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Escherichia coli K-12 substr. MG1655 Compound: S-adenosyl-L-homocysteine

Abbrev Name: SAH

Synonyms: S-adenosylhomocysteine, 2-S-adenosyl-L-homocysteine, AdoHcy, 2-S-adenosyl-L-homocysteine, S-adenosyl-homocysteine, S-adenosylhomocysteine, adenosyl-homo-cys, adenosylhomocysteine, adenosylhomo-cys, SAH

Superclasses: an acidall carboxy acidsa carboxylatean amino acidan alpha amino acida non-standard alpha amino acid
an amino acid or its derivativean amino acidan alpha amino acida non-standard alpha amino acid

Chemical Formula: C14H20N6O5S

Molecular Weight: 384.41 Daltons

Monoisotopic Molecular Weight: 385.12941350579996 Daltons

<i>S</i>-adenosyl-L-homocysteine compound structure

SMILES: C(SCC3(C(O)C(O)C(N2(C1(N=CN=C(N)C=1N=C2)))O3))CC(C([O-])=O)[N+]

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


Unification Links: CAS:979-92-0, ChEBI:57856, HMDB:HMDB00939, IAF1260:33543, KEGG:C00021, MetaboLights:MTBLC57856, PubChem:25246222

Standard Gibbs Free Energy of Formation (ΔfG in kcal/mol): -121.369

Reactions known to consume the compound:

autoinducer AI-2 biosynthesis I , S-adenosyl-L-methionine cycle I :
S-adenosyl-L-homocysteine + H2O → S-ribosyl-L-homocysteine + adenine

Reactions known to produce the compound:

5-(carboxymethoxy)uridine biosynthesis :
a 5-hydroxyuridine34 in tRNA + carboxy-S-adenosyl-L-methionine → a 5-(carboxymethoxy)uridine34 in tRNA + S-adenosyl-L-homocysteine + H+

8-amino-7-oxononanoate biosynthesis I :
a malonyl-[acp] + S-adenosyl-L-methionine → a malonyl-[acp] methyl ester + S-adenosyl-L-homocysteine

autoinducer AI-2 biosynthesis I , S-adenosyl-L-methionine cycle I :
S-adenosyl-L-methionine + a demethylated methyl donor → S-adenosyl-L-homocysteine + a methylated methyl donor + H+

cyclopropane fatty acid (CFA) biosynthesis :
a [phospholipid] olefinic fatty acid + S-adenosyl-L-methionine → a [phospholipid] cyclopropane fatty acid + S-adenosyl-L-homocysteine + H+

menaquinol-8 biosynthesis :
S-adenosyl-L-methionine + demethylmenaquinol-8 → S-adenosyl-L-homocysteine + menaquinol-8 + H+

siroheme biosynthesis :
S-adenosyl-L-methionine + precorrin-1 → S-adenosyl-L-homocysteine + precorrin-2
S-adenosyl-L-methionine + uroporphyrinogen-III → S-adenosyl-L-homocysteine + precorrin-1 + H+

ubiquinol-8 biosynthesis (prokaryotic) :
2-methoxy-6-all trans-octaprenyl-2-methoxy-1,4-benzoquinol + S-adenosyl-L-methionine → 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol + S-adenosyl-L-homocysteine + H+
3-(all-trans-octaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine → 2-methoxy-6-(all-trans-octaprenyl)phenol + S-adenosyl-L-homocysteine + H+
S-adenosyl-L-methionine + 3-demethylubiquinol-8S-adenosyl-L-homocysteine + ubiquinol-8 + H+

Not in pathways:
a [protein]-α-L-glutamate + S-adenosyl-L-methionine → a [protein]-L-glutamate-O5-methyl-ester + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + TargluS-adenosyl-L-homocysteine + Targlu-Me
S-adenosyl-L-methionine + TsrgluS-adenosyl-L-homocysteine + Tsrglu-Me
S-adenosyl-L-methionine + TrggluS-adenosyl-L-homocysteine + Trgglu-Me
S-adenosyl-L-methionine + TapgluS-adenosyl-L-homocysteine + Tapglu-Me
L-homocysteine + S-adenosyl-L-methionine → L-methionine + S-adenosyl-L-homocysteine + H+
trans-aconitate + S-adenosyl-L-methionine → (E)-3-(methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine
rRNA + S-adenosyl-L-methionine → rRNA containing N6,N6-dimethyladenine + S-adenosyl-L-homocysteine
a non-methylated ribosomal protein L11 + S-adenosyl-L-methionine → a methylated ribosomal protein L11 + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + guanine527 in 16S rRNA → S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
an rRNA + S-adenosyl-L-methionine → rRNA containing 2-methyladenine + S-adenosyl-L-homocysteine
tellurite + S-adenosyl-L-methionine → methanetelluronate + S-adenosyl-L-homocysteine
guanine46 in tRNA + S-adenosyl-L-methionine → N7-methylguanine46 in tRNA + S-adenosyl-L-homocysteine
a DNA adenine + S-adenosyl-L-methionine → S-adenosyl-L-homocysteine + a DNA 6-methylaminopurine + H+
guanine2069 in 23S rRNA + S-adenosyl-L-methionine → N7-methylguanine2069 in 23S rRNA + S-adenosyl-L-homocysteine

In Reactions of unknown directionality:

Not in pathways:
a 5-L-glutamyl-[peptide][periplasm] + an amino acid[periplasm] = a 5-L-glutamyl-amino acid[periplasm] + a peptide[periplasm]

Not in pathways:
a 2-acyl 1-lyso-phosphatidylcholine + H2O = a carboxylate + sn-glycero-3-phosphocholine + H+
an aldehyde[periplasm] + FAD[periplasm] + H2O[periplasm] = a carboxylate[periplasm] + FADH2[periplasm]

In Transport reactions:
an amino acid[periplasm]an amino acid[extracellular space]

Enzymes inhibited by S-adenosyl-L-homocysteine, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: DNA adenine methyltransferase [Bergerat90], S-adenosylmethionine:tRNA ribosyltransferase-isomerase [Van03a], chemotaxis protein methyltransferase [Neidhardt96], cyclopropane fatty acyl phospholipid synthase [Grogan97, Taylor79, Guerard04], DNA-cytosine methyltransferase [Crooks84], tRNA m1G37 methyltransferase [Hjalmarsson83, Lahoud11] Inhibitor (Mechanism unknown) of: biotin synthase [Farrar10], 5'-methylthioadenosine nucleosidase [Cornell98], trans-aconitate 2-methyltransferase [Cai99], ribonucleoside-triphosphate reductase [Eliasson92]


Bergerat90: Bergerat A, Guschlbauer W (1990). "The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli." Nucleic Acids Res 18(15);4369-75. PMID: 2201947

Cai99: Cai H, Clarke S (1999). "A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli." J Biol Chem 274(19);13470-9. PMID: 10224113

Cornell98: Cornell KA, Riscoe MK (1998). "Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product." Biochim Biophys Acta 1396(1);8-14. PMID: 9524204

Crooks84: Crooks PA, Tribe MJ, Pinney RJ (1984). "Inhibition of bacterial DNA cytosine-5-methyltransferase by S-adenosyl-L-homocysteine and some related compounds." J Pharm Pharmacol 36(2);85-9. PMID: 6143811

Eliasson92: Eliasson R, Pontis E, Fontecave M, Gerez C, Harder J, Jornvall H, Krook M, Reichard P (1992). "Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli." J Biol Chem 267(35);25541-7. PMID: 1460049

Farrar10: Farrar CE, Siu KK, Howell PL, Jarrett JT (2010). "Biotin synthase exhibits burst kinetics and multiple turnovers in the absence of inhibition by products and product-related biomolecules." Biochemistry 49(46);9985-96. PMID: 20961145

Grogan97: Grogan DW, Cronan JE (1997). "Cyclopropane ring formation in membrane lipids of bacteria." Microbiol Mol Biol Rev 1997;61(4);429-41. PMID: 9409147

Guerard04: Guerard C, Breard M, Courtois F, Drujon T, Ploux O (2004). "Synthesis and evaluation of analogues of S-adenosyl-L-methionine, as inhibitors of the E. coli cyclopropane fatty acid synthase." Bioorg Med Chem Lett 14(7);1661-4. PMID: 15026045

Hjalmarsson83: Hjalmarsson KJ, Bystrom AS, Bjork GR (1983). "Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli." J Biol Chem 258(2);1343-51. PMID: 6337136

Lahoud11: Lahoud G, Goto-Ito S, Yoshida K, Ito T, Yokoyama S, Hou YM (2011). "Differentiating analogous tRNA methyltransferases by fragments of the methyl donor." RNA 17(7);1236-46. PMID: 21602303

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

Taylor79: Taylor FR, Cronan JE (1979). "Cyclopropane fatty acid synthase of Escherichia coli. Stabilization, purification, and interaction with phospholipid vesicles." Biochemistry 1979;18(15);3292-300. PMID: 380648

Van03a: Van Lanen SG, Iwata-Reuyl D (2003). "Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA)." Biochemistry 42(18);5312-20. PMID: 12731872

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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