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MetaCyc Pathway: putrescine degradation IV
Inferred from experiment

Enzyme View:

Pathway diagram: putrescine degradation IV

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/AssimilationAmines and Polyamines DegradationPutrescine Degradation

Some taxa known to possess this pathway include : Arabidopsis thaliana col, Kocuria rosea, Pisum sativum

Expected Taxonomic Range: Actinobacteria , Viridiplantae

General Backround

Polyamines (the most common of which are putrescine, spermidine and spermine), a group of positively charged small molecules present in virtually in all living organisms, have been implicated in many biological processes, including binding to nucleic acids, stabilizing membranes, and stimulating several enzymes [Tabor85, Abraham68, Frydman92, Huang90]. Although polyamines are clearly necessary for optimal cell growth, a surplus of polyamines can cause inhibition of growth and protein synthesis [He93], and thus a balance is desired between the production and breakdown of polyamines

Several metabolic pathways for the degradation of putrescine are known.

About This Pathway

The unique feature of this variation is the enzyme catalyzing the first step, putrescine oxidase. While similar pathways in other bacteria utilize an aminotransferase for the oxidation of putrescine to 4-aminobutanal, Kocuria rosea posseses a putrescine oxidase, catalyzing a hydrogen peroxide generating reaction similar to other diamine oxidases. However, this enzyme differs strikingly from animal and plant diamine oxidases in both its substrates and inhibitor specificities [Adachi66, DeSa72].

The original literature focused on putrescine oxidase rather than the putrescine degradation pathway of Kocuria rosea, and as a result, the downstream steps are not known. The enzyme was shown to generate 1-pyrroline in vitro. This compound is spontaneously formed from 4-aminobutanal, which is assumed to be the real product of this enzyme. The fate of 4-aminobutanal, though, is unclear. It is likely that Kocuria rosea, like most other bacteria, posseses a 4-aminobutyraldehyde dehydrogenase that can convert it to 4-aminobutanoate, but there is no data to support it.

Variants: putrescine degradation I, putrescine degradation II, putrescine degradation III, putrescine degradation V

Created 13-Oct-2005 by Caspi R, SRI International


Abraham68: Abraham KA (1968). "Studies on DNA-dependent RNA polymerase from Escherichia coli. 1. The mechanism of polyamine induced stimulation of enzyme activity." Eur J Biochem 5(1);143-6. PMID: 4873311

Adachi66: Adachi, O., Yamada, H., Ogata, K. (1966). "Purification and properties of putrescine oxidase of Micrococcus rubens." Agr. Biol. Chem. 30(12): 1202-1210.

DeSa72: DeSa RJ (1972). "Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme." J Biol Chem 247(17);5527-34. PMID: 4341347

Frydman92: Frydman L, Rossomando PC, Frydman V, Fernandez CO, Frydman B, Samejima K (1992). "Interactions between natural polyamines and tRNA: an 15N NMR analysis." Proc Natl Acad Sci U S A 89(19);9186-90. PMID: 1409623

He93: He Y, Kashiwagi K, Fukuchi J, Terao K, Shirahata A, Igarashi K (1993). "Correlation between the inhibition of cell growth by accumulated polyamines and the decrease of magnesium and ATP." Eur J Biochem 217(1);89-96. PMID: 8223591

Huang90: Huang SC, Panagiotidis CA, Canellakis ES (1990). "Transcriptional effects of polyamines on ribosomal proteins and on polyamine-synthesizing enzymes in Escherichia coli." Proc Natl Acad Sci U S A 87(9);3464-8. PMID: 2185470

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

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Gruez04: Gruez A, Roig-Zamboni V, Grisel S, Salomoni A, Valencia C, Campanacci V, Tegoni M, Cambillau C (2004). "Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase." J Mol Biol 343(1);29-41. PMID: 15381418

Ishizuka93: Ishizuka H, Horinouchi S, Beppu T (1993). "Putrescine oxidase of Micrococcus rubens: primary structure and Escherichia coli." J Gen Microbiol 139(3);425-32. PMID: 8473854

Isobe87: Isobe K, Yamada H, Soejima Y, Otsuji S (1987). "A simple enzymatic differential assay for diamines, spermidine, and spermine in urine and blood." Biochem Med Metab Biol 37(1);110-20. PMID: 3566974

Jann88: Jann A, Matsumoto H, Haas D (1988). "The fourth arginine catabolic pathway of Pseudomonas aeruginosa." J Gen Microbiol 134(4);1043-53. PMID: 3141581

Koyanagi00: Koyanagi T, Matsumura K, Kuroda S, Tanizawa K (2000). "Molecular cloning and heterologous expression of pea seedling copper amine oxidase." Biosci Biotechnol Biochem 64(4);717-22. PMID: 10830482

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Missihoun11: Missihoun TD, Schmitz J, Klug R, Kirch HH, Bartels D (2011). "Betaine aldehyde dehydrogenase genes from Arabidopsis with different sub-cellular localization affect stress responses." Planta 233(2);369-82. PMID: 21053011

Moller98: Moller SG, McPherson MJ (1998). "Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H2O2-generating diamine oxidase." Plant J 13(6);781-91. PMID: 9681017

Prieto87: Prieto MI, Martin J, Balana-Fouce R, Garrido-Pertierra A (1987). "Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli." Biochimie 1987;69(11-12);1161-8. PMID: 3129020

PrietoSantos86: Prieto-Santos MI, Martin-Checa J, Balana-Fouce R, Garrido-Pertierra A (1986). "A pathway for putrescine catabolism in Escherichia coli." Biochim Biophys Acta 1986;880(2-3);242-4. PMID: 3510672

Reed03: Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)." Genome Biol 4(9);R54. PMID: 12952533

Samsonova05: Samsonova NN, Smirnov SV, Novikova AE, Ptitsyn LR (2005). "Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase." FEBS Lett 579(19);4107-12. PMID: 16023116

Shaibe85: Shaibe E, Metzer E, Halpern YS (1985). "Metabolic pathway for the utilization of L-arginine, L-ornithine, agmatine, and putrescine as nitrogen sources in Escherichia coli K-12." J Bacteriol 163(3);933-7. PMID: 3897201

Steward49: Steward, F.C., Thosmpson, J.F., Dent, C.E. (1949). "γ-aminobutyric acid: a constituent of the potato tuber?." Science 110 (2861):439-440.

Tanaka02: Tanaka Dagger K, Nakai R, Sen K, Shimizu E, Karasawa D, Yorifuji T (2002). "Purification and characterization of aminobutyraldehyde dehydrogenase from Arthrobacter Sp. TMP-1." J Biochem Mol Biol Biophys 6(3);171-5. PMID: 12186751

Vaz00: Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ (2000). "Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis." J Biol Chem 275(10);7390-4. PMID: 10702312

Yamada71: Yamada, H. (1971). "Purescine oxidase (Micrococcus rubens)." Methods Enzymol. 17(2):726-730.

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Fri Apr 29, 2016, biocyc14.