Sandbox Reserved 653

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(→Glutamate-Aspartate Aminotransferase)
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<Structure load='1x29' size='500' frame='true' align='right' caption='Structure of Glutamate-Aspartate Aminotransferase' scene='Insert optional scene name here' />
<Structure load='1x29' size='500' frame='true' align='right' caption='Structure of Glutamate-Aspartate Aminotransferase' scene='Insert optional scene name here' />
'''Introduction:'''
'''Introduction:'''
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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 to a second amino acid. These transamination reactions also involve oxaloacetate and α-ketoglutarate.
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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. AST 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.

Revision as of 19:26, 23 November 2012

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. AST 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.


Structure:


Mechanism of Structure:

Implications of Possible Actions:

References:

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