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 → Other Amino Acids Degradation|
Some taxa known to possess this pathway include : Aeromonas caviae , Aphanocapsa , Arabidopsis thaliana col , Giardia intestinalis , Halobacterium salinarum , Lactobacillus hilgardii , Lactobacillus plantarum , Mycoplasma hominis , Mycoplasma pneumoniae M129 , Oenococcus oeni , Pseudomonas aeruginosa , Spiroplasma citri , Streptococcus ratti , Treponema denticola
The citrulline degradation pathway is widely distributed among prokaryotic organisms, often associated with the degradation of arginine into citrulline (see L-arginine degradation V (arginine deiminase pathway)), it has been detected in lactic bacteria [Arena99a, Arena99, Arena05], bacilli [Ottow74, Broman78], Pseudomonas spp. [Vander84, Stalon87], Aeromonas spp. [Stalon82], clostridia [Schmidt52, Mitruka67], Mycoplasma spp. [Schimke66, Tyldesley75, Vander84, Lin86], streptococci [CasianoColon88], Spiroplasma spp. [Igwebe78], Spirochaeta spp. [Blakemore76], halobacteria [Dundas66], and cyanobacteria [Weathers78].
In addition, the pathway is also present in some primitive eukaryotic protozoans, including Trichomonas vaginalis [Linstead83], Tritrichomonas suis [Yarlett94], Hexamita inflata [Biagini03], and Giardia intestinalis, in which it plays a significant role in energy metabolism, providing a route for anaerobic substrate level phosphorylation [Schofield90].
The enzymes of this pathway, as well as arginine deiminase, have also been found in Arabidopsis thaliana col, and it was shown that Arabidopsis chloroplasts can metabolize arginine and citrulline all the way to CO2. However, since Arabidopsis rarely encounters exogenous citrulline, it is thought that in this organism the pathway may serve as a means for extracting nitrogen from endogenous sources [Ludwig93]. The ornithine carbamoyltransferase (OTC) has been identified from a T-DNA-tagged mutant of Arabidopsis and has been shown to be encoded by a gene that overlaps with another, unrelated gene (AUL1), one of the rare cases of gene convergence observed in Arabidopsis thaliana [Quesada99]. Ornithine carbamoyltransferase has also been cloned from other plant sources such as Pisum sativum [Williamson96] and Canavalia lineata [Lee00] [Lee01c].
Bacteria that employ this pathway use the enzyme ornithine carbamoyltransferase to convert L-citrulline to L-ornithine and carbamoyl-phosphate. The later is then broken into ammonia and CO2 in an ATP-forming reaction, catalyzed by the enzyme carbamate kinase, providing the bacteria with energy, carbon and nitrogen.
While this pathway is a subset of the arginine deiminase pathway, some of the organisms that employ it lack the enzyme arginine deiminase (for example, Oenococcus oeni [Arena05]), and thus are not able to utilize arginine, making this a distinct pathway.
Unification Links: AraCyc:CITRULLINE-DEG-PWY
Biagini03: Biagini GA, Yarlett N, Ball GE, Billetz AC, Lindmark DG, Martinez MP, Lloyd D, Edwards MR (2003). "Bacterial-like energy metabolism in the amitochondriate protozoon Hexamita inflata." Mol Biochem Parasitol 128(1);11-9. PMID: 12706792
Broman78: Broman K, Lauwers N, Stalon V, Wiame JM (1978). "Oxygen and nitrate in utilization by Bacillus licheniformis of the arginase and arginine deiminase routes of arginine catabolism and other factors affecting their syntheses." J Bacteriol 135(3);920-7. PMID: 690081
CasianoColon88: Casiano-Colon A, Marquis RE (1988). "Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance." Appl Environ Microbiol 54(6);1318-24. PMID: 2843090
Lee01c: Lee Y, Choi YA, Hwang ID, Kim SG, Kwon YM (2001). "cDNA cloning of two isoforms of ornithine carbamoyltransferase from Canavalia lineata leaves and the effect of site-directed mutagenesis of the carbamoyl phosphate binding site." Plant Mol Biol 46(6);651-60. PMID: 11575720
Vander84: Vander Wauven C, Pierard A, Kley-Raymann M, Haas D (1984). "Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine: evidence for a four-gene cluster encoding the arginine deiminase pathway." J Bacteriol 160(3);928-34. PMID: 6438064
Williamson96: Williamson CL, Lake MR, Slocum RD (1996). "Isolation and characterization of a cDNA encoding a pea ornithine transcarbamoylase (argF) and comparison with other transcarbamoylases." Plant Mol Biol 31(6);1087-92. PMID: 8914525
Yarlett94: Yarlett N, Lindmark DG, Goldberg B, Moharrami MA, Bacchi CJ (1994). "Subcellular localization of the enzymes of the arginine dihydrolase pathway in Trichomonas vaginalis and Tritrichomonas foetus." J Eukaryot Microbiol 41(6);554-9. PMID: 7866382
Baur87: Baur H, Stalon V, Falmagne P, Luethi E, Haas D (1987). "Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli." Eur J Biochem 166(1);111-7. PMID: 3109911
BSUB93: "Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics." (1993). Editors: Sonenshein, A.L., Hoch, J.A., Losick, R. American Society For Microbiology, Washington, DC.
Chen05: Chen L, Brugger K, Skovgaard M, Redder P, She Q, Torarinsson E, Greve B, Awayez M, Zibat A, Klenk HP, Garrett RA (2005). "The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota." J Bacteriol 187(14);4992-9. PMID: 15995215
Goodyear04: Goodyear CS, Silverman GJ (2004). "Staphylococcal toxin induced preferential and prolonged in vivo deletion of innate-like B lymphocytes." Proc Natl Acad Sci U S A 101(31);11392-7. PMID: 15273292
Hata86: Hata A, Tsuzuki T, Shimada K, Takiguchi M, Mori M, Matsuda I (1986). "Isolation and characterization of the human ornithine transcarbamylase gene: structure of the 5'-end region." J Biochem (Tokyo) 100(3);717-25. PMID: 3782067
Himmelreich96: Himmelreich R, Hilbert H, Plagens H, Pirkl E, Li BC, Herrmann R (1996). "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae." Nucleic Acids Res 1996;24(22);4420-49. PMID: 8948633
Kenklies99: Kenklies J, Ziehn R, Fritsche K, Pich A, Andreesen JR (1999). "Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC." Microbiology 1999;145 ( Pt 4);819-26. PMID: 10220161
Kuo88: Kuo LC, Miller AW, Lee S, Kozuma C (1988). "Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis." Biochemistry 1988;27(24);8823-32. PMID: 3072022
Legrain72: Legrain C, Halleux P, Stalon V, Glansdorff N (1972). "The dual genetic control of ornithine carbamolytransferase in Escherichia coli. A case of bacterial hybrid enzymes." Eur J Biochem 1972;27(1);93-102. PMID: 4558857
Legrain76: Legrain C, Stalon V (1976). "Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure and steady-state kinetic analysis." Eur J Biochem 1976;63(1);289-301. PMID: 4319
Legrain76a: Legrain C, Stalon V, Glansdorff N (1976). "Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary significance and the isolation of lambdaargF and lambdaargI transducing bacteriophages." J Bacteriol 1976;128(1);35-8. PMID: 789338
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