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Escherichia coli K-12 substr. MG1655 Pathway: superpathway of arginine and polyamine biosynthesis

Pathway diagram: superpathway of arginine and polyamine biosynthesis

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Genetic Regulation Schematic: ?

Genetic regulation schematic for superpathway of arginine and polyamine biosynthesis

Superclasses: Biosynthesis Amines and Polyamines Biosynthesis
Superpathways

Summary:
E. coli makes four polyamines, putrescine, spermidine, cadaverine, and aminopropylcadaverine, the syntheses of which are shown both here and in superpathway of polyamine biosynthesis I. In the absence of exogenous arginine, the principal flow to putrescine and hence spermidine is via ornithine decarboxylase. In the presence of exogenous arginine, however, when ornithine biosynthesis is halted by repression and feed-back inhibition, biosynthesis of putrescine occurs in two steps from arginine 1) by arginine decarboxylase (which is located in the periplasm so that the arginine that flows into polyamines never mixes with the intracellular pool of that amino acid) and then 2) by agmatinase which produces urea along with putrescine--the only urea-producing reaction in E. coli.

Review: Charlier, D. and N. Glansdorff (2004) "Biosynthesis of Arginine and Polyamines." EcoSal 3.6.1.10 [ECOSAL]

Subpathways: putrescine biosynthesis I , putrescine biosynthesis III , spermidine biosynthesis I , aminopropylcadaverine biosynthesis , superpathway of polyamine biosynthesis I , L-arginine biosynthesis I (via L-ornithine) , L-ornithine biosynthesis

Credits:
Last-Curated ? 11-Apr-2011 by Fulcher C , SRI International


References

ECOSAL: "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

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

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

Anagnostopoulos96: Anagnostopoulos CG, Kyriakidis DA (1996). "Regulation of the Escherichia coli biosynthetic ornithine decarboxylase activity by phosphorylation and nucleotides." Biochim Biophys Acta 1297(2);228-34. PMID: 8917626

Anderson75: Anderson PM, Carlson JD (1975). "Reversible reaction of cyanate with a reactive sulfhydryl group at the glutamine binding site of carbamyl phosphate synthetase." Biochemistry 1975;14(16);3688-94. PMID: 240389

Anderson77: Anderson PM (1977). "Binding of allosteric effectors to carbamyl-phosphate synthetase from Escherichia coli." Biochemistry 1977;16(4);587-93. PMID: 189806

Andrell09: Andrell J, Hicks MG, Palmer T, Carpenter EP, Iwata S, Maher MJ (2009). "Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: reversible decamer assembly controls enzyme activity." Biochemistry 48(18);3915-27. PMID: 19298070

Anton87: Anton DL, Kutny R (1987). "Mechanism of substrate inactivation of Escherichia coli S-adenosylmethionine decarboxylase." Biochemistry 26(20);6444-7. PMID: 3322380

Anton87a: Anton DL, Kutny R (1987). "Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NH2-terminal sequences." J Biol Chem 262(6);2817-22. PMID: 3546296

Applebaum75: Applebaum D, Sabo DL, Fischer EH, Morris DR (1975). "Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5'-phosphate binding site." Biochemistry 1975;14(16);3675-81. PMID: 240388

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

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Auger89: Auger EA, Redding KE, Plumb T, Childs LC, Meng SY, Bennett GN (1989). "Construction of lac fusions to the inducible arginine- and lysine decarboxylase genes of Escherichia coli K12." Mol Microbiol 3(5);609-20. PMID: 2527331

BacaDeLancey99: Baca-DeLancey RR, South MM, Ding X, Rather PN (1999). "Escherichia coli genes regulated by cell-to-cell signaling." Proc Natl Acad Sci U S A 96(8);4610-4. PMID: 10200310

Baich62: Baich A, Vogel HJ (1962). "N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli." Biochem Biophys Res Commun 7;491-6. PMID: 13863980

Bartsch90: Bartsch K, von Johnn-Marteville A, Schulz A (1990). "Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD)." J Bacteriol 1990;172(12);7035-42. PMID: 2254272

Baur90: Baur H, Tricot C, Stalon V, Haas D (1990). "Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme." J Biol Chem 265(25);14728-31. PMID: 2118516

Becker01: Becker G, Hengge-Aronis R (2001). "What makes an Escherichia coli promoter sigma(S) dependent? Role of the -13/-14 nucleotide promoter positions and region 2.5 of sigma(S)." Mol Microbiol 39(5);1153-65. PMID: 11251833

Beretskene80: Beretskene SIa, Bruzgulis PA, Ragavichus AB (1980). "[Conditions of the synthesis of lysine decarboxylase by Escherichia coli MRE 600]." Prikl Biokhim Mikrobiol 16(3);351-5. PMID: 7001435

Berg74: Berg CM, Rossi JJ (1974). "Proline excretion and indirect suppression in Escherichia coli and Salmonella typhimurium." J Bacteriol 118(3);928-34. PMID: 4598010

Bhaumik04: Bhaumik P, Koski MK, Bergmann U, Wierenga RK (2004). "Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 60(Pt 11);1964-70. PMID: 15502303

Billheimer76: Billheimer JT, Carnevale HN, Leisinger T, Eckhardt T, Jones EE (1976). "Ornithine delta-transaminase activity in Escherichia coli: its identity with acetylornithine delta-transaminase." J Bacteriol 127(3);1315-23. PMID: 8431

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Jul 28, 2015, biocyc12.