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/Assimilation → Amines and Polyamines Degradation → Putrescine Degradation|
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, Huang90a]. 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.
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
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
Huang90a: 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
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
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
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
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
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
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
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
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493