Escherichia coli K-12 substr. MG1655 Compound: putrescine

Systematic Name: 1,4-butanediamine

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

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

Component of: PuuR-putrescine

Chemical Formula: C4H14N2

Molecular Weight: 90.168 Daltons

Monoisotopic Molecular Weight: 88.1000483956 Daltons

putrescine compound structure


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


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 Change 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[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:

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[periplasmic space] + H+[periplasmic space]putrescine[cytosol] + H+[cytosol] ,
putrescine[cytosol] + L-ornithine[periplasmic space]putrescine[periplasmic space] + L-ornithine[cytosol] ,
ATP + putrescine[periplasmic space] + 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]

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

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

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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