Escherichia coli K-12 substr. MG1655 Pathway: L-ornithine biosynthesis I
Inferred from experiment

Pathway diagram: L-ornithine biosynthesis I

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Genetic Regulation Schematic

Genetic regulation schematic for L-ornithine biosynthesis I

Superclasses: BiosynthesisAmino Acids BiosynthesisOther Amino Acid BiosynthesisL-Ornithine Biosynthesis

General Background

While the amino acid L-ornithine is not involved directly in protein synthesis, it is an important intermediate in many metabolic pathways of prokaryotes and eukaryotes (see urea cycle, pyoverdine I biosynthesis and gramicidin S biosynthesis). In some bacteria L-ornithine-containing lipids and genes involved in their biosynthesis have been identified, but other bacteria such as Escherichia coli do not contain ornithine lipids (reviewed in [Geiger10]) (see MetaCyc pathway ornithine lipid biosynthesis). In E. coli L-ornithine is a precursor of the amino acid L-arginine and the polyamine putrescine, which is in turn a precursor of the polyamine spermidine.

In this pathway L-ornithine is biosynthesized from L-glutamate via N-acetylated intermediates. The presumed reason for the acetylation is that it prevents the spontaneous cyclization of glutamate derivatives, which leads to L-proline biosynthesis (see L-proline biosynthesis I), thus keeping the pathways leading to L-arginine and L-proline separate ( [Caldovic03] and references therein).

Two alternative pathways have evolved that differ in the way the key intermediate N-acetyl-L-glutamate is formed and in the way the acetyl group is removed from another key intermediate, N-acetyl-L-ornithine. In this pathway, which is less common but is found in the Enterobacteriaceae, N-acetyl-L-glutamate is formed by N-acetyl-L-glutamate synthase and N-acetyl-L-ornithine is hydrolyzed by the enzyme acetylornithine deacetylase, forming L-ornithine and acetate. In the other pathway, which is found in most prokaryotic and eukaryotic microorganisms, the two reactions are linked: the acetyl group which is removed from N-acetyl-L-ornithine is recycled onto L-glutamate, regenerating N-acetyl-L-glutamate (see L-arginine biosynthesis II (acetyl cycle)).

About This Pathway

In the ornithine biosynthesis pathway of E. coli, L-glutamate is acetylated to N-acetylglutamate by the enzyme N-acetylglutamate synthase, encoded by the argA gene. The acetyl donor for this reaction is acetyl-CoA. N-acetyl-L-glutamate is then converted in several enzymatic steps to N-acetyl-ornithine. The acetyl group is removed in the form of acetate by the enzyme acetylornithine deacetylase, encoded by the argE gene, producing L-ornithine and acetate. L-ornithine is a precursor of the amino acid L-arginine, as shown in the pathway link.

Review: Charlier, D. and N. Glansdorff (2004) "Biosynthesis of Arginine and Polyamines." EcoSal [ECOSAL]

Superpathways: L-arginine biosynthesis I (via L-ornithine), superpathway of arginine and polyamine biosynthesis

Created 15-Jan-1999 by Iourovitski I, SRI International
Revised 14-Apr-2006 by Caspi R, SRI International
Last-Curated 30-Mar-2011 by Fulcher C, SRI International


Caldovic03: Caldovic L, Tuchman M (2003). "N-acetylglutamate and its changing role through evolution." Biochem J 372(Pt 2);279-90. PMID: 12633501

ECOSAL: "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

Geiger10: Geiger O, Gonzalez-Silva N, Lopez-Lara IM, Sohlenkamp C (2010). "Amino acid-containing membrane lipids in bacteria." Prog Lipid Res 49(1);46-60. PMID: 19703488

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

BacaDeLancey99: Baca-DeLancey RR, South MM, Ding X, Rather PN (1999). "Escherichia coli genes regulated by cell-to-cell signaling." Proc Natl Acad Sci U S A 96(8);4610-4. PMID: 10200310

Baich62: Baich A, Vogel HJ (1962). "N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli." Biochem Biophys Res Commun 7;491-6. PMID: 13863980

Bartsch90: Bartsch K, von Johnn-Marteville A, Schulz A (1990). "Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD)." J Bacteriol 1990;172(12);7035-42. PMID: 2254272

Becker01: Becker G, Hengge-Aronis R (2001). "What makes an Escherichia coli promoter sigma(S) dependent? Role of the -13/-14 nucleotide promoter positions and region 2.5 of sigma(S)." Mol Microbiol 39(5);1153-65. PMID: 11251833

Berg74: Berg CM, Rossi JJ (1974). "Proline excretion and indirect suppression in Escherichia coli and Salmonella typhimurium." J Bacteriol 118(3);928-34. PMID: 4598010

Billheimer76: Billheimer JT, Carnevale HN, Leisinger T, Eckhardt T, Jones EE (1976). "Ornithine delta-transaminase activity in Escherichia coli: its identity with acetylornithine delta-transaminase." J Bacteriol 127(3);1315-23. PMID: 8431

Billheimer79: Billheimer JT, Shen MY, Carnevale HN, Horton HR, Jones EE (1979). "Isolation and characterization of acetylornithine delta-transaminase of wild-type Escherichia coli W. Comparison with arginine-inducible acetylornithine delta-transaminase." Arch Biochem Biophys 1979;195(2);401-13. PMID: 112925

Boyen92: Boyen A, Charlier D, Charlier J, Sakanyan V, Mett I, Glansdorff N (1992). "Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related." Gene 1992;116(1);1-6. PMID: 1628835

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Brown87: Brown K, Finch PW, Hickson ID, Emmerson PT (1987). "Complete nucleotide sequence of the Escherichia coli argA gene." Nucleic Acids Res 1987;15(24);10586. PMID: 3320971

Cox01: Cox RJ, Wang PSH (2001). "Is N-acetylornithine aminotransferase the real N-succinyl-LL-diaminopimelate aminotransferase in Escherichia coli and Mycobacterium smegmatis?." J. Chem. Soc., Perkin Trans. 1:2006-2008.

Cox96: Cox, R. J., Sherwin, W.A., Lam, L.K.P., Vederas, J.C. (1996). "Synthesis and evaluation of novel substrates and inhibitors of N-succinyl-L,L-diaminopimelate aminotransferase (DAP-AT) from Escherichia coli." J. Am. Chem. Soc. 118:7449-7460.

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

Dover72: Dover S, Halpern YS (1972). "Utilization of -aminobutyric acid as the sole carbon and nitrogen source by Escherichia coli K-12 mutants." J Bacteriol 1972;109(2);835-43. PMID: 4550821

Dover74: Dover S, Halpern YS (1974). "Genetic analysis of the gamma-aminobutyrate utilization pathway in Escherichia coli K-12." J Bacteriol 1974;117(2);494-501. PMID: 4590473

Eckhardt75: Eckhardt T, Leisinger T (1975). "Isolation and characterization of mutants with a feedback resistant N-acetylglutamate synthase in Escherichia coli K 12." Mol Gen Genet 138(3);225-32. PMID: 1102931

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

Germer01: Germer J, Becker G, Metzner M, Hengge-Aronis R (2001). "Role of activator site position and a distal UP-element half-site for sigma factor selectivity at a CRP/H-NS-activated sigma(s)-dependent promoter in Escherichia coli." Mol Microbiol 41(3);705-16. PMID: 11532138

Gil99: Gil F, Ramon-Maiques S, Marina A, Fita I, Rubio V (1999). "N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms." Acta Crystallogr D Biol Crystallogr 1999;55 ( Pt 7);1350-2. PMID: 10393305

GilOrtiz02: Gil-Ortiz F, Fita I, Ramon-Maiques S, Marina A, Rubio V (2002). "A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase." Acta Crystallogr D Biol Crystallogr 58(Pt 10 Pt 2);1892-5. PMID: 12351849

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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