Journal
FEBS LETTERS
Volume 591, Issue 11, Pages 1611-1622Publisher
WILEY
DOI: 10.1002/1873-3468.12667
Keywords
2-iminoglutarate-bound complex; Corynebacterium glutamicum; crystal structure; glutamate dehydrogenase
Funding
- JSPS KAKENHI [24580137]
- Grants-in-Aid for Scientific Research [24580137, 15K14685] Funding Source: KAKEN
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The NADP(+) -dependent glutamate dehydrogenase from Corynebacterium glutamicum (CgGDH) 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 CgGDH complexed with NADP(+) and 2-iminoglutarate. Among six subunits of hexameric CgGDH-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 CgGDH. Database The atomic coordinate and structure factors have been deposited in the RCSB PDB database under the accession number 5GL-D.
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