Glutamate dehydrogenase

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{{STRUCTURE_1gtm| PDB=1gtm | SIZE=400| SCENE= |right|CAPTION=Glutamate dehydrogenase trimer complex with sulfate, [[1gtm]] }}
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<StructureSection load='' size='350' side='right' caption='Glutamate dehydrogenase complex with glutamate (PDB entry [[1bgv]])' scene='49/490918/Cv/3'>
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== Function ==
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Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
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'''Glutamate dehydrogenase''' (GLDH) catalyzes the reversible conversion of glutamate to α-ketoglutarate (AKG) 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<ref>PMID:12054821</ref>.
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See also [[Citric Acid Cycle]].
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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==
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== Relevance ==
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Elevated GLDH values in blood serum indicate liver malfunction<ref>PMID:589307</ref>.
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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== Disease ==
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Mutations in GLDH1 are associated with familial hyperinsulinism<ref>PMID:10453735</ref>.
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[[1gtm]] – GLDH – ''Pyrococcus furiosus''<br />
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== Structural highlights ==
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[[1hrd]] – CsGLDH – ''Clostridium symbiosum''<br />
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[[1aup]], [[1k89]] – CsGLDH (mutant)<br />
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[[1bvu]] – GLDH – ''Thermococcus litoralis''<br />
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[[1euz]] - GLDH – ''Thermococcus profundus''<br />
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[[1b26]] – TmGLDH – ''Thermotoga maritima''<br />
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[[1b3b]], [[2tmg]] - TmGLDH (mutant)<br />
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[[1l1f]] – hGLDH1 – human<br />
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[[1nr1]] – hGLDH1 (mutant)<br />
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[[1nr7]] – bGLDH – bovine<br />
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[[3mvo]], [[3mvq]] – bGLDH1<br />
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[[2bma]] – PfGLDH – ''Plasmodium falciparum''<br />
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[[3r3j]] - PfGLDH (mutant)<br />
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[[3k8z]], [[3k92]] – GLDH (mutant) – ''Bacillus subtilis''<br />
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[[2yfq]] - bGLDH – ''Peptoniphilus asaccharolyticus''<br />
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[[3sbo]], [[2yfg]] - EcGLDH – ''Escherichia coli''<br />
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[[2yfh]] – EcGLDH/CsGLDH
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'''Glutamate dehydrogenase complex'''
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The biological assembly of GLDH from ''Clostridium symbiosum'' is <scene name='49/490918/Cv/6'>homohexamer</scene>. The <scene name='49/490918/Cv/7'>glutamate binding pocket of GLDH</scene> is in a cleft between the two domains of the enzyme with <scene name='49/490918/Cv/8'>residue D165 serving as a general base and a protein-bound water molecule as the attacking nucleophile</scene> <ref>PMID:8263917</ref>. Water molecules are shown as red spheres.
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==3D structures of glutamate dehydrogenase==
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[[Glutamate dehydrogenase 3D structures]]
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[[1hwy]] – bGLDH + NAD + 2-oxoglutarate <br />
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</StructureSection>
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[[1hwz]] – bGLDH + NADP + GTP + glutamate <br />
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[[3mw9]] - bGLDH + NAD + GTP + glutamate <br />
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[[3ete]], [[3etg]] - bGLDH + NADP + GTP + inhibitor + glutamate <br />
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[[1nqt]] - bGLDH + ADP<br />
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[[1qmu]] - bGLDH + NADP + epicatechin-e-gallate<br />
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[[1bgv]] – CsGLDH + glutamate <br />
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[[1v9l]] - GLDH + NAD – ''Pyrobaculum islandicum''<br />
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[[3aoe]] - TtGLDH + leucine – ''Thermus thermophilus''<br />
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[[3aog]] - TtGLDH + NH4 + glutamate <br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Glutamate dehydrogenase complex with glutamate (PDB entry 1bgv)

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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
  2. ↑ Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA. The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. PMID:12054821 doi:10.1016/S0022-2836(02)00161-4
  3. ↑ Van Waes L, Lieber CS. Glutamate dehydrogenase: a reliable marker of liver cell necrosis in the alcoholic. Br Med J. 1977 Dec 10;2(6101):1508-10. PMID:589307
  4. ↑ Yorifuji T, Muroi J, Uematsu A, Hiramatsu H, Momoi T. Hyperinsulinism-hyperammonemia syndrome caused by mutant glutamate dehydrogenase accompanied by novel enzyme kinetics. Hum Genet. 1999 Jun;104(6):476-9. PMID:10453735
  5. ↑ Stillman TJ, Baker PJ, Britton KL, Rice DW. Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J Mol Biol. 1993 Dec 20;234(4):1131-9. PMID:8263917 doi:http://dx.doi.org/10.1006/jmbi.1993.1665

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