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Escherichia coli K-12 substr. MG1655 Reaction: 2.1.3.3


Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 2.1.3.3

Enzymes and Genes:
ornithine carbamoyltransferase chain FInferred from experiment: argF
ornithine carbamoyltransferase chain IInferred from experiment: argI

In Pathway: L-arginine biosynthesis I (via L-ornithine)

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: ornithine carbamoyltransferase

Enzyme Commission Synonyms: citrulline phosphorylase, ornithine transcarbamylase, OTC, carbamylphosphate-ornithine transcarbamylase, L-ornithine carbamoyltransferase, L-ornithine carbamyltransferase, L-ornithine transcarbamylase, ornithine carbamyltransferase

Summary:
This is the sixth step in arginine biosynthesis. It is also part of the urea cycle.

Enzyme Commission Summary:
The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.

Citations: [Bishop67, Marshall72, Marshall72a, Marshall72b]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.1.3.3, ENZYME:EC:2.1.3.3, IUBMB-ExplorEnz:EC:2.1.3.3


References

Bishop67: Bishop SH, Grisolia S (1967). "Crystalline ornithine transcarbamylase." Biochim Biophys Acta 139(2);344-8. PMID: 6034676

Marshall72: Marshall M, Cohen PP (1972). "Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure." J Biol Chem 247(6);1641-53. PMID: 4622303

Marshall72a: Marshall M, Cohen PP (1972). "Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics." J Biol Chem 247(6);1654-68. PMID: 4622304

Marshall72b: Marshall M, Cohen PP (1972). "Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity." J Biol Chem 247(6);1669-82. PMID: 4622305


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc14.