Sandbox Reserved 653

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Revision as of 19:39, 23 November 2012 by Hanan Busaileh (Talk | contribs)
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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.
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Glutamate-Aspartate Aminotransferase

Structure of Glutamate-Aspartate Aminotransferase

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Introduction: Aspartate Aminotransferase(AST) has also been known as serum glutamic oxaloacetic transaminase (SGOT). It is an enzyme that functions within the Amino Acid Biosynthesis pathway to interconvert Glutamate and Aspartate. Aminotransferases work to transform amino acids using transamination reactions. This is a process which utilizes the exchange of an α-keto acid to alter an amino acid usually Glutamate and oxaloacetate to a second amino acid in this case Aspartate and α-ketoglutarate. The reaction is dependent on pyridoxial phosphate (PLP) a cofactor which switches between the Pyridoxial Phosphate(PLP) form and the Pyridoxamine Phosphate (PMP) form. The reaction is important in both amino acid synthesis and degradation. When looking at the formation of aspartate it is synthesized from oxaloacetate which is a key step of the citric acid cycle. Also glutamate can be degraded into ammonium ions through the oxidative deamination process. Aspartate Aminotransferae is generally found and has been studied in E.coli, pig heart cytosol, and chicken mitochondira. It is also present in other microorganisms such as Thermus thermophilus and Haloferax. However within these organisms it is commonly found in the muscles, tissues, heart,liver, and kidneys. This is why Aspartate Aminotransferase is so important in tests that monitor liver disease and damage to any of the above organs.


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