Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Reaction: 2.1.3.3

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.1.3.3

Enzymes and Genes:
ornithine carbamoyltransferase chain F Inferred from experiment : argF
ornithine carbamoyltransferase chain I Inferred from experiment : argI

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

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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: ?

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 SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC13B.