Cloned (Comment) | Organism |
---|---|
- |
Corynebacterium glutamicum |
Crystallization (Comment) | Organism |
---|---|
in complex with NADPH and 2-oxoglutarate. The enzyme functions as a hexamer, and each monomer comprises a Rossmann-fold cofactor-binding domain and a substrate-binding domain. In the apo-form, GDH exists as an open state, and upon binding of the substrate and cofactor the protein undergoes a conformation change to a closed state | Corynebacterium glutamicum |
Protein Variants | Comment | Organism |
---|---|---|
K116A | almost complete loss of activity | Corynebacterium glutamicum |
K128A | almost complete loss of activity | Corynebacterium glutamicum |
K92A | almost complete loss of activity | Corynebacterium glutamicum |
N347A | almost complete loss of activity | Corynebacterium glutamicum |
R208A | almost complete loss of activity | Corynebacterium glutamicum |
S379A | almost complete loss of activity | Corynebacterium glutamicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | P31026 | - |
- |
Corynebacterium glutamicum ATCC 13032 | P31026 | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | the NADP-binding pocket is mainly formed by the cofactor-binding domain, with partial contribution by the substrate-binding domain | Corynebacterium glutamicum |