MOXD1

MOXD1
Identifikatori
Aliasi	MOXD1
Vanjski ID-jevi	OMIM: 609000 MGI: 1921582 HomoloGene: 22904 GeneCards: MOXD1
Lokacija gena (čovjek)
Hrom.	Hromosom 6 (čovjek)
Kraj	132,401,475 bp
Lokacija gena (miš)
Hrom.	Hromosom 10 (miš)
Kraj	24,178,688 bp
Ontologija gena
Molekularna funkcija	• monooxygenase activity; • oxidoreductase activity; • GO:0001948, GO:0016582 vezivanje za proteine; • catalytic activity; • vezivanje iona metala; • copper ion binding; • dopamine beta-monooxygenase activity; • 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;
Ćelijska komponenta	• integral component of membrane; • endoplasmic reticulum membrane; • Endoplazmatski retikulum; • membrana; • Vanćelijsko; • secretory granule membrane; • citoplazma;
Biološki proces	• octopamine biosynthetic process; • dopamine catabolic process; • norepinephrine biosynthetic process;
	Izvori:Amigo / QuickGO
Ortolozi
	26002
	59012
	ENSG00000079931
	ENSMUSG00000020000
	Q6UVY6
	Q9CXI3
	NM_015529
	NM_021509
	NP_056344
	NP_067484
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Protein 1 DBH-olike monooksigenaze, znan i kao monooksigenaza X, jest enzim koji je kod ljudi kodiran genom MOXD1.^[5]^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 613 aminokiselina, а molekulska težina 69.652 Da.^[7]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MCCWPLLLLW	GLLPGTAAGG	SGRTYPHRTL	LDSEGKYWLG	WSQRGSQIAF
RLQVRTAGYV	GFGFSPTGAM	ASADIVVGGV	AHGRPYLQDY	FTNANRELKK
DAQQDYHLEY	AMENSTHTII	EFTRELHTCD	INDKSITDST	VRVIWAYHHE
DAGEAGPKYH	DSNRGTKSLR	LLNPEKTSVL	STALPYFDLV	NQDVPIPNKD
TTYWCQMFKI	PVFQEKHHVI	KVEPVIQRGH	ESLVHHILLY	QCSNNFNDSV
LESGHECYHP	NMPDAFLTCE	TVIFAWAIGG	EGFSYPPHVG	LSLGTPLDPH
YVLLEVHYDN	PTYEEGLIDN	SGLRLFYTMD	IRKYDAGVIE	AGLWVSLFHT
IPPGMPEFQS	EGHCTLECLE	EALEAEKPSG	IHVFAVLLHA	HLAGRGIRLR
HFRKGKEMKL	LAYDDDFDFN	FQEFQYLKEE	QTILPGDNLI	TECRYNTKDR
AEMTWGGLST	RSEMCLSYLL	YYPRINLTRC	ASIPDIMEQL	QFIGVKEIYR
PVTTWPFIIK	SPKQYKNLSF	MDAMNKFKWT	KKEGLSFNKL	VLSLPVNVRC
SKTDNAEWSI	QGMTALPPDI	ERPYKAEPLV	CGTSSSSSLH	RDFSINLLVC
LLLLSCTLST	KSL

Funkcija

DBH-oliki protein 1 održava mnoge strukturna obilježja dopamin beta-monooksigenaza DBH.^[8] Budući da je peptidil glicin alfa-hidroksilirajuća monooksigenaza (PHM; EC 1.14.17.3) homologna dopamin beta-monooksigenazi (DBM; EC 1.14.17.1)^[9] ovo se odnosi na strukturnu osnovu za novu porodicu bakarni tip II, značajno specifičnu za monooksigenaze ovisne od askorbata.^[9] na osnovu odgovarajućeg mišjeg homologa.^[6] Put sinteze kateholamina je moguće vezivanje kateholamina za metabolički bakar.^[10] enzimski domen, svojstvo nalik neuronskom koje kodira MOX bez signalne sekvence [metabolizam|[metabolizma]] enzima koji rješava monooksigenazni X hemijski put ^[10] nepoznatog supstrata,^[6] egzogeni MOX se ne izlučuje i lokalizira se u cijelom endoplazmatskom retikulumu,^[11] i u endokrinim i/ili u neendokrinim ćelijama.^[10]

Klinički značaj

Nedostatak DBH efikasno je liječen L-treo-3,4-dihidroksifenilserinom (DOPS).^[12]

Također gledajte

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000079931 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020000 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: monooxygenase, DBH-like 1".
^ ^a ^b ^c Chambers KJ, Tonkin LA, Chang E, Shelton DN, Linskens MH, Funk WD (septembar 1998). "Identification and cloning of a sequence homologue of dopamine beta-hydroxylase" (PDF). Gene. 218 (1–2): 111–20. doi:10.1016/S0378-1119(98)00344-8. PMID 9751809.
^ "UniProt, Q6UVY6" (jezik: engleski). Pristupljeno 9. 10. 2021.
^ Prigge ST, Mains RE, Eipper BA, Amzel LM (august 2000). "New insights into copper monooxygenases and peptide amidation: structure, mechanism and function". Cell Mol Life Sci. 57 (8–9): 1236–59. doi:10.1007/PL00000763. ISSN 1420-682X. PMID 11028916. S2CID 12738480.
^ ^a ^b Southan C, Kruse LI (septembar 1989). "Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain". FEBS Lett. 255 (1): 116–20. doi:10.1016/0014-5793(89)81072-5. PMID 2792366. S2CID 84464131.
^ ^a ^b ^c Xin X, Mains RE, Eipper BA (novembar 2004). "Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum". J. Biol. Chem. 279 (46): 48159–67. doi:10.1074/jbc.M407486200. PMID 15337741.
^ Greška kod citiranja: Nevaljana oznaka <ref>; nije naveden tekst za reference s imenom pmid15337741|
^ Vincent S, Robertson D (maj 2002). "The broader view: catecholamine abnormalities". Clin Auton Res. Suppl. 1 (7): 144–9. doi:10.1007/s102860200018. ISSN 0959-9851. PMID 12102462. S2CID 28678929.

Dopunska literatura

Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
Xin X, Mains RE, Eipper BA (2004). "Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum". J. Biol. Chem. 279 (46): 48159–67. doi:10.1074/jbc.M407486200. PMID 15337741.
Bon S, Lamouroux A, Vigny A, Massoulié J, Mallet J, Henry JP (oktobar 1991). "Amphiphilic and nonamphiphilic forms of bovine and human dopamine beta-hydroxylase". J. Neurochem. 57 (4): 1100–11. doi:10.1111/j.1471-4159.1991.tb08267.x. ISSN 0022-3042. PMID 1654385. S2CID 85087782.

Vanjski linkovi

Portal Biologija

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000079931 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020000 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: monooxygenase, DBH-like 1".

[pmid9751809-6] Chambers KJ, Tonkin LA, Chang E, Shelton DN, Linskens MH, Funk WD (septembar 1998). "Identification and cloning of a sequence homologue of dopamine beta-hydroxylase" (PDF). Gene. 218 (1–2): 111–20. doi:10.1016/S0378-1119(98)00344-8. PMID 9751809.

[UniProt-7] "UniProt, Q6UVY6" (jezik: engleski). Pristupljeno 9. 10. 2021.

[pmid11028916-8] Prigge ST, Mains RE, Eipper BA, Amzel LM (august 2000). "New insights into copper monooxygenases and peptide amidation: structure, mechanism and function". Cell Mol Life Sci. 57 (8–9): 1236–59. doi:10.1007/PL00000763. ISSN 1420-682X. PMID 11028916. S2CID 12738480.

[pmid2792366-9] Southan C, Kruse LI (septembar 1989). "Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain". FEBS Lett. 255 (1): 116–20. doi:10.1016/0014-5793(89)81072-5. PMID 2792366. S2CID 84464131.

[pmid15337741-10] Xin X, Mains RE, Eipper BA (novembar 2004). "Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum". J. Biol. Chem. 279 (46): 48159–67. doi:10.1074/jbc.M407486200. PMID 15337741.

[pmid15337741|-11] Greška kod citiranja: Nevaljana oznaka <ref>; nije naveden tekst za reference s imenom pmid15337741|

[pmid12102462-12] Vincent S, Robertson D (maj 2002). "The broader view: catecholamine abnormalities". Clin Auton Res. Suppl. 1 (7): 144–9. doi:10.1007/s102860200018. ISSN 0959-9851. PMID 12102462. S2CID 28678929.

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