If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-lysine Degradation|
Under conditions of anaerobiosis and phosphate starvation (believed to reflect conditions in the gut), E. coli converts glucose to weak organic acids which, though they are excreted, can reenter the cell and cause bactericidal acid stress even at only moderately acidic pH. Acid resistance system 4 (AR4) is the lysine-dependent acid resistance system which allows for the survival of E. coli under these conditions when lysine is available. AR4 couples the transport activity of a lysine:cadaverine antiporter, CadB, with lysine decarboxylase, CadA. CadB functions by exchanging external lysine for internal cadaverine. Lysine is imported into the cell through CadB. Within the cell lysine is decarboxylated by CadA to cadaverine, releasing CO2 and replacing it with a proton. Cadaverine is then exported through CadB. This effectively consumes protons within the cytoplasm, raising the pH. The glutamate-dependent acid resistance system (AR2) is also able to provide acid resistance to E. coli growing under conditions of anaerobiosis and phosphate starvation, but to a slightly lesser degree than AR4 possibly due to the different pH optimums of their respective decarboxylase enzymes. [Moreau07] AR2 is more efficient than AR3 or AR4 as a mediator of acid resistance at low pH. [Foster04]
Citations: [Neidhardt96 ]
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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
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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
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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
Kanjee11: 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
Kanjee11a: 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
Kikuchi97a: 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
Kikuchi98: Kikuchi Y, Kurahashi O, Nagano T, Kamio Y (1998). "RpoS-dependent expression of the second lysine decarboxylase gene in Escherichia coli." Biosci Biotechnol Biochem 62(6);1267-70. PMID: 9692215
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