO1/2 activity is critical for appropriate T3 levels in the brain during development.
R-HSA-209792 (Reactome) Serotonin N-acetyltransferase (AANAT) catalyzes the N-acetylation of serotonin to form N-acetylserotonin. AANAT utilizes acetyl-CoA as the donor of the acetyl group.
R-HSA-209815 (Reactome) Tyrosines can be iodinated in thyroglobulin to produce precursors for thyroid hormone synthesis.
R-HSA-209821 (Reactome) Hydroxyindole-O-methyltransferase (HIOMT) catalyzes the last step in the synthesis of melatonin. Melatonin is synthesized and released by the pineal gland and is thought to control circadian rhythms. HIOMT has 3 isoforms and utilizes S-adenosyl-L-methionine (SAM) as the methyl donor in the conversion of N-acetyl-5HT to melatonin.
R-HSA-209823 (Reactome) Tyrosine hydroxylase (TH) is the first enzyme in catecholamine biosynthesis, as well as being the rate-limiting enzyme in that process. TH requires tetrahydrobiopterin and uses iron as a cofactor in the 3,4-hydroxylation of tyrosine to produce dopa. Four isoforms of TH are expressed in the human brain and all have enzymatic activity (Nagatsu, T, 1989; Lewis, DA et al, 1993).
R-HSA-209828 (Reactome) The first and rate limiting step in serotonin (5-HT) biosynthesis is catalyzed by tryptophan hydroxylase. The enzyme requires iron(II), tetrahydrobiopterin, and dioxygen cofactors for the hydroxylation of L-tryptophan to 5-hydroxytryptophan. Tryptophan hydroxylase belongs to a small family of monooxygenases that utilize tetrahydrobiopterins. Other members are phenylalanine hydroxylase and tyrosine hydroxylase (Fitzpatrick, PF, 1999; Walther et al, 2003).
R-HSA-209840 (Reactome) Thyroxine (T4) can be formed by the combination of two diiodotyrosines. The hormone thyrotropin can stimulate the production of T3 and T4.
R-HSA-209859 (Reactome) Aromatic L-amino acid decarboxylase (AADC) catalyzes the decarboxylation of both dopa and 5-hydroxytryptophan to dopamine and serotonin, respectively. AADC functions as a homodimer, utilizing pyridoxal phosphate as a cofactor.
R-HSA-209891 (Reactome) Dopamine beta-hydroxylase (DBH; dopamine beta-monooxygenase) is a copper-containing glycoprotein consisting of four identical subunits and catalyzes the oxidation of dopamine to norepinephrine. It requires ascorbic acid as an electron donor. DBH is localized in the norepinephrinergic and epinephrinergic neurons in the central nervous system. The enzyme exists in the secretory vesicles as both soluble and membrane-bound forms. The soluble form is secreted with catecholamines by exocytosis whereas the membrane-bound form is recycled into the vesicles.
R-HSA-209903 (Reactome) Phenylethanolamine N-methyltransferase (PNMT) is the terminal enzyme in catecholamine biosynthesis. It performs transmethylation of noradrenaline to adrenaline using S-adenosyl L-methionine (SAM) as the methyl donor.
R-HSA-209910 (Reactome) Iodide (I-) is transported from blood serum into the thyroid cell by the Na+/I- symporter (sodium/iodide). This intrinsic membrane protein uses energy from the inward movement of Na+ to drive the process and accumulate I- in the cell, maintaining a cellular concentration 30-40 times that of the serum concentration. This process, also called the iodide trap, is stimulated by TSH (thyroid stimulating hormone) and is saturable by large amounts of I-.
R-HSA-209921 (Reactome) The human iodotyrosine dehalogenase 1 (DEHAL1) gene is composed of six exons. Two isoforms (DEHAL1 and DEHAL1B) have been published, both of which have a nitroreductase domain and arise from differential splicing in exon 5. The DEHAL1 isoform is a transmembrane protein that catalyzes the NADPH-dependent deiodination of monoiodotyrosine (MIT) and diiodotyrosine (DIT).
R-HSA-209924 (Reactome) Aromatic L-amino acid decarboxylase (AADC, dopa decarboxylase) decarboxylates dopa to form dopamine.
R-HSA-209925 (Reactome) Mono- and di-iodinated tyrosine can combine to form tri-iodothyronine (T3). The hormone thyrotropin can stimulate the production of T3 and T4.
R-HSA-209960 (Reactome) The human iodotyrosine dehalogenase 1 (DEHAL1) gene is composed of six exons. Two isoforms (DEHAL1 and DEHAL1B) have been published, both of which have a nitroreductase domain and arise from differential splicing in exon 5. The DEHAL1 isoform is a transmembrane protein that catalyzes the NADPH-dependent deiodination of monoiodotyrosine (MIT) and diiodotyrosine (DIT).
R-HSA-209973 (Reactome) Tyrosines can be iodinated in thyroglobulin to produce precursors for thyroid hormone synthesis.
R-HSA-350869 (Reactome) Type III iodothyronine deiodinase (DIO3) is an integral membrane protein (Baqui M et al, 2003) and catalyzes the conversion of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). Both RT3 and T2 are inactive metabolites. It is thought DIO3 plays an essential role for regulation of thyroid hormone inactivation during embryological development.
R-HSA-350901 (Reactome) The first step in the biogenesis of thyroid hormones is the oxidation of iodide (I-) by H2O2/peroxidase after being taken up by the thyroid gland. This event is known as organification.
R-HSA-351596 (Reactome) While dopamine is synthesized in the cytosol, its conversion to noradrenaline is mediated by a vesicle-associated enzyme. The process by which dopamine is transported across the vesicle membrane has not been elucidated yet, however.
R-HSA-351604 (Reactome) While noradrenaline is synthesized in the secretory vesicle, its conversion to adrenaline is mediated by a cytosolic enzyme. The process by which noradrenaline is transported across the vesicle membrane has not been worked out, however.
R-HSA-5693681 (Reactome) Dual oxidases 1 and 2 (DUOX1, 2) mediates the generation of hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase for thyroid hormone formation and lactoperoxidase (Edens et al. 2001, Ameziane-El-Hassani et al. 2005).
SLC5A5mim-catalysisR-HSA-209910 (Reactome)
T3ArrowR-HSA-209772 (Reactome)
T3ArrowR-HSA-209925 (Reactome)
T3ArrowR-HSA-350869 (Reactome)
T4ArrowR-HSA-209840 (Reactome)
T4R-HSA-209772 (Reactome)
T4R-HSA-350869 (Reactome)
TH:Fe2+mim-catalysisR-HSA-209823 (Reactome)
TPH:Fe++mim-catalysisR-HSA-209828 (Reactome)
TPOmim-catalysisR-HSA-209815 (Reactome)
TPOmim-catalysisR-HSA-209840 (Reactome)
TPOmim-catalysisR-HSA-209925 (Reactome)
TPOmim-catalysisR-HSA-209973 (Reactome)
TPOmim-catalysisR-HSA-350901 (Reactome)
ThyrotropinArrowR-HSA-209840 (Reactome)
ThyrotropinArrowR-HSA-209925 (Reactome)
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