Crystallization and preliminary structural analyses of glutamate dehydrogenase from Peptoniphilus asaccharolyticus.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 5): 523-6, 2010 May 01.
Article
in En
| MEDLINE
| ID: mdl-20445250
ABSTRACT
Glutamate dehydrogenase (EC 1.4.1.2-4) from Peptoniphilus asaccharolyticus has been expressed as a selenomethionine-derivatized recombinant protein and diffraction-quality crystals have been grown that are suitable for structure determination. Preliminary structural analyses indicate that the protein assembles as a homohexameric enzyme complex in solution, similar to other bacterial and mammalian enzymes to which its sequence identity varies between 25 and 40%. The structure will provide insight into its preference for the cofactor NADH (over NADPH) by comparisons with the known structures of mammalian and bacterial enzymes.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptostreptococcus
/
Glutamate Dehydrogenase
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2010
Document type:
Article
Affiliation country: