S-Adenosyl-L-homocysteine: Difference between revisions
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| verifiedrevid = 460764948 |
| verifiedrevid = 460764948 |
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| Name=''S''-Adenosyl- |
| Name=''S''-Adenosyl-<small>L</small>-homocysteine |
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| ImageFile=S-Adenosyl-L-homocystein.svg |
| ImageFile=S-Adenosyl-L-homocystein.svg |
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| ImageSize= 300px |
| ImageSize= 300px |
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| IUPACName= |
| IUPACName=''S''-(5′-Deoxyadenos-5′-yl)-<small>L</small>-homocysteine |
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| SystematicName=(2''S'')-2-Amino-4-({[(2''S'',3''S'',4''R'',5''R'')-5-(6-amino-9''H''-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}sulfanyl)butanoic acid |
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| OtherNames=AdoHcy, 2-''S''-adenosyl- |
| OtherNames=AdoHcy, 2-''S''-adenosyl-<small>L</small>-homocysteine,<br>5′-''S''-(3-Amino-3-carboxypropyl)-5′-thioadenosine |
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''S''-adenosylhomocysteine, SAH |
''S''-adenosylhomocysteine, SAH |
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|Section1={{Chembox Identifiers |
|Section1={{Chembox Identifiers |
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| CASNo_Ref = {{cascite|correct|CAS}} |
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| CASNo=979-92-0 |
| CASNo=979-92-0 |
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| UNII_Ref = {{fdacite|correct|FDA}} |
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| UNII = 8K31Q2S66S |
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| ChEMBL_Ref = {{ebicite|correct|EBI}} |
| ChEMBL_Ref = {{ebicite|correct|EBI}} |
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| ChEMBL = 418052 |
| ChEMBL = 418052 |
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| Formula= |
| Formula= |
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| C=14 | H=20 | N=6 | O=5 | S=1 |
| C=14 | H=20 | N=6 | O=5 | S=1 |
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| MolarMass=384.412 |
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| Appearance= |
| Appearance= |
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'''''S''-Adenosyl- |
'''''S''-Adenosyl-<small>L</small>-homocysteine''' ('''SAH''') is the [[biosynthetic]] precursor to [[homocysteine]].<ref>{{cite journal | vauthors = Finkelstein JD | title = Pathways and regulation of homocysteine metabolism in mammals | journal = Seminars in Thrombosis and Hemostasis | volume = 26 | issue = 3 | pages = 219–225 | year = 2000 | pmid = 11011839 | doi = 10.1055/s-2000-8466 }}</ref> SAH is formed by the [[demethylation]] of [[S-Adenosyl methionine|''S''-adenosyl-<small>L</small>-methionine]].<ref>{{cite journal | vauthors = Ribbe MW, Hu Y, Hodgson KO, Hedman B | title = Biosynthesis of nitrogenase metalloclusters | journal = Chemical Reviews | volume = 114 | issue = 8 | pages = 4063–4080 | date = April 2014 | pmid = 24328215 | pmc = 3999185 | doi = 10.1021/cr400463x }}</ref><ref>{{cite journal | vauthors = James SJ, Melnyk S, Pogribna M, Pogribny IP, Caudill MA | title = Elevation in S-adenosylhomocysteine and DNA hypomethylation: potential epigenetic mechanism for homocysteine-related pathology | journal = The Journal of Nutrition | volume = 132 | issue = 8 Suppl | pages = 2361S–2366S | date = August 2002 | pmid = 12163693 | doi = 10.1093/jn/132.8.2361S | doi-access = free }}</ref> [[Adenosylhomocysteinase]] converts SAH into homocysteine and [[adenosine]]. |
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== Biological role == |
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⚫ | |||
[[DNA methyltransferase]]s are inhibited by SAH.<ref>{{cite journal | vauthors = Kumar R, Srivastava R, Singh RK, Surolia A, Rao DN | title = Activation and inhibition of DNA methyltransferases by S-adenosyl-L-homocysteine analogues | journal = Bioorganic & Medicinal Chemistry | volume = 16 | issue = 5 | pages = 2276–2285 | date = March 2008 | pmid = 18083524 | doi = 10.1016/j.bmc.2007.11.075 }}</ref> Two ''S''-adenosyl-<small>L</small>-homocysteine [[Cofactor (biochemistry)|cofactor]] products can bind the active site of DNA methyltransferase 3B and prevent the DNA duplex from binding to the [[active site]], which inhibits [[DNA methylation]].<ref>{{cite journal | vauthors = Lin CC, Chen YP, Yang WZ, Shen JC, Yuan HS | title = Structural insights into CpG-specific DNA methylation by human DNA methyltransferase 3B | journal = Nucleic Acids Research | volume = 48 | issue = 7 | pages = 3949–3961 | date = April 2020 | pmid = 32083663 | pmc = 7144912 | doi = 10.1093/nar/gkaa111 }}</ref> |
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⚫ | |||
{{Reflist}} |
{{Reflist}} |
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==External links== |
== External links == |
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*[http://biocyc.org/ECOLI/NEW-IMAGE?type=COMPOUND&object=ADENOSYL-HOMO-CYS BioCYC E.Coli K-12 Compound: S-adenosyl-L-homocysteine] |
*[http://biocyc.org/ECOLI/NEW-IMAGE?type=COMPOUND&object=ADENOSYL-HOMO-CYS BioCYC E.Coli K-12 Compound: S-adenosyl-L-homocysteine] |
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[[Category:Nucleosides]] |
[[Category:Nucleosides]] |
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[[Category:Purines]] |
[[Category:Purines]] |
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[[Category:Alpha-Amino acids]] |
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[[Category:Amino acid derivatives]] |
[[Category:Amino acid derivatives]] |
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Latest revision as of 17:10, 17 September 2023
Names | |
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IUPAC name
S-(5′-Deoxyadenos-5′-yl)-L-homocysteine
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Systematic IUPAC name
(2S)-2-Amino-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}sulfanyl)butanoic acid | |
Other names
AdoHcy, 2-S-adenosyl-L-homocysteine,
5′-S-(3-Amino-3-carboxypropyl)-5′-thioadenosine S-adenosylhomocysteine, SAH | |
Identifiers | |
3D model (JSmol)
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ChEBI | |
ChEMBL | |
ChemSpider | |
ECHA InfoCard | 100.012.328 |
KEGG | |
MeSH | S-Adenosylhomocysteine |
PubChem CID
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UNII | |
CompTox Dashboard (EPA)
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Properties | |
C14H20N6O5S | |
Molar mass | 384.41 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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S-Adenosyl-L-homocysteine (SAH) is the biosynthetic precursor to homocysteine.[1] SAH is formed by the demethylation of S-adenosyl-L-methionine.[2][3] Adenosylhomocysteinase converts SAH into homocysteine and adenosine.
Biological role
[edit]DNA methyltransferases are inhibited by SAH.[4] Two S-adenosyl-L-homocysteine cofactor products can bind the active site of DNA methyltransferase 3B and prevent the DNA duplex from binding to the active site, which inhibits DNA methylation.[5]
References
[edit]- ^ Finkelstein JD (2000). "Pathways and regulation of homocysteine metabolism in mammals". Seminars in Thrombosis and Hemostasis. 26 (3): 219–225. doi:10.1055/s-2000-8466. PMID 11011839.
- ^ Ribbe MW, Hu Y, Hodgson KO, Hedman B (April 2014). "Biosynthesis of nitrogenase metalloclusters". Chemical Reviews. 114 (8): 4063–4080. doi:10.1021/cr400463x. PMC 3999185. PMID 24328215.
- ^ James SJ, Melnyk S, Pogribna M, Pogribny IP, Caudill MA (August 2002). "Elevation in S-adenosylhomocysteine and DNA hypomethylation: potential epigenetic mechanism for homocysteine-related pathology". The Journal of Nutrition. 132 (8 Suppl): 2361S–2366S. doi:10.1093/jn/132.8.2361S. PMID 12163693.
- ^ Kumar R, Srivastava R, Singh RK, Surolia A, Rao DN (March 2008). "Activation and inhibition of DNA methyltransferases by S-adenosyl-L-homocysteine analogues". Bioorganic & Medicinal Chemistry. 16 (5): 2276–2285. doi:10.1016/j.bmc.2007.11.075. PMID 18083524.
- ^ Lin CC, Chen YP, Yang WZ, Shen JC, Yuan HS (April 2020). "Structural insights into CpG-specific DNA methylation by human DNA methyltransferase 3B". Nucleic Acids Research. 48 (7): 3949–3961. doi:10.1093/nar/gkaa111. PMC 7144912. PMID 32083663.