Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.1.4 extracted from

  • Son, H.F.; Kim, I.K.; Kim, K.J.
    Structural insights into domain movement and cofactor specificity of glutamate dehydrogenase from Corynebacterium glutamicum (2015), Biochem. Biophys. Res. Commun., 459, 387-392 .
    View publication on PubMed
Search for more literature for 1.4.1.4

Cloned(Commentary)

Cloned (Comment) Organism
-
 Corynebacterium glutamicum

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Corynebacterium glutamicum P31026
-
-
Corynebacterium glutamicum ATCC 13032 P31026
-
-

Cofactor

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