Compound: N6-Methyladenosine
SMILES: O1[C@@H](n2c3ncnc(c3nc2)NC)[C@H](O)[C@@H]([C@H]1CO)O
InChIKey: VQAYFKKCNSOZKM-IOSLPCCCSA-N
Synonyms: N6-Methyladenosine, 1867-73-8, N-Methyladenosine, 6-Methyladenosine, N(6)-Methyladenosine, 6-Methylaminopurinosine, 6-Methylaminopurine riboside, N6-methyladenosine (m6A), 6-Methylaminopurine D-riboside, 6-Methylaminopurine ribonucleoside, NSC-29409, CHEBI:21891, CLE6G00625, DTXSID6020858, (2R,3S,4R,5R)-2-(hydroxymethyl)-5-[6-(methylamino)-9H-purin-9-yl]oxolane-3,4-diol, N(6)mAdo, (2R,3S,4R,5R)-2-(hydroxymethyl)-5-(6-(methylamino)-9H-purin-9-yl)oxolane-3,4-diol, RefChem:927418, DTXCID20858, Adenosine, N-methyl-, (2R,3S,4R,5R)-2-(Hydroxymethyl)-5-(6-(methylamino)-9H-purin-9-yl)tetrahydrofuran-3,4-diol, MFCD00005739, (N-6)-Methyladenosine, M6A, (2R,3S,4R,5R)-2-(hydroxymethyl)-5-[6-(methylamino)purin-9-yl]oxolane-3,4-diol, CHEMBL383144, 6-Methylamino-9-beta-D-ribofuranosylpurine, (2R,3S,4R,5R)-2-(hydroxymethyl)-5-[6-(methylamino)purin-9-yl]tetrahydrofuran-3,4-diol, (2R,3S,4R,5R)-2-Hydroxymethyl-5-(6-methylamino-purin-9-yl)-tetrahydro-furan-3,4-diol, 6-Methyladenosine;N-Methyladenosine, UNII-CLE6G00625, NSC627045, 4rdn, 6MD, Prestwick_343, 6-Methylaminopurine 9-ribofuranoside, N6 -methyladenosine, N(6)-monomethyladenosine, Prestwick0_000338, Prestwick1_000338, Prestwick2_000338, Prestwick3_000338, adenosine, N(6)-methyl-, Epitope ID:140951, SCHEMBL40634, BSPBio_000375, MLS002153780, SPBio_002296, BPBio1_000413, orb1300626, VQAYFKKCNSOZKM-IOSLPCCCSA-N, GLXC-20834, HMS1569C17, HMS2096C17, HMS2234N05, HMS3713C17, HY-N0086, (-)-6-(Methylamino)purine riboside, BDBM50163023, EBC-50093, PDSP1_001030, PDSP2_001014, s3190, AKOS024260287, CCG-220338, CS-3285, GS-6701, MSK167094-1000AW, NM32281, NCGC00162241-01, NCGC00162241-02, NCGC00162241-04, NCGC00162241-09, BP-58658, DA-65904, SMR001233164, SY102619, 6-Methylamino-9-|_-D-ribofuranosylpurine, 6-methylamino-9-beta-D-ribofuranosyl-Purine, ST50412061, SW196617-3, 6-methylamino-9-beta-delta-ribofuranosyl-Purine, EN300-255003, F12902, Purine, 6-methylamino-9-beta-D-ribofuranosyl-, F384967, Q6951996, BRD-K81807412-001-03-1, BRD-K81807412-001-10-6, Z2088406258, N6-Methyladenosine Solution in Acetonitrile/Water, 1000ug/mL, (4S,2R,3R,5R)-5-(hydroxymethyl)-2-[6-(methylamino)purin-9-yl]oxolane-3,4-diol
Theoretical properties:
molecular_formula: C11H15N5O4
molecular_weight: 281.27 g/mol
exact_mass: 281.11240398 g/mol
formal_charge: 0
hydrogen_bond_donor_count: 4
hydrogen_bond_acceptor_count: 8
rotatable_bond_count: 3
heavy_atom_count: 20
topological_polar_surface_area: 126 Å²
isotope_atom_count: 0
covalently_bonded_unit_count: 1
Physical properties:
Descriptions:
{"pubchem": "N(6)-methyladenosine is a methyladenosine compound with one methyl group attached to N6 of the adenine nucleobase.", "chebi": "A methyladenosine compound with one methyl group attached to N<small><sup>6</small></sup> of the adenine nucleobase.", "chembl": "Unnamed Compound is a small molecule listed in the ChEMBL database but has not progressed to an approved clinical phase.", "wikipedia": "N6-Methyladenosine (m6A) was originally identified and partially characterised in the 1970s, and is an abundant modification in mRNA and DNA. It is found within some viruses, and most eukaryotes including mammals, insects, plants and yeast. It is also found in tRNA, rRNA, and small nuclear RNA (snRNA) as well as several long non-coding RNA, such as Xist.\nThe methylation of adenosine (on RNA) is directed by a large m6A methyltransferase complex containing METTL3, which is the subunit that binds S-adenosyl-L-methionine (SAM). In vitro, this methyltransferase complex preferentially methylates RNA oligonucleotides containing GGACU and a similar preference was identified in vivo in mapped m6A sites in Rous sarcoma virus genomic RNA and in bovine prolactin mRNA. More recent studies have characterized other key components of the m6A methyltransferase complex in mammals, including METTL14, Wilms tumor 1 associated protein (WTAP), VIRMA and METTL5. Following a 2010 speculation of m6A in mRNA being dynamic and reversible, the discovery of the first m6A demethylase, fat mass and obesity-associated protein (FTO) in 2011 confirmed this hypothesis and revitalized the interests in the study of m6A. A second m6A demethylase alkB homolog 5 (ALKBH5) was later discovered as well.\nThe biological functions of m6A are mediated through a group of RNA binding proteins that specifically recognize the methylated adenosine on RNA. These binding proteins are named m6A readers. The YT521-B homology (YTH) domain family of proteins (YTHDF1, YTHDF2, YTHDF3 and YTHDC1) have been characterized as direct m6A readers and have a conserved m6A-binding pocket. Insulin-like growth factor-2 mRNA-binding proteins 1, 2, and 3 (IGF2BP1\u20133) are reported as a novel class of m6A readers. IGF2BPs use K homology (KH) domains to selectively recognize m6A-containing RNAs and promote their translation and stability. These m6A readers, together with m6A methyltransferases (writers) and demethylases (erasers), establish a complex mechanism of m6A regulation in which writers and erasers determine the distributions of m6A on RNA, whereas readers mediate m6A-dependent functions. m6A has also been shown to mediate a structural switch termed m6A switch. \nThe specificity of m6A installation on mRNA is controlled by exon architecture and exon junction complexes. Exon junction complexes suppress m6A methylation near exon-exon junctions by packaging nearby RNA and protecting it from methylation by the m6A methyltransferase complex. m6A regions in long internal and terminal exons, away from exon-exon junctions and exon junction complexes, escape suppression and can be methylated by the methyltransferase complex.\nIn eukaryotes, m6dA (DNA) is enriched in transcriptionally permissive regions, colocalizing with H3K4me3 nucleosomes. Production of m6dA is mediated by AMT1 (MTA1) and AMT6/7 (MTA9), which are distantly related to the RNA-methylating enzymes. The two form a complex and are inferred to exist in the common ancestor of extant eukaryotes, but have been lost in many lineages including animals and plants."}