Pyrroline-5-carboxylate dehydrogenase
From Proteopedia
Jump to navigationJump to search
| ||||||||||||
3D structures of pyrroline-5-carboxylate dehydrogenase
Updated on 23-August-2026
FunctionPyrroline-5-carboxylate dehydrogenase or Delta-1-pyrroline-5-carboxylate dehydrogenase(PCD) catalyzes the reversible dehydrogenation of 1-pyrroline-5-carboxylate to glutamate using NAD or NADP as cofactors. PCD participates in glutamate, proline and arginine metabolism. PCD is the second enzyme in proline degradation hence it is important in stress conditions when plants accumulate proline[1]. See also Aldehyde dehydrogenase. DiseaseMutation in PCD results in the metabolic disorder type II hyperprolinemia[2]. Structural highlightsPCD ligand glutarate binds in the cleft between the catalytic and NAD-binding domains. Water molecules are shown as red spheres. A cystein residue is the nucleophile attacker of the aldehyde[3].
| ||||||||||||
Updated on 23-August-2026
This page was last modified 08:36, 23 August 2026.