Glutamate dehydrogenase

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{{STRUCTURE_1gtm| PDB=1gtm | SIZE=400| SCENE= |right|CAPTION=Glutamate dehydrogenase trimer complex with sulfate, [[1gtm]] }}
{{STRUCTURE_1gtm| PDB=1gtm | SIZE=400| SCENE= |right|CAPTION=Glutamate dehydrogenase trimer complex with sulfate, [[1gtm]] }}
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== Function ==
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'''Glutamate dehydrogenase''' (GLDH) catalyzes the reversible conversion of glutamate to α-ketoglutarate and ammonium. The ammonia is removed via the urea cycle. [[NAD]] or NADP is a cofactor in GLDH activity. NAD is a cofactor in the forward reaction while NADP is a cofactor in the reverse reaction. GLDH is regulated by the cell’s energy state. ATP and GTP inhibit the enzyme while ADP, GDP and leucine positively enhance it<ref>PMID:14299621</ref>. '''Glutamate dehydrogenase 1''' (GLDH1) catalyzes the deamination of glutamate to 2-oxoglutarate and ammonium. GLDH1 is regulated in the same manner as GLDH.
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== Relevance ==
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Elevated GLDH values in blood serum indicate liver malfunction.
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'''Glutamate dehydrogenase''' (GLDH) catalyzes the reversible conversion of glutamate to α-ketoglutarate and ammonium. The ammonia is removed via the urea cycle. Elevated GLDH values in blood serum indicate liver malfunction. NAD or NADP is a cofactor in GLDH activity. NAD is a cofactor in the forward reaction while NADP is a cofactor in the reverse. GLDH is regulated by the cell’s energy state. ATP and GTP inhibit the enzyme while ADP, GDP and leucine positively enhance it. Glutamate dehydrogenase 1 (GLDH1) catalyzes the deamination of glutamate to 2-oxoglutarate and ammonium. GLDH1 is regulated in the same manner as GLDH.
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==3D structures of glutamate dehydrogenase==
==3D structures of glutamate dehydrogenase==
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**[[4fhn]] – EcGLDH + Nup37 + Nup120<br />
**[[4fhn]] – EcGLDH + Nup37 + Nup120<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 14:10, 7 March 2016

Template:STRUCTURE 1gtm

Contents

Function

Glutamate dehydrogenase (GLDH) catalyzes the reversible conversion of glutamate to α-ketoglutarate and ammonium. The ammonia is removed via the urea cycle. NAD or NADP is a cofactor in GLDH activity. NAD is a cofactor in the forward reaction while NADP is a cofactor in the reverse reaction. GLDH is regulated by the cell’s energy state. ATP and GTP inhibit the enzyme while ADP, GDP and leucine positively enhance it[1]. Glutamate dehydrogenase 1 (GLDH1) catalyzes the deamination of glutamate to 2-oxoglutarate and ammonium. GLDH1 is regulated in the same manner as GLDH.

Relevance

Elevated GLDH values in blood serum indicate liver malfunction.

3D structures of glutamate dehydrogenase

Updated on 07-March-2016

References

  1. ↑ FRIEDEN C. GLUTAMATE DEHYDROGENASE. VI. SURVEY OF PURINE NUCLEOTIDE AND OTHER EFFECTS ON THE ENZYME FROM VARIOUS SOURCES. J Biol Chem. 1965 May;240:2028-35. PMID:14299621

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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