DBH

DBH
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген DBH[d][1]
Молекуляр функция связывание с ионом металла[d][2], monooxygenase activity[d][2][2], oxidoreductase activity[d][2], oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen[d][3], L-ascorbic acid binding[d][2], активность катализатора[d][4][2], dopamine beta-monooxygenase activity[d][3][3][5][…], copper ion binding[d][3][5][6], dopamine beta-monooxygenase activity[d][3][3][5][…], copper ion binding[d][2][7][8][…], oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen[d][2][9] һәм dopamine beta-monooxygenase activity[d][2][8][4][…]
Күзәнәк компоненты цитоплазма[10], transport vesicle membrane[d][2], мембрана өлеше[d][2], chromaffin granule lumen[d][2], chromaffin granule membrane[d][2], цитоплазматическая везикула[d][2], мембрана[d][4][2], күзәнәк тышындагы өлкә[d][11][2], күзәнәк тышындагы мохит[d][5], secretory granule membrane[d][3][5], secretory granule lumen[d][2][2][8], внутриклеточная мембранная органелла[d][2], эндоплазматик челтәр[2], центр организации микротрубочек[d][2], күзәнәк тышындагы мохит[d][8][9], цитоплазма[4][9] һәм secretory granule membrane[d][2][8][9]
Биологик процесс response to amphetamine[d][2], chemical synaptic transmission[d][12], homoiothermy[d][2], leukocyte mediated immunity[d][2], визуальное обучение[d][2], fear response[d][2], behavioral response to ethanol[d][2], locomotory behavior[d][2], regulation of extrinsic apoptotic signaling pathway[d][2], regulation of cell population proliferation[d][2], positive regulation of vasoconstriction[d][2], glucose homeostasis[d][2], Maternal behavior[d][2], хәтер[2], leukocyte migration[d][2], response to pain[d][2], blood vessel remodeling[d][2], cytokine production[d][2], associative learning[d][2], catecholamine biosynthetic process[d][2][2], dopamine catabolic process[d][3][5][10], norepinephrine biosynthetic process[d][13][3][3], octopamine biosynthetic process[d][9], dopamine catabolic process[d][2][8][4][…], norepinephrine biosynthetic process[d][14][2][2][…] һәм positive regulation of cold-induced thermogenesis[d][15][2]
Тәэсир итешә nepicastat[d][16]
Шифр КФ 1.14.17.1

DBH (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[17][18]

Искәрмәләр

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 2,33 2,34 2,35 2,36 2,37 2,38 2,39 2,40 2,41 2,42 2,43 2,44 2,45 GOA
  3. ↑ 3,00 3,01 3,02 3,03 3,04 3,05 3,06 3,07 3,08 3,09 GOA
  4. ↑ 4,0 4,1 4,2 4,3 4,4 A Lamouroux, A Vigny, Biguet N. F. et al. The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme // EMBO J. — NPG, 1987. — ISSN 0261-4189; 1460-2075 — doi:10.1002/(ISSN)1460-2075 — PMID:3443096
  5. ↑ 5,0 5,1 5,2 5,3 5,4 5,5 Kobayashi K, Morita S, Mizuguchi T et al. Functional and high level expression of human dopamine beta-hydroxylase in transgenic mice // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1994. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:7961964
  6. ↑ Harris P., Zhao Y., Walter T. S. et al. The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution // Sci. Adv. / M. McNutt — AAAS, 2016. — ISSN 2375-2548 — doi:10.1126/SCIADV.1500980 — PMID:27152332
  7. ↑ Harris P., Zhao Y., Walter T. S. et al. The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution // Sci. Adv. / M. McNutt — AAAS, 2016. — ISSN 2375-2548 — doi:10.1126/SCIADV.1500980 — PMID:27152332
  8. ↑ 8,0 8,1 8,2 8,3 8,4 8,5 Kobayashi K, Morita S, Mizuguchi T et al. Functional and high level expression of human dopamine beta-hydroxylase in transgenic mice // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1994. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:7961964
  9. ↑ 9,0 9,1 9,2 9,3 9,4 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform. — OUP, 2011. — ISSN 1467-5463; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
  10. ↑ 10,0 10,1 A Lamouroux, A Vigny, Biguet N. F. et al. The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme // EMBO J. — NPG, 1987. — ISSN 0261-4189; 1460-2075 — doi:10.1002/(ISSN)1460-2075 — PMID:3443096
  11. ↑ Pounds J. G. The human plasma proteome: a nonredundant list developed by combination of four separate sources // Mol. Cell. Proteomics — American Society for Biochemistry and Molecular Biology, 2004. — ISSN 1535-9476; 1535-9484 — doi:10.1074/MCP.M300127-MCP200 — PMID:14718574
  12. ↑ A J Man in 't Veld, F Boomsma, P Moleman et al. Congenital dopamine-beta-hydroxylase deficiency. A novel orthostatic syndrome // Lancet / R. Horton — Elsevier, 1987. — ISSN 0140-6736; 1474-547X — doi:10.1016/S0140-6736(87)90002-X — PMID:2880016
  13. ↑ Barrie E. S., Mezher A. Human Bacterial Artificial Chromosome (BAC) Transgenesis Fully Rescues Noradrenergic Function in Dopamine β-Hydroxylase Knockout Mice // PLOS ONE / PLOS ONE Editors — PLoS, 2016. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0154864 — PMID:27148966
  14. ↑ Barrie E. S., Mezher A. Human Bacterial Artificial Chromosome (BAC) Transgenesis Fully Rescues Noradrenergic Function in Dopamine β-Hydroxylase Knockout Mice // PLOS ONE / PLOS ONE Editors — PLoS, 2016. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0154864 — PMID:27148966
  15. ↑ Thomas S. A., Palmiter R. D. Thermoregulatory and metabolic phenotypes of mice lacking noradrenaline and adrenaline // Nature / M. Skipper — NPG, Springer Science+Business Media, 1997. — ISSN 1476-4687; 0028-0836 — doi:10.1038/387094A0 — PMID:9139828
  16. ↑ IUPHAR/BPS Guide to PHARMACOLOGY
  17. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  18. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)


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