Sandbox Reserved 644

This Sandbox is Reserved from 30/08/2012, through 01/02/2013 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 636 through Sandbox Reserved 685.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing For more help, look at this link: http://proteopedia.org/w/Help:Getting_Started_in_Proteopedia Ornithine TranscarbamoylaseOrnithine Transcarbamoylase IntroductionIntroduction Ornithine transcarbamoylase (OTC) is an enzyme that catalyzes the reaction between carbamoyl phosphate and ornithine to form citrulline and phosphate. In plants and microbes, OTC is involved in arginine biosynthesis, but in mammals it is located in the mitochondria and is part of the urea cycle. OTC is often associated with Ornithine transcarbamoylase deficiency (OTCD). OTCD is a common urea cycle disorder, and it is a genetic disorder which results in a mutated and ineffective form of the enzyme OTC. StructureStructure OTC is a trimer. The monomer unit has a CP-binding domain and an amino acid-binding domain. Each of the two discrete substrate-binding domains (SBDs) have an α/β topology with a central β-pleated sheet embedded in flanking α-helices. The active sites are located at the interface between the protein monomers. References: