Glutaminase-Asparaginase (Pseudomonas 7A)

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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 4 alpha helix

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