TPH1

From Wikipedia, the free encyclopedia

Tryptophan hydroxylase 1 (tryptophan 5-monooxygenase)

PDB rendering based on 1mlw.

Available structures: 1mlw

Identifiers

Symbol(s)

TPH1; MGC119994; TPH; TPRH

External IDs

OMIM: 191060 MGI: 98796 HomoloGene: 3080

EC number

1.14.16.4

Gene ontology
Molecular Function:	• monooxygenase activity • tryptophan 5-monooxygenase activity • iron ion binding • amino acid binding • metal ion binding
Biological Process:	• serotonin biosynthetic process from tryptophan • metabolic process • aromatic amino acid family metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004179 (mRNA)
NP_004170 (protein)

NM_009414 (mRNA)
NP_033440 (protein)

Location

Chr 11: 18 - 18.02 Mb

Chr 7: 46.52 - 46.54 Mb

Pubmed search

[1]

[2]

Tryptophan hydroxylase 1 (tryptophan 5-monooxygenase), also known as TPH1, is a human gene.^[1]

Tryptophan hydroxylase (TPH; EC 1.14.16.4) catalyzes the biopterin-dependent monooxygenation of tryptophan to 5-hydroxytryptophan (5HT), which is subsequently decarboxylated to form the neurotransmitter serotonin. It is thus the rate-limiting enzyme in the biosynthesis of serotonin. TPH expression is limited to a few specialized tissues: raphe neurons, pinealocytes, mast cells, mononuclear leukocytes, beta-cells of the islets of Langerhans, and intestinal and pancreatic enterochromaffin cells.[supplied by OMIM]^[1]

[edit] See also

Tryptophan hydroxylase

[edit] References

^ ^a ^b Entrez Gene: TPH1 tryptophan hydroxylase 1 (tryptophan 5-monooxygenase).

[edit] Further reading

Li D, He L (2007). "Further clarification of the contribution of the tryptophan hydroxylase (TPH) gene to suicidal behavior using systematic allelic and genotypic meta-analyses.". Hum. Genet. 119 (3): 233–40. doi:10.1007/s00439-005-0113-x. PMID 16450114.
Nielsen DA, Dean M, Goldman D (1993). "Genetic mapping of the human tryptophan hydroxylase gene on chromosome 11, using an intronic conformational polymorphism.". Am. J. Hum. Genet. 51 (6): 1366–71. PMID 1463016.
Craig SP, Boularand S, Darmon MC, et al. (1991). "Localization of human tryptophan hydroxylase (TPH) to chromosome 11p15.3----p14 by in situ hybridization.". Cytogenet. Cell Genet. 56 (3-4): 157–9. PMID 2055111.
Boularand S, Darmon MC, Ganem Y, et al. (1990). "Complete coding sequence of human tryptophan hydroxylase.". Nucleic Acids Res. 18 (14): 4257. PMID 2377472.
Ledley FD, Grenett HE, Bartos DP, et al. (1987). "Assignment of human tryptophan hydroxylase locus to chromosome 11: gene duplication and translocation in evolution of aromatic amino acid hydroxylases.". Somat. Cell Mol. Genet. 13 (5): 575–80. PMID 2889273.
Ichimura T, Uchiyama J, Kunihiro O, et al. (1996). "Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase.". J. Biol. Chem. 270 (48): 28515–8. PMID 7499362.
Tipper JP, Citron BA, Ribeiro P, Kaufman S (1995). "Cloning and expression of rabbit and human brain tryptophan hydroxylase cDNA in Escherichia coli.". Arch. Biochem. Biophys. 315 (2): 445–53. doi:10.1006/abbi.1994.1523. PMID 7986090.
Furukawa Y, Ikuta N, Omata S, et al. (1993). "Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein.". Biochem. Biophys. Res. Commun. 194 (1): 144–9. doi:10.1006/bbrc.1993.1796. PMID 8101440.
Kuhn DM, Arthur R, States JC (1997). "Phosphorylation and activation of brain tryptophan hydroxylase: identification of serine-58 as a substrate site for protein kinase A.". J. Neurochem. 68 (5): 2220–3. PMID 9109552.
Wang GA, Coon SL, Kaufman S (1998). "Alternative splicing at the 3'-cDNA of human tryptophan hydroxylase.". J. Neurochem. 71 (4): 1769–72. PMID 9751214.
Austin MC, O'Donnell SM (1999). "Regional distribution and cellular expression of tryptophan hydroxylase messenger RNA in postmortem human brainstem and pineal gland.". J. Neurochem. 72 (5): 2065–73. PMID 10217286.
Yu PL, Fujimura M, Okumiya K, et al. (1999). "Immunohistochemical localization of tryptophan hydroxylase in the human and rat gastrointestinal tracts.". J. Comp. Neurol. 411 (4): 654–65. PMID 10421874.
Kowlessur D, Kaufman S (1999). "Cloning and expression of recombinant human pineal tryptophan hydroxylase in Escherichia coli: purification and characterization of the cloned enzyme.". Biochim. Biophys. Acta 1434 (2): 317–30. PMID 10525150.
McKinney J, Teigen K, Frøystein NA, et al. (2002). "Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity.". Biochemistry 40 (51): 15591–601. PMID 11747434.
Serretti A, Cristina S, Lilli R, et al. (2002). "Family-based association study of 5-HTTLPR, TPH, MAO-A, and DRD4 polymorphisms in mood disorders.". Am. J. Med. Genet. 114 (4): 361–9. doi:10.1002/ajmg.10356. PMID 11992558.
Slominski A, Pisarchik A, Semak I, et al. (2002). "Serotoninergic and melatoninergic systems are fully expressed in human skin.". FASEB J. 16 (8): 896–8. doi:10.1096/fj.01-0952fje. PMID 12039872.
Yohrling IV GJ, Jiang GC, DeJohn MM, et al. (2002). "Inhibition of tryptophan hydroxylase activity and decreased 5-HT1A receptor binding in a mouse model of Huntington's disease.". J. Neurochem. 82 (6): 1416–23. PMID 12354289.
Wang L, Erlandsen H, Haavik J, et al. (2002). "Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin.". Biochemistry 41 (42): 12569–74. PMID 12379098.
Slominski A, Pisarchik A, Semak I, et al. (2002). "Serotoninergic system in hamster skin.". J. Invest. Dermatol. 119 (4): 934–42. doi:10.1046/j.1523-1747.2002.00156.x. PMID 12406341.
Ono H, Shirakawa O, Kitamura N, et al. (2003). "Tryptophan hydroxylase immunoreactivity is altered by the genetic variation in postmortem brain samples of both suicide victims and controls.". Mol. Psychiatry 7 (10): 1127–32. doi:10.1038/sj.mp.4001150. PMID 12476329.