Glutamate dehydrogenase
From Proteopedia
(Difference between revisions)
| Line 39: | Line 39: | ||
**[[2yfh]] – EcGLDH/CsGLDH<br /> | **[[2yfh]] – EcGLDH/CsGLDH<br /> | ||
**[[4xgi]] – GLDH – ''Burkholderia thailandensis''<br /> | **[[4xgi]] – GLDH – ''Burkholderia thailandensis''<br /> | ||
| + | **[[5xvi]] – AnGLDH – ''Aspergillus niger''<br /> | ||
*Glutamate dehydrogenase complex | *Glutamate dehydrogenase complex | ||
| Line 56: | Line 57: | ||
**[[3aog]] - TtGLDH + NH4 + glutamate <br /> | **[[3aog]] - TtGLDH + NH4 + glutamate <br /> | ||
**[[4fhn]] – EcGLDH + Nup37 + Nup120<br /> | **[[4fhn]] – EcGLDH + Nup37 + Nup120<br /> | ||
| - | **[[5ijz]] - | + | **[[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]] | ||
Revision as of 10:12, 30 May 2018
| |||||||||||
3D structures of glutamate dehydrogenase
Updated on 30-May-2018
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
