Structural basis for the catalytic mechanism and α-ketoglutarate cooperativity of glutamate dehydrogenase.

ABSTRACT: Glutamate dehydrogenase (GDH) is a key enzyme connecting carbon and nitrogen metabolism in all living organisms. Despite extensive studies on GDHs from both prokaryotic and eukaryotic organisms in the last 40 years, the structural basis of the catalytic features of this enzyme remains incomplete. This study reports the structural basis of the GDH catalytic mechanism and allosteric behavior. We determined the first high-resolution crystal structures of glutamate dehydrogenase from the fungus Aspergillus niger (AnGDH), a unique NADP⁺-dependent allosteric enzyme that is forward-inhibited by the formation of mixed disulfide. We determined the structures of the active enzyme in its apo form and in binary/ternary complexes with bound substrate (α-ketoglutarate), inhibitor (isop

SUBMITTER: Prakash P 

PROVIDER: S-EPMC5925808 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature