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Escherichia coli K-12 substr. MG1655 Compound: putrescine

Systematic Name: 1,4-butanediamine

Synonyms: diaminobutane, 1,4-diaminobutane, 1,4-butanediamine, tetramethylenediamine

Superclasses: an aminean aliphatic aminean aliphatic diaminean aliphatic alpha,omega-diamine


Component of: PuuR-putrescine

Chemical Formula: C4H14N2

Molecular Weight: 90.168 Daltons

Monoisotopic Molecular Weight: 90.1156984598 Daltons

putrescine compound structure

SMILES: C([N+])CCC[N+]

InChI: InChI=1S/C4H12N2/c5-3-1-2-4-6/h1-6H2/p+2

InChIKey: InChIKey=KIDHWZJUCRJVML-UHFFFAOYSA-P

Unification Links: CAS:110-60-1, ChEBI:326268, ChemSpider:2695170, HMDB:HMDB01414, IAF1260:33980, KEGG:C00134, MetaboLights:MTBLC326268, PubChem:3452892

Standard Gibbs Free Energy of Formation (ΔfG in kcal/mol): -6.02

Reactions known to consume the compound:

putrescine degradation I :
putrescine + 2-oxoglutarate → 4-aminobutanal + L-glutamate

putrescine degradation II :
putrescine + L-glutamate + ATP → γ-glutamyl-L-putrescine + ADP + phosphate + H+

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

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

Reactions known to produce the compound:

L-arginine degradation III (arginine decarboxylase/agmatinase pathway) , putrescine biosynthesis I :
agmatine + H2O → urea + putrescine

putrescine biosynthesis III , superpathway of ornithine degradation :
L-ornithine + H+ → CO2 + putrescine

Reactions known to both consume and produce the compound:

Not in pathways:
putrescine + 2-oxoglutarate ↔ L-glutamate + 1-pyrroline + H2O

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:
putrescine[periplasm] + H+[periplasm]putrescine[cytosol] + H+[cytosol],
putrescine[cytosol] + L-ornithine[periplasm]putrescine[periplasm] + L-ornithine[cytosol],
ATP + putrescine[periplasm] + H2O → ADP + putrescine[cytosol] + phosphate + H+

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

Inhibitor (Competitive) of: arginine decarboxylase, biosynthetic [Wu73], ornithine decarboxylase [Applebaum77], lysine:cadaverine antiporter [Soksawatmaekhin04], cadaverine:H+ symporter [Soksawatmaekhin04] Inhibitor (Mechanism unknown) of: dihydrofolate reductase [Baccanari75], lysine decarboxylase [Wertheimer83, Yamamoto97] Activates: mprA Inferred from experiment [Sakamoto15]

In Growth Media: PMA carbon source test + putrescine, Gutnick minimal salts medium base + putrescine, PMA nitrogen source test + putrescine

Regulated Transcription Units (4 total):

Notes:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


References

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

Sakamoto15: Sakamoto A, Terui Y, Yoshida T, Yamamoto T, Suzuki H, Yamamoto K, Ishihama A, Igarashi K, Kashiwagi K (2015). "Three Members of Polyamine Modulon under Oxidative Stress Conditions: Two Transcription Factors (SoxR and EmrR) and a Glutathione Synthetic Enzyme (GshA)." PLoS One 10(4);e0124883. PMID: 25898225

Soksawatmaekhin04: Soksawatmaekhin W, Kuraishi A, Sakata K, Kashiwagi K, Igarashi K (2004). "Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli." Mol Microbiol 51(5);1401-12. PMID: 14982633

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

Yamamoto97: Yamamoto Y, Miwa Y, Miyoshi K, Furuyama J, Ohmori H (1997). "The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme." Genes Genet Syst 1997;72(3);167-72. PMID: 9339543


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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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