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Contents

   



(Top)
 


1 Biological role  





2 References  





3 External links  














S-Adenosyl-L-homocysteine






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From Wikipedia, the free encyclopedia
 

(Redirected from S-adenosyl homocysteine)

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

CAS Number

3D model (JSmol)

ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.012.328 Edit this at Wikidata

IUPHAR/BPS

KEGG
MeSH S-Adenosylhomocysteine

PubChem CID

UNII

CompTox Dashboard (EPA)

  • 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

Chemical formula

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 ?)

Infobox references

S-Adenosyl-L-homocysteine (SAH) is the biosynthetic precursor to homocysteine.[1] SAH is formed by the demethylationofS-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.
  • ^ 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.
  • External links[edit]

  • t
  • e

  • Retrieved from "https://en.wikipedia.org/w/index.php?title=S-Adenosyl-L-homocysteine&oldid=1175818975"

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    This page was last edited on 17 September 2023, at 17:10 (UTC).

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