Pyrroline-5-carboxylate dehydrogenase

From Proteopedia

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 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].

spinqualitylabelsall models 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

3D structures of pyrroline-5-carboxylate dehydrogenase

Updated on 09-February-2022

Pyrroline-5-carboxylate dehydrogenase

3v9g, 4oe5 – hPCD – human

3v9h, 3v9i – hPCD (mutant)

3v9j, 4lgz, 4e3x – mPCD – mouse

4oe6 – yPCD – yeast

1uzb - TtPCD –Termus thermophilus

4k57 - TtPCD (mutant)

3qan – PCD – Bacillus halodurans

3rjl - PCD – Bacillus licheniformis

4idm – MtPCD – Mycobacterium tuberculosis

4ids, 4jdc - MtPCD (mutant)

PCD complex with cofactor

3v9l - mPCD + NAD

7mer, 7mes – m1-PCD + NAD + hydroxyl-proline

4oe4 - yPCD + NAD

2bhp, 2bja – TtPCD + NAD

2ehq - TtPCD + NADP

2bhq - TtPCD + glutamate + NAD

2bjk - TtPCD + citrate + NAD

2ehu, 2ejl - TtPCD + serine + NAD

2eii - TtPCD + valine + NAD

2eit, 2ejd - TtPCD + alanine + NAD

2eiw, 2ej6, 2j40 - TtPCD + proline + NAD

2j5n - TtPCD + glycine + NAD

4ihi - MtPCD + NAD

4ns3 - MtPCD (mutant) + cobalamin + NAD

PCD other complexes

4lh0 - mPCD + glyoxylate

4lh1 - mPCD + malonate

4lh2 - mPCD + succinate

4lh3 - mPCD + glutarate

3v9k - mPCD + proline

4lem - MtPCD (mutant) + cobalamin

2iy6 - TtPCD + citrate

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