Glutamate dehydrogenase
From Proteopedia
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| - | <StructureSection load='1bgv' size=' | + | <StructureSection load='1bgv' 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 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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**[[3k8z]], [[3k92]] – GLDH (mutant) – ''Bacillus subtilis''<br /> | **[[3k8z]], [[3k92]] – GLDH (mutant) – ''Bacillus subtilis''<br /> | ||
**[[2yfq]] - bGLDH – ''Peptoniphilus asaccharolyticus''<br /> | **[[2yfq]] - bGLDH – ''Peptoniphilus asaccharolyticus''<br /> | ||
| - | **[[3sbo | + | **[[3sbo]], [[4bht]], [[4fcc]] - EcGLDH – ''Escherichia coli''<br /> |
**[[2yfh]] – EcGLDH/CsGLDH<br /> | **[[2yfh]] – EcGLDH/CsGLDH<br /> | ||
**[[4xgi]] – GLDH – ''Burkholderia thailandensis''<br /> | **[[4xgi]] – GLDH – ''Burkholderia thailandensis''<br /> | ||
Revision as of 09:18, 17 November 2016
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3D structures of glutamate dehydrogenase
Updated on 17-November-2016
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
- ↑ 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
