If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: L-arginine succinyltransferase pathway, AST pathway, ammonia-producing L-arginine catabolic pathway, L-arginine catabolism
|Superclasses:||Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-arginine Degradation|
This pathway (called the AST pathway for its crucial enzyme, arginine succinyltransferase) is the major arginine-degrading pathway found in E. coli. It yields 2 molecules of ammonia and 2 of glutamate and can satisfy E. coli's total nitrogen requirement, but not its total carbon requirement. This pathway does, however, permit other organisms, for example Klebsiella aerogenes, to utilize arginine as a total source of carbon. With the exception of succinylarginine dihydrolase and succinylornithine transaminase, enzymes of this pathway from E. coli have not been characterized beyond assaying crude extracts. Succinylornithine transaminase gained special attention and was originally designated as argM because is can substitute for acetylornithine transaminase (encoded by argD) in the biosynthesis of arginine. The substrates of the two enzymes differ only in ornithine's being acetylated in the biosynthetic pathway and succinylated in the degradative pathway.
Variants: L-arginine degradation III (arginine decarboxylase/agmatinase pathway) , superpathway of L-arginine and L-ornithine degradation , superpathway of L-arginine, putrescine, and 4-aminobutanoate degradation
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Kuznetsova05: Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29(2);263-79. PMID: 15808744
Lal14: Lal PB, Schneider BL, Vu K, Reitzer L (2014). "The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli." Mol Microbiol 94(4);843-56. PMID: 25243376
Newman13: Newman J, Seabrook S, Surjadi R, Williams CC, Lucent D, Wilding M, Scott C, Peat TS (2013). "Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (AstC) from Escherichia coli." PLoS One 8(3);e58298. PMID: 23484010
Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554
Shirai03: Shirai H, Mizuguchi K (2003). "Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism." FEBS Lett 555(3);505-10. PMID: 14675764
Stancik02: Stancik LM, Stancik DM, Schmidt B, Barnhart DM, Yoncheva YN, Slonczewski JL (2002). "pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli." J Bacteriol 184(15);4246-58. PMID: 12107143
Tocilj05: Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler M (2005). "Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli." J Biol Chem 280(16);15800-8. PMID: 15703173
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