Pyrroline-5-carboxylate dehydrogenase

From Proteopedia

Mouse pyrroline-5-carboxylate dehydrogenase dimer complex with glutarate and PEG400 (PDB entry 4lh3) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function 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. Disease Mutation in PCD results in the metabolic disorder type II hyperprolinemia[2]. Structural highlights PCD ligand . Water molecules are shown as red spheres. A [3].

3D structures of pyrroline-5-carboxylate dehydrogenase

Updated on 09-February-2022

References

1. ↑ Deuschle K, Funck D, Forlani G, Stransky H, Biehl A, Leister D, van der Graaff E, Kunze R, Frommer WB. The role of [Delta]1-pyrroline-5-carboxylate dehydrogenase in proline degradation. Plant Cell. 2004 Dec;16(12):3413-25. Epub 2004 Nov 17. PMID:15548746 doi:http://dx.doi.org/10.1105/tpc.104.023622
2. ↑ Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA. Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. PMID:9700195
3. ↑ Pemberton TA, Tanner JJ. Structural basis of substrate selectivity of Delta-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): Semialdehyde chain length. Arch Biochem Biophys. 2013 Aug 6. pii: S0003-9861(13)00231-2. doi:, 10.1016/j.abb.2013.07.024. PMID:23928095 doi:10.1016/j.abb.2013.07.024