Escherichia coli K-12 substr. MG1655 Compound: L-ornithine

Synonyms: Ornithine, 2, 5-diaminovaleric acid, 2, 5-diaminopentanoic acid, 2, 5-diaminopentanoate, α,δ-diaminovaleric acid

Superclasses: an amino acid or its derivative an amino acid an alpha amino acid a non-standard alpha amino acid ornithine
an amino acid or its derivative an amino acid an alpha amino acid a non-standard alpha amino acid
an amino acid or its derivative an amino acid an L-amino acid

Chemical Formula: C5H13N2O2

Molecular Weight: 133.17 Daltons

Monoisotopic Molecular Weight: 132.0898776398 Daltons

L-ornithine compound structure

SMILES: C(C[N+])CC([N+])C([O-])=O

InChI: InChI=1S/C5H12N2O2/c6-3-1-2-4(7)5(8)9/h4H,1-3,6-7H2,(H,8,9)/p+1/t4-/m0/s1


Unification Links: ChEBI:46911 , ChemSpider:5360242 , HMDB:HMDB00214 , IAF1260:37976 , KEGG:C00077 , MetaboLights:MTBLC46911 , PubChem:6992088

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -85.66

Reactions known to consume the compound:

putrescine biosynthesis III , superpathway of ornithine degradation :
L-ornithine + H+ → CO2 + putrescine

Reactions known to produce the compound:

L-ornithine biosynthesis :
N-acetyl-L-ornithine + H2O → L-ornithine + acetate

Not in pathways:
a polypeptide + H2O → a polypeptide + an L-amino acid

Reactions known to both consume and produce the compound:

L-arginine biosynthesis I (via L-ornithine) :
L-ornithine + carbamoyl-phosphate ↔ L-citrulline + phosphate + H+

In Reactions of unknown directionality:

Not in pathways:
a 5-L-glutamyl-[peptide][periplasmic space] + an amino acid[periplasmic space] = a 5-L-glutamyl-amino acid[periplasmic space] + a peptide[periplasmic space]

In Transport reactions:
putrescine[cytosol] + L-ornithine[periplasmic space] → putrescine[periplasmic space] + L-ornithine[cytosol] ,
ATP + L-ornithine[periplasmic space] + H2O → ADP + L-ornithine[cytosol] + phosphate + H+ ,
an L-amino acid[cytosol]an L-amino acid[periplasmic space]

Enzymes activated by L-ornithine, sorted by the type of activation, are:

Activator (Allosteric) of: carbamoyl phosphate synthetase [Anderson77, Trotta74]

Enzymes inhibited by L-ornithine, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: lysine:cadaverine antiporter [Soksawatmaekhin04] , acetylornithine deacetylase [Comment 1] , arginine decarboxylase, degradative [Blethen68] , cadaverine:H+ symporter [Soksawatmaekhin04]

Inhibitor (Noncompetitive) of: agmatinase [Satishchandran86]

In Growth Media: Gutnick minimal salts medium base + L-ornithine , PMA nitrogen source test + L-ornithine , PMA carbon source test + L-ornithine


Anderson77: Anderson PM (1977). "Binding of allosteric effectors to carbamyl-phosphate synthetase from Escherichia coli." Biochemistry 1977;16(4);587-93. PMID: 189806

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

JavidMajd00: Javid-Majd F, Blanchard JS (2000). "Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase." Biochemistry 2000;39(6);1285-93. PMID: 10684608

Satishchandran86: Satishchandran C, Boyle SM (1986). "Purification and properties of agmatine ureohydrolyase, a putrescine biosynthetic enzyme in Escherichia coli." J Bacteriol 1986;165(3);843-8. PMID: 3081491

Soksawatmaekhin04: Soksawatmaekhin W, Kuraishi A, Sakata K, Kashiwagi K, Igarashi K (2004). "Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli." Mol Microbiol 51(5);1401-12. PMID: 14982633

Trotta74: Trotta PP, Pinkus LM, Haschemeyer RH, Meister A (1974). "Reversible dissociation of the monomer of glutamine-dependent carbamyl phosphate synthetase into catalytically active heavy and light subunits." J Biol Chem 1974;249(2);492-9. PMID: 4358555

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Mar 31, 2015, biocyc13.