MTR (gen)

MTR
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 2O2K, 4CCZ
Identifikatori
Aliasi	MTR
Vanjski ID-jevi	OMIM: 156570 MGI: 894292 HomoloGene: 37280 GeneCards: MTR
EC broj	2.1.1.13
Lokacija gena (čovjek) Hrom. Hromosom 1 (čovjek)[1] Bend 1q43 Početak 236,795,260 bp[1] Kraj 236,921,278 bp[1]
Lokacija gena (miš) Hrom. Hromosom 13 (miš)[2] Bend 13 A1|13 4.52 cM Početak 12,197,598 bp[2] Kraj 12,272,999 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • GO:0102674, GO:0102675 methyltransferase activity • GO:0001948, GO:0016582 vezivanje za proteine • methionine synthase activity • vezivanje iona cinka • cobalamin binding • vezivanje iona metala • aktivnost sa transferazom Ćelijska komponenta • citoplazma • citosol Biološki proces • nervous system development • pteridine-containing compound metabolic process • methionine biosynthetic process • response to axon injury • cellular amino acid biosynthetic process • cobalamin metabolic process • cellular response to nitric oxide • axon regeneration • cell metabolism • Metilacija • sulfur amino acid metabolic process Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	4548	238505
Ensembl	ENSG00000116984	ENSMUSG00000021311
UniProt	Q99707	A6H5Y3
RefSeq (mRNK)	NM_000254 NM_001291939 NM_001291940	NM_001081128
RefSeq (bjelančevina)	NP_000245 NP_001278868 NP_001278869	NP_001074597
Lokacija (UCSC)	Chr 1: 236.8 – 236.92 Mb	Chr 13: 12.2 – 12.27 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Metionin-sintaza znana i kao MS, MeSe, MTR osdgovorna za regeneraciju metionina iz homocisteina. To jest protein koji je kod ljudi kodiran genom MTR (5-metiltetrahidrofolat-homocistein metiltransferaza) sa hromosoma 1.^[5][6] Metionin-sintaza čini dio ciklusa S-adenozilmetionina (SAMe) biosinteze i regeneracije.^[7] Kod životinja ovaj enzim zahtijeva Vitamin B12 (kobalamin) kao kofaktor, dok je oblik koji se nalazi u biljkama neovisan o kobalaminu.^[8] Mikroorganizmi eksprimiraju oblike zavisne i nezavisne od kobalamina.^[8]

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000116984 - Ensembl, maj 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000021311 - 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.
5. ^ "MTR 5-methyltetrahydrofolate-homocysteine methyltransferase (Homo sapiens)". Entrez. 19. 5. 2009. Pristupljeno 24. 5. 2009.
6. ^ Li YN, Gulati S, Baker PJ, Brody LC, Banerjee R, Kruger WD (decembar 1996). "Cloning, mapping and RNA analysis of the human methionine synthase gene". Human Molecular Genetics. 5 (12): 1851–8. doi:10.1093/hmg/5.12.1851. PMID 8968735.
7. ^ Banerjee RV, Matthews RG (mart 1990). "Cobalamin-dependent methionine synthase". FASEB Journal. 4 (5): 1450–9. doi:10.1096/fasebj.4.5.2407589. hdl:2027.42/154369. PMID 2407589. S2CID 8210250.
8. ^ ^{a b} Zydowsky, T. M. (1986). "Stereochemical analysis of the methyl transfer catalyzed by cobalamin-dependent methionine synthase from Escherichia coli B". Journal of the American Chemical Society. 108 (11): 3152–3153. doi:10.1021/ja00271a081.