Crystallization and preliminary structural analyses of glutamate dehydrogenase from Peptoniphilus asaccharolyticus.
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.
Oliveira
Tania F
TF
School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland.
Carrigan
John B
JB
Hamza
Muaawia A
MA
Sharkey
Michael A
MA
Engel
Paul C
PC
Khan
Amir R
AR
D018360:Crystallography, X-Ray; D015870:Gene Expression; D005969:Glutamate Dehydrogenase / Q000737:chemistry* / Q000235:genetics; D010462:Peptostreptococcus / Q000201:enzymology*
D005969:Glutamate Dehydrogenase
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