Sandbox Reserved 641

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<Structure load='1l1f' size='500' frame='true' align='right' caption='Glutamate Dehydrogenase' scene='Insert optional scene name here' />
<Structure load='1l1f' size='500' frame='true' align='right' caption='Glutamate Dehydrogenase' scene='Insert optional scene name here' />
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== '''Overview''' ==
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== '''Introduction''' ==
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Glutamate Dehydrogenase (GDH)is used to remove the ketone group and replace it with an α-amine group on the α-carbon. This forms glutamate, one of the 20 essential amino acids.
== '''Structure''' ==
== '''Structure''' ==
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== '''Mechanism''' ==
== '''Mechanism''' ==
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NH4+ + α-ketoglutarate + NADPH + 2 H+ → glutamate + NADP+ + H2O
::[[Image:glutamatedehydrogenase.jpeg]]
::[[Image:glutamatedehydrogenase.jpeg]]

Revision as of 23:48, 7 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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Contents

Glutamate Dehydrogenase

Glutamate Dehydrogenase

Drag the structure with the mouse to rotate

Introduction

Glutamate Dehydrogenase (GDH)is used to remove the ketone group and replace it with an α-amine group on the α-carbon. This forms glutamate, one of the 20 essential amino acids.

Structure

Glutamate Dehydrogenase is a hexamer that is comprised of two trimer subunits. These two subunits are stacked and composed of three domains. The top of each domain contains a "NAD-binding domain" that has the conserved nucleotide-binding motif. A larger helix-loop-helix structure rises above this and is referred to as an "antenna." This antenna contains approximately 50 amino acids and plays a major role in regulation of the enzyme. (1)

Mechanism

NH4+ + α-ketoglutarate + NADPH + 2 H+ → glutamate + NADP+ + H2O

Image:glutamatedehydrogenase.jpeg


(1) http://www.sciencedirect.com.prox.lib.ncsu.edu/science/article/pii/S0968000408001898 (2) http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1974.tb03565.x/pdf (3) http://onlinelibrary.wiley.com/doi/10.1002/prot.340120109/pdf (4) http://www.sciencedirect.com/science/article/pii/S0969212699801014x/pdf (3) http://onlinelibrary.wiley.com/doi/10.1002/prot.340120109/pdf (4) http://www.sciencedirect.com/science/article/pii/S0969212699801014

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