This is a default text for your page Rafael Bertelli Ferraro/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
L-asparaginase is an enzyme that converts L-asparagine into asparctic acid and ammonia. In adition this enzyme have a side activity analogous to previous one, which is the catalysis of D-glutamine into glutamate and ammonia.
Disease
Lymphoblastic Acute Leukemia, is a blood cancer that affects mainly childs (2-5 age); consists of non-controled proliferation of lymphocytic lineages since lymphoblasts to younges lymphocitic cells.
Relevance
Cancer cells are unable to perform synthesis of L-asparagine due to the lack of Asparagine Synthetase enzyme, which means that all source of L-asparagine is exogenous, unlike normal cells that can synthesize their own L-asparagine. When bacterial L-asparaginase is injected into the bloodstream, circulating L-asparagine is depleted, so cancer cells become unable to perform protein synthesis, that leads affected cells to apoptosis without harm to normal cells.
Structural highlights
Pseudomonas 7A Glutaminase-Asparaginase (PGA) consists of a tetrameric structure. Each is identical and possesses 337 residues.
In the amminoterminal portion of each monomer, is able to identify and , unlike the carboxyl-terminal domain which have and
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.