2.02012-05-31 13:52:10 -06002015-06-03 15:54:06 -0600ECMDB01414M2MDB000378PutrescinePutrescine is a polyamine. Putrescine is related to cadaverine (another polyamine). Both are produced by the breakdown of amino acids in living and dead organisms and both are toxic in large doses. Putrescine and cadaverine are largely responsible for the foul odor of putrefying flesh. Putrescine attacks s-adenosyl methionine and converts it to spermidine. Spermidine in turn attacks another s-adenosyl methionine and converts it to spermine. Putrescine is synthesized in small quantities by healthy living cells by the action of ornithine decarboxylase. The polyamines, of which putrescine is one of the simplest, appear to be growth factors necessary for cell division. (Wikipedia)1,4-Butanediamine1,4-Butylenediamine1,4-Diaminobutane1,4-TetramethylenediamineButylenediamineDiaminobutanePutrescinTetramethyldiamineTetramethylenediamineC4H12N288.151588.100048394butane-1,4-diamineputrescine110-60-1NCCCCNInChI=1S/C4H12N2/c5-3-1-2-4-6/h1-6H2KIDHWZJUCRJVML-UHFFFAOYSA-NSolidCytosolExtra-organismPeriplasmlogp-0.98logs0.43solubility2.36e+02 g/lmelting_point27.5 oClogp-0.85pka_strongest_basic10.51iupacbutane-1,4-diamineaverage_mass88.1515mono_mass88.100048394smilesNCCCCNformulaC4H12N2inchiInChI=1S/C4H12N2/c5-3-1-2-4-6/h1-6H2inchikeyKIDHWZJUCRJVML-UHFFFAOYSA-Npolar_surface_area52.04refractivity27.38polarizability11.07rotatable_bond_count3acceptor_count2donor_count2physiological_charge2formal_charge0Glutathione metabolismThe biosynthesis of glutathione starts with the introduction of L-glutamic acid through either a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a
glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione.
This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione.
PW000833ec00480MetabolicArginine and proline metabolismec00330ABC transportersec02010Collection of Reactions without pathwaysPW001891MetabolicS-adenosyl-L-methionine biosynthesisS-adenosyl-L-methionine biosynthesis(SAM) is synthesized in the cytosol of the cell from L-methionine and ATP. This reaction is catalyzed by methionine adenosyltransferase. L methione is taken up from the environment through a complex reaction coupled transport and then proceeds too synthesize the s adenosylmethionine through a adenosylmethionine synthase. The S-adenosylmethionine then interacts with a hydrogen ion through a adenosylmethionine decarboxylase resulting in a carbon dioxide and a S-adenosyl 3-methioninamine.This compound interacts with a putrescine through a spermidine synthase resulting in a spermidine, a hydrogen ion and a S-methyl-5'-thioadenosine. The latter compound is degraded by interacting with a water molecule through a 5' methylthioadenosine nucleosidase resulting in a adenine and a S-methylthioribose which is then release into the environmentPW000837Metabolicarginine metabolismThe metabolism of L-arginine starts with the acetylation of L-glutamic acid resulting in a N-acetylglutamic acid while releasing a coenzyme A and a hydrogen ion. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NDPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine.
L-glutamine is used to synthesize carbamoyl phosphate through the interaction of L-glutamine, water, ATP, and hydrogen carbonate. This reaction yields ADP, L-glutamic acid, phosphate, and hydrogen ion.
Carbamoyl phosphate and ornithine are used to catalyze the production of citrulline through an ornithine carbamoyltransferase. Citrulline reacts with L-aspartic acid through an ATP dependent enzyme, argininosuccinate synthase to produce pyrophosphate, AMP and argininosuccinic acid. Argininosussinic acid is then lyase to produce L-arginine and fumaric acid.
L-arginine can be metabolized into succinic acid by two different sets of reactions:
1. Arginine reacts with succinyl-CoA through a arginine N-succinyltransferase resulting in N2-succinyl-L-arginine while releasing CoA and Hydrogen Ion. N2-succinyl-L-arginine is then dihydrolase to produce a N2-succinyl-L-ornithine through a N-succinylarginine dihydrolase. This compound in turn reacts with oxoglutaric acid through succinylornithine transaminase resulting in L-glutamic acid and N2-succinyl-L-glutamic acid 5-semialdehyde. This compoud in turn reacts with a NAD dependent dehydrogenase resulting in N2-succinylglutamate while releasing NADH and hydrogen ion. N2-succinylglutamate reacts with water through a succinylglutamate desuccinylase resulting in L-glutamic acid and
a succinic acid. The succinic acid is then incorporated in the TCA cycle
2.Argine reacts with carbon dioxide and a hydrogen ion through a biodegradative arginine decarboxylase, resulting in Agmatine. This compound is then transformed into putrescine by reacting with water and an agmatinase, and releasing urea. Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid.
Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle.
L-arginine is eventua lly metabolized into succinic acid which then goes to the TCA cyclePW000790Metabolicornithine metabolism
In the ornithine biosynthesis pathway of E. coli, L-glutamate is acetylated to N-acetylglutamate by the enzyme N-acetylglutamate synthase, encoded by the argA gene. The acetyl donor for this reaction is acetyl-CoA. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NADPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine. Ornithine interacts with hydrogen ion through a Ornithine decarboxylase resulting in a carbon dioxide release and a putrescine
Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid.
Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle.
PW000791MetabolicPutrescine Degradation IISeveral metabolic pathways for putrescine degradation as a source of nitrogen for E. coli K-12 are known. The first putrescine degradation pathway was found in in 1985. That pathway is dedicated to the degradation of intracellular putrescine. A second pathway was found in E. coli K-12 twenty years later. This pathway seems to be dedicated to the degradation of extracellular putrescine.
The pathway was discovered following the discovery of a cluster of seven unassigned genes on the E. coli K-12 chromosome. In addition to a putrescine transporter, encoded by the puuP gene, the cluster contains four genes that encode the enzymes involved in this pathway, and two additional genes (puuE and puuR) that encode an enzyme involved in the catabolism of GABA (see superpathway of 4-aminobutanoate degradation) and a regulator.
In this pathway, putrescine is γ-glutamylated at the expense of an ATP molecule. The resulting γ-glutamyl-putrescine is oxidized to γ-glutamyl-γ-aminobutyraldehyde, which is then dehydrogenated into 4-(glutamylamino) butanoate. In the last step, the γ-glutamyl group is removed by hydrolysis, generating 4-aminobutyrate.
The key difference between this pathway and putrescine degradation I is the γ-glutamylation of putrescine. In the other pathway, putrescine is degraded directly to 4-amino-butanal.
Wild type E. coli cells are unable to utilize putrescine as the sole source of carbon at temperatures above 30°C. It is possible to select for mutants that possess this ability; these mutants contain elevated levels of the enzymes in this pathway. (EcoCyc)PW002054MetabolicSpermidine Biosynthesis ISpermidine is formed by the addition of a propylamine moiety to putrescine, catalyzed by an aminopropyltransferase termed spermidine synthase, the the product of gene speE. The source of the propylamine group is decarboxylated S-adenosyl-L-methionine (S-adenosyl-L-methioninamine) which is produced by the action of the pyruvoyl-containing enzyme adenosylmethionine decarboxylase. The other product of the aminopropyltransferase reaction is S-methyl-5'-thioadenosine (MTA), which can be recycled back to L-methionine in many organisms, but not in E. coli.
Inhibition of E. coli adenosylmethionine decarboxylase by spermidine appears to be the most significant regulator of polyamine biosynthesis, probably limiting it when the intracellular spermidine concentration becomes excessive. In E. coli most intracellular spermidine is bound to nucleic acids and phospholipids. (EcoCyc)PW002040MetabolicSpermidine biosynthesis and metabolismSpermidine metabolism starts with S-adenosyl-L-methionine reacting with a hydrogen ion through a adenosylmethionine decarboxylase resulting in the release of a carbon dioxide and a S-adenosyl 3-(methylthio)propylamine. The later compound in turn reacts with putrescine resulting in the release of a hydrogen ion, a spermidine and a S-methyl-5'-thioadenosine. S-methyl-5'-thioadenosine in turn reacts with a water molecule through a 5-methylthioadenosine nucleosidase resulting in the release of a adenine and a S-methyl-5-thio-D-ribose which in in turn is released into the environment. PW002085Metabolicputrescine degradation IPUTDEG-PWYputrescine degradation IIPWY0-1221putrescine biosynthesis IIIPWY-46superpathway of ornithine degradationORNDEG-PWYarginine degradation III (arginine decarboxylase/agmatinase pathway)PWY0-823putrescine biosynthesis IPWY-40spermidine biosynthesis IBSUBPOLYAMSYN-PWYSpecdb::CMs746Specdb::CMs747Specdb::CMs748Specdb::CMs1047Specdb::CMs1193Specdb::CMs1405Specdb::CMs2625Specdb::CMs27668Specdb::CMs28746Specdb::CMs28781Specdb::CMs30397Specdb::CMs30674Specdb::CMs30825Specdb::CMs31330Specdb::CMs31331Specdb::CMs31332Specdb::CMs31682Specdb::CMs31683Specdb::CMs31684Specdb::CMs32116Specdb::CMs32315Specdb::CMs165229Specdb::EiMs1324Specdb::NmrOneD1300Specdb::NmrOneD1703Specdb::NmrOneD4775Specdb::NmrOneD96058Specdb::NmrOneD96059Specdb::NmrOneD96060Specdb::NmrOneD96061Specdb::NmrOneD96062Specdb::NmrOneD96063Specdb::NmrOneD96064Specdb::NmrOneD96065Specdb::NmrOneD96066Specdb::NmrOneD96067Specdb::NmrOneD96068Specdb::NmrOneD96069Specdb::NmrOneD96070Specdb::NmrOneD96071Specdb::NmrOneD96072Specdb::NmrOneD96073Specdb::NmrOneD96074Specdb::NmrOneD96075Specdb::NmrOneD96076Specdb::NmrOneD96077Specdb::NmrOneD166482Specdb::MsMs1568Specdb::MsMs1569Specdb::MsMs1570Specdb::MsMs5291Specdb::MsMs5292Specdb::MsMs5293Specdb::MsMs5294Specdb::MsMs5295Specdb::MsMs5296Specdb::MsMs5297Specdb::MsMs5298Specdb::MsMs5302Specdb::MsMs19850Specdb::MsMs19851Specdb::MsMs19852Specdb::MsMs21401Specdb::MsMs21402Specdb::MsMs21403Specdb::MsMs445781Specdb::MsMs445782Specdb::MsMs445783Specdb::MsMs445784Specdb::MsMs445785Specdb::MsMs447934Specdb::MsMs2228912Specdb::NmrTwoD1069Specdb::NmrTwoD1644HMDB01414104513837702C0289617148PUTRESCINEPUTPutrescineKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72.18402659van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Hamana, K. (1996). "Distribution of diaminopropane and acetylspermidine in Enterobacteriaceae." Can J Microbiol 42:107-114.8742354Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4.19212411Thiele I, Swainston N, Fleming RM, Hoppe A, Sahoo S, Aurich MK, Haraldsdottir H, Mo ML, Rolfsson O, Stobbe MD, Thorleifsson SG, Agren R, Bolling C, Bordel S, Chavali AK, Dobson P, Dunn WB, Endler L, Hala D, Hucka M, Hull D, Jameson D, Jamshidi N, Jonsson JJ, Juty N, Keating S, Nookaew I, Le Novere N, Malys N, Mazein A, Papin JA, Price ND, Selkov E Sr, Sigurdsson MI, Simeonidis E, Sonnenschein N, Smallbone K, Sorokin A, van Beek JH, Weichart D, Goryanin I, Nielsen J, Westerhoff HV, Kell DB, Mendes P, Palsson BO: A community-driven global reconstruction of human metabolism. Nat Biotechnol. 2013 Mar 3. doi: 10.1038/nbt.2488.23455439Venza M, Visalli M, Cicciu D, Teti D: Determination of polyamines in human saliva by high-performance liquid chromatography with fluorescence detection. J Chromatogr B Biomed Sci Appl. 2001 Jun 5;757(1):111-7.11419735El Baze P, Milano G, Verrando P, Renee N, Ortonne JP: Polyamine levels in normal human skin. A comparative study of pure epidermis, pure dermis, and suction blister fluid. Arch Dermatol Res. 1983;275(4):218-21.6625645Gimelli G, Giglio S, Zuffardi O, Alhonen L, Suppola S, Cusano R, Lo Nigro C, Gatti R, Ravazzolo R, Seri M: Gene dosage of the spermidine/spermine N(1)-acetyltransferase ( SSAT) gene with putrescine accumulation in a patient with a Xp21.1p22.12 duplication and keratosis follicularis spinulosa decalvans (KFSD). Hum Genet. 2002 Sep;111(3):235-41. Epub 2002 Aug 1.12215835Janne J, Alhonen L, Pietila M, Keinanen TA: Genetic approaches to the cellular functions of polyamines in mammals. Eur J Biochem. 2004 Mar;271(5):877-94.15009201Reeben M, Arbatova J, Palgi J, Miettinen R, Halmekyto M, Alhonen L, Janne J, Riekkinen P Sr, Saarma M: Induced expression of neurotrophins in transgenic mice overexpressing ornithine decarboxylase and overproducing putrescine. J Neurosci Res. 1996 Sep 1;45(5):542-8.8875319Takagi K, Tatsumi Y, Kitaichi K, Iwase M, Shibata E, Nakao M, Matsumoto T, Takagi K, Hasegawa T: A sensitive colorimetric assay for polyamines in erythrocytes using oat seedling polyamine oxidase. Clin Chim Acta. 2004 Feb;340(1-2):219-27.14734216Harik SI, Sutton CH: Putrescine as a biochemical marker of malignant brain tumors. Cancer Res. 1979 Dec;39(12):5010-5.227593Halmekyto M, Alhonen L, Alakuijala L, Janne J: Transgenic mice over-producing putrescine in their tissues do not convert the diamine into higher polyamines. Biochem J. 1993 Apr 15;291 ( Pt 2):505-8.8484731Goldman SS, Volkow ND, Brodie J, Flamm ES: Putrescine metabolism in human brain tumors. J Neurooncol. 1986;4(1):23-9.3746382Yamazaki H, Tsukahara T, Uki J, Matsuzaki S: Elevated levels of free putrescine and N1-acetylspermidine in cyst fluids of malignant brain tumours. J Neurol Neurosurg Psychiatry. 1986 Feb;49(2):209-10.3950641Janne J, Alhonen L, Keinanen TA, Pietila M, Uimari A, Pirinen E, Hyvonen MT, Jarvinen A: Animal disease models generated by genetic engineering of polyamine metabolism. J Cell Mol Med. 2005 Oct-Dec;9(4):865-82.16364196Dudley, H. W.; Thorpe, W. V. Synthesis of N-methylputrescine and of putrescine. Biochemical Journal (1925), 19 845-9. Spermidine synthaseP09158SPEE_ECOLIspeEhttp://ecmdb.ca/proteins/P09158.xmlSpermidine N(1)-acetyltransferaseP0A951ATDA_ECOLIspeGhttp://ecmdb.ca/proteins/P0A951.xmlOrnithine decarboxylase, constitutiveP21169DCOR_ECOLIspeChttp://ecmdb.ca/proteins/P21169.xmlOrnithine decarboxylase, inducibleP24169DCOS_ECOLIspeFhttp://ecmdb.ca/proteins/P24169.xmlPutrescine aminotransferaseP42588PAT_ECOLIpatAhttp://ecmdb.ca/proteins/P42588.xmlAgmatinaseP60651SPEB_ECOLIspeBhttp://ecmdb.ca/proteins/P60651.xmlSpermidine/putrescine import ATP-binding protein PotAP69874POTA_ECOLIpotAhttp://ecmdb.ca/proteins/P69874.xmlGamma-glutamylputrescine synthetaseP78061PUUA_ECOLIpuuAhttp://ecmdb.ca/proteins/P78061.xmlPutative ABC transporter periplasmic-binding protein ydcSP76108YDCS_ECOLIydcShttp://ecmdb.ca/proteins/P76108.xmlUncharacterized ABC transporter ATP-binding protein ydcTP77795YDCT_ECOLIydcThttp://ecmdb.ca/proteins/P77795.xmlInner membrane ABC transporter permease protein ydcUP77156YDCU_ECOLIydcUhttp://ecmdb.ca/proteins/P77156.xmlInner membrane ABC transporter permease protein ydcVP0AFR9YDCV_ECOLIydcVhttp://ecmdb.ca/proteins/P0AFR9.xmlSpermidine/putrescine transport system permease protein potBP0AFK4POTB_ECOLIpotBhttp://ecmdb.ca/proteins/P0AFK4.xmlSpermidine/putrescine transport system permease protein potCP0AFK6POTC_ECOLIpotChttp://ecmdb.ca/proteins/P0AFK6.xmlPutrescine transport system permease protein potIP0AFL1POTI_ECOLIpotIhttp://ecmdb.ca/proteins/P0AFL1.xmlPutrescine transport system permease protein potHP31135POTH_ECOLIpotHhttp://ecmdb.ca/proteins/P31135.xmlPutrescine transport ATP-binding protein potGP31134POTG_ECOLIpotGhttp://ecmdb.ca/proteins/P31134.xmlPutrescine-binding periplasmic proteinP31133POTF_ECOLIpotFhttp://ecmdb.ca/proteins/P31133.xmlSpermidine/putrescine-binding periplasmic proteinP0AFK9POTD_ECOLIpotDhttp://ecmdb.ca/proteins/P0AFK9.xmlSpermidine/putrescine import ATP-binding protein PotAP69874POTA_ECOLIpotAhttp://ecmdb.ca/proteins/P69874.xmlPutative ABC transporter periplasmic-binding protein ydcSP76108YDCS_ECOLIydcShttp://ecmdb.ca/proteins/P76108.xmlUncharacterized ABC transporter ATP-binding protein ydcTP77795YDCT_ECOLIydcThttp://ecmdb.ca/proteins/P77795.xmlInner membrane ABC transporter permease protein ydcUP77156YDCU_ECOLIydcUhttp://ecmdb.ca/proteins/P77156.xmlInner membrane ABC transporter permease protein ydcVP0AFR9YDCV_ECOLIydcVhttp://ecmdb.ca/proteins/P0AFR9.xmlSpermidine/putrescine transport system permease protein potBP0AFK4POTB_ECOLIpotBhttp://ecmdb.ca/proteins/P0AFK4.xmlSpermidine/putrescine transport system permease protein potCP0AFK6POTC_ECOLIpotChttp://ecmdb.ca/proteins/P0AFK6.xmlPutrescine transport system permease protein potIP0AFL1POTI_ECOLIpotIhttp://ecmdb.ca/proteins/P0AFL1.xmlPutrescine transport system permease protein potHP31135POTH_ECOLIpotHhttp://ecmdb.ca/proteins/P31135.xmlPutrescine importerP76037PUUP_ECOLIpuuPhttp://ecmdb.ca/proteins/P76037.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlPutrescine-ornithine antiporterP0AAF1POTE_ECOLIpotEhttp://ecmdb.ca/proteins/P0AAF1.xmlPutrescine transport ATP-binding protein potGP31134POTG_ECOLIpotGhttp://ecmdb.ca/proteins/P31134.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlPutrescine-binding periplasmic proteinP31133POTF_ECOLIpotFhttp://ecmdb.ca/proteins/P31133.xmlSpermidine/putrescine-binding periplasmic proteinP0AFK9POTD_ECOLIpotDhttp://ecmdb.ca/proteins/P0AFK9.xmlAdenosine triphosphate + Water + Putrescine > ADP + Hydrogen ion + Phosphate + PutrescineABC-25-RXNAdenosine triphosphate + Water + Putrescine > ADP + Hydrogen ion + Phosphate + PutrescineABC-25-RXNHydrogen ion + Ornithine + L-Ornithine <> Carbon dioxide + Putrescine + EthylenediamineR00670ORNDECARBOX-RXNS-Adenosylmethioninamine + Putrescine + Ethylenediamine <> 5'-Methylthioadenosine + Hydrogen ion + SpermidineR01920SPERMIDINESYN-RXNAdenosine triphosphate + L-Glutamate + Putrescine + Ethylenediamine <> ADP + gamma-Glutamyl-L-putrescine + Hydrogen ion + PhosphateR07414RXN0-3901Agmatine + Water <> Putrescine + Urea + EthylenediamineR01157AGMATIN-RXNalpha-Ketoglutarate + Putrescine > 4-Aminobutyraldehyde + L-GlutamateR01155Ornithine <> Putrescine + Carbon dioxideR00670Acetyl-CoA + Putrescine <> Coenzyme A + N-AcetylputrescineR01154Putrescine + alpha-Ketoglutarate <> 4-Aminobutyraldehyde + L-GlutamateR01155Agmatine + Water <> Putrescine + UreaR01157S-Adenosylmethioninamine + Putrescine <> 5'-Methylthioadenosine + SpermidineR01920SPERMIDINESYN-RXNAdenosine triphosphate + L-Glutamate + Putrescine <> ADP + Phosphate + gamma-Glutamyl-L-putrescineR07414Adenosine triphosphate + Putrescine + Water > ADP + Phosphate + Putrescine + Hydrogen ionABC-25-RXNAdenosine triphosphate + Putrescine + Water > ADP + Phosphate + Putrescine + Hydrogen ionABC-25-RXNWater + Agmatine > Urea + PutrescineAGMATIN-RXNHydrogen ion + Ornithine > Carbon dioxide + PutrescineORNDECARBOX-RXNPutrescine + Oxoglutaric acid <> 4-Aminobutyraldehyde + L-GlutamatePUTTRANSAM-RXNPutrescine + L-Glutamate + Adenosine triphosphate > Hydrogen ion + gamma-Glutamyl-L-putrescine + ADP + PhosphateRXN0-3901Putrescine + S-Adenosylmethioninamine > Hydrogen ion + Spermidine + 5'-MethylthioadenosineSPERMIDINESYN-RXNOrnithine > Putrescine + Carbon dioxidePutrescine + Oxoglutaric acid > L-Glutamate + 1-Pyrroline + WaterAdenosine triphosphate + L-Glutamate + Putrescine > ADP + Inorganic phosphate + gamma-Glutamyl-L-putrescineS-Adenosylmethioninamine + Putrescine > 5'-Methylthioadenosine + SpermidinePutrescine + Adenosine triphosphate + L-Glutamic acid + L-Glutamate > Phosphate + Adenosine diphosphate + Hydrogen ion + gamma-Glutamyl-L-putrescine + ADPPW_R002685Putrescine + Oxoglutaric acid > L-Glutamic acid + 4-Aminobutyraldehyde + L-GlutamatePW_R002689Ornithine + Hydrogen ion + Ornithine > Putrescine + Carbon dioxidePW_R002695Putrescine + S-Adenosylmethioninamine > Spermidine + Hydrogen ion + 5'-S-methyl-5'-thioadenosinePW_R005166Putrescine + Oxoglutaric acid <> L-Glutamic acid + 1-Pyrroline + Water + L-GlutamatePW_R005441Decarboxy-SAM + Putrescine > 5'-Methylthioadenosine + Spermidine + Hydrogen ionPW_R005961S-Adenosylmethioninamine + Putrescine + Ethylenediamine <>5 5'-Methylthioadenosine + Hydrogen ion + SpermidineHydrogen ion + Ornithine + L-Ornithine <> Carbon dioxide + Putrescine + EthylenediamineOrnithine <> Putrescine + Carbon dioxideS-Adenosylmethioninamine + Putrescine + Ethylenediamine <>5 5'-Methylthioadenosine + Hydrogen ion + Spermidine199 Medium with Earle’s salts –which contains 21 amino acids, 17 vitamins, 10 components of nucleic acids, sodium acetate, glucose, NaC1, KCl, CaC12, MgS04, Na2HP04, and Fe(N03)3Shake flask2040.0uM0.037 oCK12 HB101Mid Log Phase81600000Hamana, K. (1996). "Distribution of diaminopropane and acetylspermidine in Enterobacteriaceae." Can J Microbiol 42:107-114.8742354199 Medium with Earle’s salts –which contains 21 amino acids, 17 vitamins, 10 components of nucleic acids, sodium acetate, glucose, NaC1, KCl, CaC12, MgS04, Na2HP04, and Fe(N03)3Shake flask3060.0uM0.037 oCK12 HB101Stationary Phase122400000Hamana, K. (1996). "Distribution of diaminopropane and acetylspermidine in Enterobacteriaceae." Can J Microbiol 42:107-114.8742354Luria-Bertani (LB) mediaShake flask281.0uMtrue24.037 oCBL21 DE3Stationary phase cultures (overnight culture)112360096000Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911Luria-Bertani (LB) mediaShake flask1124.33uMtrue41.6337 oCBL21 DE3Stationary phase cultures (overnight culture)4497333166533Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911