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Escherichia coli K-12 substr. MG1655 Pathway: aminopropylcadaverine biosynthesis

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

Locations of Mapped Genes:

Genetic Regulation Schematic: ?

Superclasses: Biosynthesis Amines and Polyamines Biosynthesis

Summary:
Polyamines are important for cell growth and are believed to be involved in many processes including DNA, RNA, and protein synthesis, as well as membrane integrity and resistance to stress, to name a few. Cadaverine and aminopropylcadaverine are alternative polyamines that can at least partially substitute for purtrescine and spermidine, the primary polyamines found in E. coli. Lysine is decarboxylated to form cadaverine which is then converted to aminopropylcadaverine by the aminopropyltransferase, SpeE.

Citations: [Dion72, Igarashi86, Soksawatmaekhin04]

Superpathways: superpathway of polyamine biosynthesis I , superpathway of arginine and polyamine biosynthesis

Credits:
Created 16-Feb-2007 by Johnson A , TIGR


References

Dion72: Dion AS, Cohen SS (1972). "Polyamine stimulation of nucleic acid synthesis in an uninfected and phage-infected polyamine auxotroph of Escherichia coli K12 (arginine-agmatine ureohydrolase-putrescine-spermidine-lysine-cadaverine)." Proc Natl Acad Sci U S A 69(1);213-7. PMID: 4550506

Igarashi86: Igarashi K, Kashiwagi K, Hamasaki H, Miura A, Kakegawa T, Hirose S, Matsuzaki S (1986). "Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines." J Bacteriol 166(1);128-34. PMID: 3514574

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

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

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

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

Boeker83: Boeker EA, Fischer EH (1983). "Lysine decarboxylase (Escherichia coli B)." Methods Enzymol 94;180-4. PMID: 6353151

Bowman73: Bowman WH, Tabor CW, Tabor H (1973). "Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli." J Biol Chem 1973;248(7);2480-6. PMID: 4572733

BRENDA, 2014: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Chattopadhyay09: Chattopadhyay MK, Tabor CW, Tabor H (2009). "Polyamines are not required for aerobic growth of Escherichia coli: preparation of a strain with deletions in all of the genes for polyamine biosynthesis." J Bacteriol 191(17);5549-52. PMID: 19542271

Day01: Day WA, Fernandez RE, Maurelli AT (2001). "Pathoadaptive mutations that enhance virulence: genetic organization of the cadA regions of Shigella spp." Infect Immun 69(12);7471-80. PMID: 11705922

Dell94: Dell CL, Neely MN, Olson ER (1994). "Altered pH and lysine signalling mutants of cadC, a gene encoding a membrane-bound transcriptional activator of the Escherichia coli cadBA operon." Mol Microbiol 14(1);7-16. PMID: 7830562

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

El10: El Bakkouri M, Gutsche I, Kanjee U, Zhao B, Yu M, Goret G, Schoehn G, Burmeister WP, Houry WA (2010). "Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity." Proc Natl Acad Sci U S A 107(52);22499-504. PMID: 21148420

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Goldemberg80: Goldemberg SH (1980). "Lysine decarboxylase mutants of Escherichia coli: evidence for two enzyme forms." J Bacteriol 141(3);1428-31. PMID: 6767710

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Kamio83: Kamio Y, Terawaki Y (1983). "Purification and properties of Selenomonas ruminantium lysine decarboxylase." J Bacteriol 153(2);658-64. PMID: 6401702

Kanjee11: Kanjee U, Gutsche I, Alexopoulos E, Zhao B, El Bakkouri M, Thibault G, Liu K, Ramachandran S, Snider J, Pai EF, Houry WA (2011). "Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase." EMBO J 30(5);931-44. PMID: 21278708

Kanjee11a: Kanjee U, Gutsche I, Ramachandran S, Houry WA (2011). "The Enzymatic Activities of the Escherichia coli Basic Aliphatic Amino Acid Decarboxylases Exhibit a pH Zone of Inhibition." Biochemistry 50(43);9388-98. PMID: 21957966

Kikuchi97: Kikuchi Y, Kojima H, Tanaka T, Takatsuka Y, Kamio Y (1997). "Characterization of a second lysine decarboxylase isolated from Escherichia coli." J Bacteriol 1997;179(14);4486-92. PMID: 9226257

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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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