This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-arginine Degradation|
Some taxa known to possess this pathway include : Arthrobacter globiformis, Arthrobacter sp. KUJ8602, Brevibacterium helvolum, Leishmania donovani, Pimelobacter simplex, Streptomyces griseus, Streptomyces violaceochromogenes
Several Actinobacteria, including Streptomyces griseus, Streptomyces violaceochromogenes, Brevibacterium helvolum and Arthrobacter globiformis can utilize L-arginine as the sole source for carbon and nitrogen utilizing a pathway that involves the intermediate 4-guanidinobutyramide [Van62, Van62a, Yorifuji89, Yorifuji95]. The same pathway was also observed in the eukaryotic parasite Leishmania donovani [Bera87].
In this pathway L-arginine is degraded via 4-guanidinobutyramide, 4-guanidinobutanoate, and 4-aminobutanoate, which is eventually degraded via succinate semialdehyde into succinate, and fed into the TCA cycle I (prokaryotic) (see the pathway superpathway of 4-aminobutanoate degradation) [Hatt56, Nguyen66]. ammonia and urea are produced during this process, providing the direct nitrogen source for the organism (urea can be used after it is split by the enzyme urease into ammonia and CO2).
Variants: L-arginine degradation I (arginase pathway), L-arginine degradation II (AST pathway), L-arginine degradation III (arginine decarboxylase/agmatinase pathway), L-arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway), L-arginine degradation V (arginine deiminase pathway), L-arginine degradation VI (arginase 2 pathway), L-arginine degradation VII (arginase 3 pathway), L-arginine degradation VIII (arginine oxidase pathway), L-arginine degradation IX (arginine:pyruvate transaminase pathway), L-arginine degradation XI, L-arginine degradation XII, L-citrulline-nitric oxide cycle, superpathway of L-arginine and L-ornithine degradation, superpathway of L-arginine, putrescine, and 4-aminobutanoate degradation
Hatt56: Hatt, J.L., Thi, A.N., Van Thoai, N. (1956). "[Metabolism of guanidine derivatives. V. Enzymic oxidation of arginine to guanidinobutyramide.]." Biochim Biophys Acta 22(1);116-23. PMID: 13373855
Kato86: Kato, T., Yamaga, M., Tsukahara, S. (1986). "Guanidine compounds in fruit trees and their seasonal variations in citrus (Citrus unshiu Marc)." Journal of the Japanese Society for Horticultural Science 55(2):169-173.
Yorifuji89: Yorifuji, T., Hirabayashi, K., Nagashima, T., Inagaki, N., Shimizu, E., Imada, K., Katsumi, T., Sawamura, S. (1989). "Distribution of the arginine oxygenase pathway among coryneform bacteria." Agric. biol. Chem. 53(4):1103-1110.
Yorifuji95: Yorifuji T, Kaneoke M, Okazaki T, Shimizu E (1995). "Degradation of 2-ketoarginine by guanidinobutyrase in arginine aminotransferase pathway of Brevibacterium helvolum." Biosci Biotechnol Biochem 59(3);512-3. PMID: 7766193
Arakawa03: Arakawa N, Igarashi M, Kazuoka T, Oikawa T, Soda K (2003). "D-arginase of Arthrobacter sp. KUJ 8602: characterization and its identity with Zn(2+)-guanidinobutyrase." J Biochem (Tokyo) 133(1);33-42. PMID: 12761196
Hatt56a: Hatt, J.L., Roche, J., Van Thoai, N., Tran Thi, A.N. (1956). "[Metabolism of guanidine derivatives. VI. Degradation of guanidine derivatives in Streptomyces griseus (Waksman)]." Biochim Biophys Acta 22(2);337-41. PMID: 13382852
Nakada02: Nakada Y, Itoh Y (2002). "Characterization and regulation of the gbuA gene, encoding guanidinobutyrase in the arginine dehydrogenase pathway of Pseudomonas aeruginosa PAO1." J Bacteriol 184(12);3377-84. PMID: 12029055
Romagnoli14: Romagnoli G, Verhoeven MD, Mans R, Fleury Rey Y, Bel-Rhlid R, van den Broek M, Maleki Seifar R, Ten Pierick A, Thompson M, Muller V, Wahl SA, Pronk JT, Daran JM (2014). "An alternative, arginase-independent pathway for arginine metabolism in Kluyveromyces lactis involves guanidinobutyrase as a key enzyme." Mol Microbiol. PMID: 24912400
Van62b: Van Thoai, N., Olomucki, A. (1962). "Arginine decarboxy-oxydase II. Oxydation de la canavanine et de l'homoarginine en β-guanidoxypropionamide et en δ-guanidovaleramide." Biochim. Biophys. Acta 59:545-552.
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