Glutamate dehydrogenase
From Proteopedia
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<StructureSection load='' size='350' side='right' caption='Glutamate dehydrogenase complex with glutamate (PDB entry [[1bgv]])' scene='49/490918/Cv/3'> | <StructureSection load='' size='350' side='right' caption='Glutamate dehydrogenase complex with glutamate (PDB entry [[1bgv]])' scene='49/490918/Cv/3'> | ||
== Function == | == 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<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>. | + | '''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>. |
See also [[Citric Acid Cycle]]. | See also [[Citric Acid Cycle]]. | ||
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</StructureSection> | </StructureSection> | ||
| - | ==3D structures of glutamate dehydrogenase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *Glutamate dehydrogenase | ||
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| - | **[[1l1f]] – hGLDH1 – human<br /> | ||
| - | **[[1nr1]], [[6dqg]] – hGLDH1 (mutant)<br /> | ||
| - | **[[6g2u]] – hGLDH2<br /> | ||
| - | **[[1nr7]] – bGLDH – bovine<br /> | ||
| - | **[[6dhn]], [[6dhl]], [[3jcg]] – bGLDH1<br /> | ||
| - | **[[5k12]] – bGLDH1 – Cryo-EM<br /> | ||
| - | **[[1gtm]] – GLDH – ''Pyrococcus furiosus''<br /> | ||
| - | **[[1hrd]] – CsGLDH – ''Clostridium symbiosum''<br /> | ||
| - | **[[1aup]], [[1k89]] – CsGLDH (mutant)<br /> | ||
| - | **[[1bvu]] – GLDH – ''Thermococcus litoralis''<br /> | ||
| - | **[[1euz]] - GLDH – ''Thermococcus profundus''<br /> | ||
| - | **[[1b26]] – TmGLDH – ''Thermotoga maritima''<br /> | ||
| - | **[[1b3b]], [[2tmg]] - TmGLDH (mutant)<br /> | ||
| - | **[[2bma]] – PfGLDH – ''Plasmodium falciparum''<br /> | ||
| - | **[[3r3j]] - PfGLDH (mutant)<br /> | ||
| - | **[[3k8z]], [[3k92]] – GLDH (mutant) – ''Bacillus subtilis''<br /> | ||
| - | **[[2yfq]] - bGLDH – ''Peptoniphilus asaccharolyticus''<br /> | ||
| - | **[[3sbo]], [[4bht]], [[4fcc]] - EcGLDH – ''Escherichia coli''<br /> | ||
| - | **[[2yfh]] – EcGLDH/CsGLDH<br /> | ||
| - | **[[4xgi]] – GLDH – ''Burkholderia thailandensis''<br /> | ||
| - | **[[5xvi]] – AnGLDH – ''Aspergillus niger''<br /> | ||
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| - | *Glutamate dehydrogenase complex | ||
| - | **[[1hwy]] – bGLDH + NAD + 2-oxoglutarate <br /> | ||
| - | **[[6dhd]] – bGLDH + NADP + GTP + glutamate <br /> | ||
| - | **[[6dhm]] - bGLDH + NAD + GTP + glutamate <br /> | ||
| - | **[[3ete]], [[3etg]] - bGLDH + NADP + GTP + inhibitor + glutamate <br /> | ||
| - | **[[1nqt]], [[6dhk]] - bGLDH + ADP<br /> | ||
| - | **[[6dhq]] - bGLDH + NADP + epicatechin-3-gallate<br /> | ||
| - | **[[3jd0]] – bGLDH1 + GTP<br /> | ||
| - | **[[3jd1]], [[3jd2]] – bGLDH1 + NAD<br /> | ||
| - | **[[3jd3]], [[3jd4]] – bGLDH1 + GTP + NAD<br /> | ||
| - | **[[1bgv]] – CsGLDH + glutamate <br /> | ||
| - | **[[1v9l]] - GLDH + NAD – ''Pyrobaculum islandicum''<br /> | ||
| - | **[[3aoe]] - TtGLDH + leucine – ''Thermus thermophilus''<br /> | ||
| - | **[[3aog]] - TtGLDH + NH4 + glutamate <br /> | ||
| - | **[[4fhn]] – EcGLDH + Nup37 + Nup120<br /> | ||
| - | **[[5ijz]] - CgGLDH + NAD + 2-oxoglutarate – ''Corynebacterium glutamicum''<br /> | ||
| - | **[[5gud]] – CgGLDH + NADP <br /> | ||
| - | **[[5xvv]] – AnGLDH + oxoglutarate <br /> | ||
| - | **[[5xvx]] – AnGLDH + NADP + oxoglutarate <br /> | ||
| - | **[[5xw0]] – AnGLDH + NADP + isophthalate <br /> | ||
| - | **[[5xwc]] – AnGLDH + NADP + iminoglutarate + amino-hydroxyglutarate<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
