S-Adenosyl-L-homocysteine: Difference between revisions

S-Adenosyl-l-homocysteine
Names
	IUPAC name S-(5′-Deoxyadenos-5′-yl)-l-homocysteine
	Other names AdoHcy, 2-S-adenosyl-l-homocysteine,; 5′-S-(3-Amino-3-carboxypropyl)-5′-thioadenosine S-adenosylhomocysteine, SAH
Identifiers
CAS Number	979-92-0 ;
3D model (JSmol)	Interactive image;
ChEBI	CHEBI:16680 ;
ChEMBL	ChEMBL418052 ;
ChemSpider	388301 ;
ECHA InfoCard	100.012.328
IUPHAR/BPS	5265;
KEGG	C00021 ;
MeSH	S-Adenosylhomocysteine
PubChem CID	439155;
UNII	8K31Q2S66S ;
CompTox Dashboard (EPA)	DTXSID30895860 ;
	InChI 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 Key: ZJUKTBDSGOFHSH-WFMPWKQPSA-N ; 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;
	SMILES 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	384.412
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). verify (what is ?) Infobox references

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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.

References

^ Finkelstein, J. D. (2000). "Pathways and regulation of homocysteine metabolism in mammals". Semin. Thromb. Hemost. 26 (3): 219–25. doi:10.1055/s-2000-8466. PMID 11011839.
^ Ribbe, M. W.; Hu, Y.; Hodgson, K. O.; Hedman, B. (2014). "Biosynthesis of Nitrogenase Metalloclusters". Chem. Rev. 114 (8): 4063–4080. doi:10.1021/cr400463x. PMC 3999185. PMID 24328215.
^ James, S. Jill; Melnyk, Stepan; Pogribna, Marta; Pogribny, Igor P; Caudill, Marie A (2002). "Elevation in S-Adenosylhomocysteine and DNA Hypomethylation: Potential Epigenetic Mechanism for Homocysteine-Related Pathology". The Journal of Nutrition. 132 (8): 2361S–2366S. doi:10.1093/jn/132.8.2361S. PMID 12163693.

External links

BioCYC E.Coli K-12 Compound: S-adenosyl-L-homocysteine

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[1] Finkelstein, J. D. (2000). "Pathways and regulation of homocysteine metabolism in mammals". Semin. Thromb. Hemost. 26 (3): 219–25. doi:10.1055/s-2000-8466. PMID 11011839.

[2] Ribbe, M. W.; Hu, Y.; Hodgson, K. O.; Hedman, B. (2014). "Biosynthesis of Nitrogenase Metalloclusters". Chem. Rev. 114 (8): 4063–4080. doi:10.1021/cr400463x. PMC 3999185. PMID 24328215.

[3] James, S. Jill; Melnyk, Stepan; Pogribna, Marta; Pogribny, Igor P; Caudill, Marie A (2002). "Elevation in S-Adenosylhomocysteine and DNA Hypomethylation: Potential Epigenetic Mechanism for Homocysteine-Related Pathology". The Journal of Nutrition. 132 (8): 2361S–2366S. doi:10.1093/jn/132.8.2361S. PMID 12163693.

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-'''''S''-Adenosyl-{{sm|l}}-homocysteine''' ('''SAH''') is the [[biosynthetic]] precursor to [[homocysteine]].<ref>{{cite journal|author=Finkelstein, J. D.|year=2000|title=Pathways and regulation of homocysteine metabolism in mammals|journal=Semin. Thromb. Hemost.|volume=26|page=219–225|doi=10.1055/s-2000-8466|pmid=11011839}}</ref>  SAH is formed by the [[demethylation]] of [[S-Adenosyl methionine|''S''-adenosyl-{{sm|l}}-methionine]].<ref>{{cite journal|author1=Ribbe, M. W. |author2=Hu, Y. |author3=Hodgson, K. O. |author4=Hedman, B. |title=Biosynthesis of Nitrogenase Metalloclusters|journal=Chem. Rev.|year=2014|volume=114|issue=8 |pages=4063–4080|doi=10.1021/cr400463x|pmid=24328215 |pmc=3999185}}</ref><ref>{{cite journal|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|doi-access=free}}</ref>   [[Adenosylhomocysteinase]] converts SAH into homocysteine and [[adenosine]].
+'''''S''-Adenosyl-{{sm|l}}-homocysteine''' ('''SAH''') is the [[biosynthetic]] precursor to [[homocysteine]].<ref>{{cite journal|author=Finkelstein, J. D.|year=2000|title=Pathways and regulation of homocysteine metabolism in mammals|journal=Semin. Thromb. Hemost.|volume=26|issue=3|pages=219–25|doi=10.1055/s-2000-8466|pmid=11011839}}</ref>  SAH is formed by the [[demethylation]] of [[S-Adenosyl methionine|''S''-adenosyl-{{sm|l}}-methionine]].<ref>{{cite journal|author1=Ribbe, M. W. |author2=Hu, Y. |author3=Hodgson, K. O. |author4=Hedman, B. |title=Biosynthesis of Nitrogenase Metalloclusters|journal=Chem. Rev.|year=2014|volume=114|issue=8 |pages=4063–4080|doi=10.1021/cr400463x|pmid=24328215 |pmc=3999185}}</ref><ref>{{cite journal|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|doi-access=free}}</ref>   [[Adenosylhomocysteinase]] converts SAH into homocysteine and [[adenosine]].
 ==References==