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Asparaginase
From Proteopedia
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{{STRUCTURE_2p2n| PDB=2p2n | SIZE=400| SCENE= |right|CAPTION=E. coli asparaginase I tetramer complex with aspartic acid, asparagine, ethylene glycol and Cl- ions (green), [[2p2n]] }} | {{STRUCTURE_2p2n| PDB=2p2n | SIZE=400| SCENE= |right|CAPTION=E. coli asparaginase I tetramer complex with aspartic acid, asparagine, ethylene glycol and Cl- ions (green), [[2p2n]] }} | ||
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== Function == | == Function == | ||
Revision as of 11:11, 5 November 2015
Contents |
Function
Asparaginase (ASP) catalyzes the conversion of asparagine to aspartic acid (AA). The ALL cells require high concentrations of asparagine which becomes scarce when high doses of ASP are present.
Relevance
ASP I is used in the food processing industry to reduce the formation of the carcinogen acrylamide in the production of starchy food products. A different kind of ASP – ASP II – is used as drug (Elspar) in the treatment of cancer such as acute lymphoblastic leukemia (ALL).
Structural highlights
ASP I active site is located at the N terminal region in the interface between subunits.
3D structures of asparaginase
Updated on 05-November-2015
Proteopedia Page Contributors and Editors (what is this?)
Joel L. Sussman, Michal Harel, Alexander Berchansky, Jaime Prilusky
