Premium
Crystal structure of the 2‐iminoglutarate‐bound complex of glutamate dehydrogenase from Corynebacterium glutamicum
Author(s) -
Tomita Takeo,
Yin Lulu,
Nakamura Shugo,
Kosono Saori,
Kuzuyama Tomohisa,
Nishiyama Makoto
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12667
Subject(s) - corynebacterium glutamicum , glutamate dehydrogenase , cofactor , stereochemistry , protein data bank (rcsb pdb) , active site , chemistry , enzyme , crystal structure , substrate (aquarium) , biochemistry , glutamate receptor , biology , crystallography , ecology , receptor , gene
The NADP + ‐dependent glutamate dehydrogenase from Corynebacterium glutamicum (Cg GDH ) is considered to be one of the key enzymes in the industrial fermentation of glutamate due to its high glutamate‐producing activity. We determined the crystal structure of Cg GDH complexed with NADP + and 2‐iminoglutarate. Among six subunits of hexameric Cg GDH ‐binding NADP + , only four subunits bind 2‐iminoglutarate in a closed form, while the other two are in an open form. In the closed form, 2‐iminoglutarate is bound to the substrate‐binding site with the 2‐imino group stacked by the nicotinamide ring of the coenzyme, suggesting a prehydride transfer state in a hypothesized reaction scheme with the imino intermediate. We also conducted MD simulations and provide insights into the extreme preference for the glutamate‐producing reaction of Cg GDH . Database The atomic coordinate and structure factors have been deposited in the RCSB PDB database under the accession number 5GUD .