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| ImageFile=S-Adenosyl-L-homocystein.svg
| ImageFile=S-Adenosyl-L-homocystein.svg
| ImageSize= 300px
| ImageSize= 300px
| IUPACName= ''S''-(5'-Deoxyadenos-5'-yl)-<small>L</small>-homocysteine
| IUPACName=''S''-(5′-Deoxyadenos-5′-yl)-<small>L</small>-homocysteine
| 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
| OtherNames=AdoHcy, 2-''S''-adenosyl-<small>L</small>-homocysteine,<br>5'-''S''-(3-Amino-3-carboxypropyl)-5'-thioadenosine
| OtherNames=AdoHcy, 2-''S''-adenosyl-<small>L</small>-homocysteine,<br>5′-''S''-(3-Amino-3-carboxypropyl)-5′-thioadenosine
''S''-adenosylhomocysteine, SAH
''S''-adenosylhomocysteine, SAH
|Section1={{Chembox Identifiers
|Section1={{Chembox Identifiers
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| CASNo_Ref = {{cascite|correct|CAS}}
| CASNo_Ref = {{cascite|correct|CAS}}
| CASNo=979-92-0
| CASNo=979-92-0
| UNII_Ref = {{fdacite|correct|FDA}}
| UNII = 8K31Q2S66S
| ChEMBL_Ref = {{ebicite|correct|EBI}}
| ChEMBL_Ref = {{ebicite|correct|EBI}}
| ChEMBL = 418052
| ChEMBL = 418052
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| Formula=
| Formula=
| C=14 | H=20 | N=6 | O=5 | S=1
| C=14 | H=20 | N=6 | O=5 | S=1
| MolarMass=384.412
| Appearance=
| Appearance=
| Density=
| Density=
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}}
}}


'''''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]].
'''''S''-Adenosyl-<small>L</small>-homocysteine''' ('''SAH''') is an [[amino acid]] derivative used in several metabolic pathways in most organisms. It is an intermediate in the synthesis of [[cysteine]] and [[adenosine]].<ref>{{cite journal|url=https://academic.oup.com/jn/article/132/8/2361S/4687579|doi=10.1093/jn/132.8.2361S|pmid=12163693|title=Elevation in S-Adenosylhomocysteine and DNA Hypomethylation: Potential Epigenetic Mechanism for Homocysteine-Related Pathology|journal=The Journal of Nutrition|volume=132|issue=8|pages=2361S–2366S|year=2002|last1=James|first1=S. Jill|last2=Melnyk|first2=Stepan|last3=Pogribna|first3=Marta|last4=Pogribny|first4=Igor P|last5=Caudill|first5=Marie A}}</ref>


== Biological role ==
SAH is formed by the [[demethylation]] of [[S-Adenosyl methionine|''S''-adenosyl-<small>L</small>-methionine]] and is converted to homocysteine and adenosine by [[adenosylhomocysteinase]].
[[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>


==References==
== References ==
{{Reflist}}
{{Reflist}}


==External links==
== External links ==
*[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]]
[[Category:Purines]]
[[Category:Purines]]
[[Category:Alpha-Amino acids]]
[[Category:Amino acid derivatives]]
[[Category:Amino acid derivatives]]


Latest revision as of 17:10, 17 September 2023

S-Adenosyl-L-homocysteine
Names
IUPAC name
S-(5′-Deoxyadenos-5′-yl)-L-homocysteine
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)
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.012.328 Edit this at Wikidata
KEGG
MeSH S-Adenosylhomocysteine
UNII
  • InChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1 checkY
    Key: ZJUKTBDSGOFHSH-WFMPWKQPSA-N checkY
  • InChI=1/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
    Key: ZJUKTBDSGOFHSH-WFMPWKQPBX
  • O=C(O)[C@@H](N)CCSC[C@H]3O[C@@H](n2cnc1c(ncnc12)N)[C@H](O)[C@@H]3O
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).
checkY verify (what is checkY☒N ?)

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]
  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.
  5. ^ 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.
[edit]
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