If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Biosynthesis → Amines and Polyamines Biosynthesis|
|Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-arginine Degradation|
This arginine catabolic pathway has been discovered in Escherichia coli K-12 by Shaibe et al. [Shaibe85]. The pathway is essentially identical to an anabolic pathway that is used by many bacteria for the biosynthesis of putrescine (see putrescine biosynthesis I [Morris70]. Even though the main catabolic arginine pathway of Escherichia coli K-12 is the succinyltransferase pathway (L-arginine degradation II (AST pathway)), this pathway provides an alternative route, and is used under certain growth conditions. Interestingly, unlike Escherichia coli K-12, wild-type E. coli strains are unable to use L-arginine as a carbon source, even though they can use it as a nitrogen source [Cunin86].
Escherichia coli K-12 has two forms of the enzyme arginine decarboxylase: a constitutive biosynthetic form, encoded by the speA gene, and an inducible catabolic form, encoded by the adiA gene. When the catabolic form is not expressed, the pathway operates only in an anabolic manner, catalyzing the biosynthesis of putrescine, which is used by the bacteria either directly or as a precursor for the biosynthesis of other polyamines (see superpathway of polyamine biosynthesis I). However, when the cells are grown in an arginine-rich medium, especially if the medium is acidic and conditions are semi-anaerobic, the catabolic arginine decarboxylase is expressed, and the pathway operates in a catabolic manner, feeding putrescine via 4-aminobutanoate and succinate into the TCA cycle I (prokaryotic) [Tabor85].
Variants: L-arginine degradation II (AST pathway)
Shaibe85: Shaibe E, Metzer E, Halpern YS (1985). "Metabolic pathway for the utilization of L-arginine, L-ornithine, agmatine, and putrescine as nitrogen sources in Escherichia coli K-12." J Bacteriol 163(3);933-7. PMID: 3897201
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
Bitonti87: Bitonti AJ, Casara PJ, McCann PP, Bey P (1987). "Catalytic irreversible inhibition of bacterial and plant arginine decarboxylase activities by novel substrate and product analogues." Biochem J 1987;242(1);69-74. PMID: 3297044
Blethen68: Blethen SL, Boeker EA, Snell EE (1968). "Argenine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme." J Biol Chem 1968;243(8);1671-7. PMID: 4870599
Boyle84: Boyle SM, Markham GD, Hafner EW, Wright JM, Tabor H, Tabor CW (1984). "Expression of the cloned genes encoding the putrescine biosynthetic enzymes and methionine adenosyltransferase of Escherichia coli (speA, speB, speC and metK)." Gene 30(1-3);129-36. PMID: 6392022
Carvajal04: Carvajal N, Orellana MS, Salas M, Enriquez P, Alarcon R, Uribe E, Lopez V (2004). "Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group." Arch Biochem Biophys 430(2);185-90. PMID: 15369817
Carvajal99: Carvajal N, Lopez V, Salas M, Uribe E, Herrera P, Cerpa J (1999). "Manganese is essential for catalytic activity of Escherichia coli agmatinase." Biochem Biophys Res Commun 258(3);808-11. PMID: 10329468
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
Gong03: Gong S, Richard H, Foster JW (2003). "YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli." J Bacteriol 185(15);4402-9. PMID: 12867448
Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726
Showing only 20 references. To show more, press the button "Show all references".
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493