Escherichia coli K-12 substr. MG1655 Compound: spermidine

Synonyms: N-(3-aminopropyl)butane-1,4-diamine

Superclasses: an amine an aliphatic amine an aliphatic diamine an aliphatic alpha,omega-diamine

Chemical Formula: C7H22N3

Molecular Weight: 148.27 Daltons

Monoisotopic Molecular Weight: 145.1578976255 Daltons

spermidine compound structure


InChI: InChI=1S/C7H19N3/c8-4-1-2-6-10-7-3-5-9/h10H,1-9H2/p+3


Unification Links: CAS:124-20-9 , ChEBI:57834 , ChemSpider:5360248 , HMDB:HMDB01257 , IAF1260:34593 , KEGG:C00315 , MetaboLights:MTBLC57834 , PubChem:6992097

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): 4.79

Reactions known to consume the compound:

glutathionylspermidine biosynthesis :
spermidine + glutathione + ATP → glutathionylspermidine + ADP + phosphate + H+

Not in pathways:
acetyl-CoA + spermidineN1-acetylspermidine + coenzyme A + H+

Not in pathways:
an aliphatic amine[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] → an aldehyde[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

Reactions known to produce the compound:

spermidine biosynthesis I :
putrescine + S-adenosyl 3-(methylthio)propylamine → spermidine + S-methyl-5'-thioadenosine + H+

Not in pathways:
glutathionylspermidine + H2O → glutathione + spermidine

Reactions known to both consume and produce the compound:

Not in pathways:
an aliphatic α,ω-diamine + 2-oxoglutarate ↔ an aliphatic ω-aminoaldehyde + L-glutamate

In Reactions of unknown directionality:

Not in pathways:
an aliphatic α,ω-diamine + acetyl-CoA = an aliphatic N-acetyl-diamine + coenzyme A + H+

In Transport reactions:
spermidine[cytosol] + H+[periplasmic space]spermidine[periplasmic space] + H+[cytosol] ,
ATP + spermidine[periplasmic space] + H2O → ADP + spermidine[cytosol] + phosphate + H+

Enzymes activated by spermidine, sorted by the type of activation, are:

Activator (Mechanism unknown) of: acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase [Vallari82]

Enzymes inhibited by spermidine, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: ornithine decarboxylase [Applebaum77] , arginine decarboxylase, degradative [Blethen68]

Inhibitor (Mechanism unknown) of: spermidine synthase [Bowman73, Comment 1] , arginine decarboxylase, biosynthetic [Wu73, Comment 2] , adenosylmethionine decarboxylase [Tabor85, Kashiwagi88] , dihydrofolate reductase [Baccanari75] , lysine decarboxylase [Wertheimer83]

This compound has been characterized as an alternative substrate of the following enzymes: putrescine aminotransferase , diamine transaminase , spermidine synthase

Activates: AtoS monomer + ATP → AtoS-P + ADP

Regulated Transcription Units (1 total): ?


Transcription-unit diagram


Applebaum77: Applebaum DM, Dunlap JC, Morris DR (1977). "Comparison of the biosynthetic and biodegradative ornithine decarboxylases of Escherichia coli." Biochemistry 1977;16(8);1580-4. PMID: 15587

Baccanari75: Baccanari D, Phillips A, Smith S, Sinski D, Burchall J (1975). "Purification and properties of Escherichia coli dihydrofolate reductase." Biochemistry 1975;14(24);5267-73. PMID: 46

Blethen68: Blethen SL, Boeker EA, Snell EE (1968). "Argenine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme." J Biol Chem 1968;243(8);1671-7. PMID: 4870599

Bowman73: Bowman WH, Tabor CW, Tabor H (1973). "Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli." J Biol Chem 1973;248(7);2480-6. PMID: 4572733

Kashiwagi88: Kashiwagi K, Igarashi K (1988). "Adjustment of polyamine contents in Escherichia coli." J Bacteriol 170(7);3131-5. PMID: 3290196

Tabor83: Tabor CW, Tabor H (1983). "Putrescine aminopropyltransferase (Escherichia coli)." Methods Enzymol 1983;94;265-70. PMID: 6312268

Tabor85: Tabor CW, Tabor H (1985). "Polyamines in microorganisms." Microbiol Rev 1985;49(1);81-99. PMID: 3157043

Vallari82: Vallari DS, Rock CO (1982). "Role of spermidine in the activity of sn-glycerol-3-phosphate acyltransferase from Escherichia coli." Arch Biochem Biophys 1982;218(2);402-8. PMID: 6760815

Wertheimer83: Wertheimer SJ, Leifer Z (1983). "Putrescine and spermidine sensitivity of lysine decarboxylase in Escherichia coli: evidence for a constitutive enzyme and its mode of regulation." Biochem Biophys Res Commun 114(2);882-8. PMID: 6349639

Wu73: Wu WH, Morris DR (1973). "Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties." J Biol Chem 1973;248(5);1687-95. PMID: 4571773

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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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