|Gene:||cadA||Accession Numbers: EG10131 (MetaCyc), b4131, ECK4125|
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of lysine decarboxylase 1 = [CadA]10
There are two lysine decarboxylases in E. coli, encoded by the cadA and ldcC genes. The cadA gene product, lysine decarboxylase 1 (LDC1), is more active, is thermostable, and has a lower pH optimum than the ldcC-encoded enzyme, LDC2 [Goldemberg80]. [Lemonnier98, Yamamoto97, Kikuchi97]
LDC1 is part of the lysine-dependent acid resistance system 4 (AR4) which confers resistance to weak organic acids produced during carbohydrate fermentation under conditions of anaerobiosis and phosphate starvation. Lysine decarboxylase is a biodegradative enzyme. It is induced under acidic pH conditions and plays a role in maintaining pH homeostasis or extending the growth period by detoxification of the extracellular medium. The CO2 produced by CadA may be physiologically important when the TCA cycle is down-regulated under conditions of anaerobiosis and low pH, and CO2 production is therefore reduced [Takayama94].
Lysine provides protection during anaerobic phosphate starvation, dramatically increasing viability, and a cadBA deletion completely reverses this effect [Moreau07]. Overproduction of CadA affects the growth rate [Mandic98]. A speA speB speC speD cadA quintuple mutant is viable, albeit slow growing, on media deficient in amines, indicating that polyamines are not required for growth [Tabor80].
LDC1 production is induced under anaerobic growth conditions and acid pH [Goldemberg80]. Regulation has been described [Auger89, Meng92, Shi93, Takayama94, Neely94, Dell94, Shi95, Reams97, Rowbury97, Pruss97, Kikuchi98, Kikuchi98, Neely96, Popkin80, Beretskene80, Watson92]. cadBA is positively regulated by CadC [Watson92].
|Map Position: [4,354,493 <- 4,356,640]|
Molecular Weight of Polypeptide: 81.26 kD (from nucleotide sequence)
Molecular Weight of Multimer: 81 kD (experimental) [Meng92a]
Unification Links: ASAP:ABE-0013526 , CGSC:943 , DIP:DIP-35646N , EchoBASE:EB0129 , EcoGene:EG10131 , EcoliWiki:b4131 , Mint:MINT-1234345 , ModBase:P0A9H3 , OU-Microarray:b4131 , PortEco:cadA , PR:PRO_000022240 , Protein Model Portal:P0A9H3 , RefSeq:NP_418555 , RegulonDB:EG10131 , SMR:P0A9H3 , String:511145.b4131 , UniProt:P0A9H3
Relationship Links: InterPro:IN-FAMILY:IPR000310 , InterPro:IN-FAMILY:IPR005308 , InterPro:IN-FAMILY:IPR008286 , InterPro:IN-FAMILY:IPR011193 , InterPro:IN-FAMILY:IPR015421 , InterPro:IN-FAMILY:IPR015422 , InterPro:IN-FAMILY:IPR015424 , PDB:Structure:3N75 , PDB:Structure:3Q16 , Pfam:IN-FAMILY:PF01276 , Pfam:IN-FAMILY:PF03709 , Pfam:IN-FAMILY:PF03711 , Prosite:IN-FAMILY:PS00703
|Biological Process:||GO:0006554 - lysine catabolic process
GO:0006520 - cellular amino acid metabolic process [GOA01]
|Molecular Function:||GO:0005515 - protein binding
GO:0008923 - lysine decarboxylase activity [GOA01a, Kikuchi97, Goldemberg80]
GO:0042802 - identical protein binding [Kanjee11, Snider06]
GO:0003824 - catalytic activity [GOA01]
GO:0016829 - lyase activity [UniProtGOA11]
GO:0016831 - carboxy-lyase activity [UniProtGOA11, GOA01]
GO:0030170 - pyridoxal phosphate binding [GOA01]
|Cellular Component:||GO:0005737 - cytoplasm
[UniProtGOA11a, UniProtGOA11, GOA01]
GO:0005829 - cytosol [DiazMejia09]
|MultiFun Terms:||cell processes → adaptations → pH|
Enzymatic reaction of: lysine decarboxylase
Synonyms: lysine decarboxylase, inducible, LDC, L-lysine carboxy-lyase, acid-inducible LDC
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
The reaction is physiologically favored in the direction shown.
In Pathways: superpathway of arginine and polyamine biosynthesis , superpathway of polyamine biosynthesis I , superpathway of lysine degradation , aminopropylcadaverine biosynthesis , lysine degradation I
The cadA encoded enzyme is more active, is thermostable, and has a lower pH optimum than the other enzyme [Lemonnier98].
The Km of lysine decarboxylase is measured to be 2.0 mM [Vienozinskiene85]. Constitutive and inducible forms are observed [Goldemberg80]. The low-level activity observed under noninducing conditions is sensitive to putrescine and spermidine [Wertheimer83].
Enzyme activity assays are presented [Vienozinskiene85].
10/20/97 Gene b4131 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10131; confirmed by SwissProt match.
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
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
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, 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
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
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
Maurelli98: Maurelli AT, Fernandez RE, Bloch CA, Rode CK, Fasano A (1998). ""Black holes" and bacterial pathogenicity: a large genomic deletion that enhances the virulence of Shigella spp. and enteroinvasive Escherichia coli." Proc Natl Acad Sci U S A 95(7);3943-8. PMID: 9520472
McCormick99: McCormick BA, Fernandez MI, Siber AM, Maurelli AT (1999). "Inhibition of Shigella flexneri-induced transepithelial migration of polymorphonuclear leucocytes by cadaverine." Cell Microbiol 1(2);143-55. PMID: 11207548
Neely94: Neely MN, Dell CL, Olson ER (1994). "Roles of LysP and CadC in mediating the lysine requirement for acid induction of the Escherichia coli cad operon." J Bacteriol 176(11);3278-85. PMID: 8195083
Park96: Park YK, Bearson B, Bang SH, Bang IS, Foster JW (1996). "Internal pH crisis, lysine decarboxylase and the acid tolerance response of Salmonella typhimurium." Mol Microbiol 20(3);605-11. PMID: 8736539
Pruss97: Pruss BM, Markovic D, Matsumura P (1997). "The Escherichia coli flagellar transcriptional activator flhD regulates cell division through induction of the acid response gene cadA." J Bacteriol 179(11);3818-21. PMID: 9171439
Reams97: Reams SG, Lee N, Mat-Jan F, Clark DP (1997). "Effect of chelating agents and respiratory inhibitors on regulation of the cadA gene in Escherichia coli." Arch Microbiol 167(4);209-16. PMID: 9075621
Rowbury97: Rowbury RJ (1997). "Regulatory components, including integration host factor, CysB and H-NS, that influence pH responses in Escherichia coli." Lett Appl Microbiol 24(5);319-28. PMID: 9172436
Sabo74: Sabo DL, Boeker EA, Byers B, Waron H, Fischer EH (1974). "Purification and physical properties of inducible Escherichia coli lysine decarboxylase." Biochemistry 1974;13(4);662-70. PMID: 4590109
Sabo74a: Sabo DL, Fischer EH (1974). "Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5'-phosphate binding site." Biochemistry 13(4);670-6. PMID: 4204273
Snider06: Snider J, Gutsche I, Lin M, Baby S, Cox B, Butland G, Greenblatt J, Emili A, Houry WA (2006). "Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase." J Biol Chem 281(3);1532-46. PMID: 16301313
Tabor80: Tabor H, Hafner EW, Tabor CW (1980). "Construction of an Escherichia coli strain unable to synthesize putrescine, spermidine, or cadaverine: characterization of two genes controlling lysine decarboxylase." J Bacteriol 144(3);952-6. PMID: 7002915
Tabor83: Tabor CW, Tabor H, Hafner EH (1983). "Mass screening for mutants in the biosynthetic pathway for polyamines in Escherichia coli: a general method for mutants in enzymatic reactions producing CO2." Methods Enzymol 94;83-91. PMID: 6413821
Watson92: Watson N, Dunyak DS, Rosey EL, Slonczewski JL, Olson ER (1992). "Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH." J Bacteriol 174(2);530-40. PMID: 1370290
Wertheimer83: Wertheimer SJ, Leifer Z (1983). "Putrescine and spermidine sensitivity of lysine decarboxylase in Escherichia coli: evidence for a constitutive enzyme and its mode of regulation." Biochem Biophys Res Commun 114(2);882-8. PMID: 6349639
Yamamoto97: Yamamoto Y, Miwa Y, Miyoshi K, Furuyama J, Ohmori H (1997). "The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme." Genes Genet Syst 1997;72(3);167-72. PMID: 9339543
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