Эчтәлеккә күчү

DBH

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/DBH latin yazuında])
DBH
Нинди таксонда бар H. sapiens[d][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], intracellular membrane-bounded organelle[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]

  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; 1460-2075doi:10.1002/(ISSN)1460-2075PMID: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. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1994. — ISSN 0021-9258; 1083-351X; 1067-8816PMID: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. McNuttAAAS, 2016. — ISSN 2375-2548doi:10.1126/SCIADV.1500980PMID: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. McNuttAAAS, 2016. — ISSN 2375-2548doi:10.1126/SCIADV.1500980PMID: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. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1994. — ISSN 0021-9258; 1083-351X; 1067-8816PMID: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; 1477-4054doi:10.1093/BIB/BBR042PMID: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; 1460-2075doi:10.1002/(ISSN)1460-2075PMID:3443096
  11. Pounds J. G. The human plasma proteome: a nonredundant list developed by combination of four separate sources // Mol. Cell. ProteomicsAmerican Society for Biochemistry and Molecular Biology, 2004. — ISSN 1535-9476; 1535-9484doi:10.1074/MCP.M300127-MCP200PMID: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. HortonElsevier BV, 1987. — ISSN 0140-6736; 1474-547Xdoi:10.1016/S0140-6736(87)90002-XPMID: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 EditorsPLoS, 2016. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0154864PMID: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 EditorsPLoS, 2016. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0154864PMID:27148966
  15. Thomas S. A., Palmiter R. D. Thermoregulatory and metabolic phenotypes of mice lacking noradrenaline and adrenaline // Nature / M. SkipperNPG, Springer Science+Business Media, 1997. — ISSN 1476-4687; 0028-0836doi:10.1038/387094A0PMID:9139828
  16. IUPHAR/BPS Guide to PHARMACOLOGY
  17. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  18. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.
  • 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.)