Function
Pyrroline-5-carboxylate reductase (PYCR) catalyzes the reversible oxidation of 1-pyrroline-5-carboxylate to proline using NAD or NADP as cofactors. This is the last step in the biosynthesis of proline from glutamate[1].
Disease
Mutations in PYCR cause microcephaly and hypomyelination[2].
Structural highlights
The active site of PYCR contains the NAD cofactor and glutamate[3]
- ↑ Giberti S, Funck D, Forlani G. Delta1-Pyrroline-5-carboxylate reductase from Arabidopsis thaliana: stimulation or inhibition by chloride ions and feedback regulation by proline depend on whether NADPH or NADH acts as co-substrate. New Phytol. 2014 May;202(3):911-9. doi: 10.1111/nph.12701. Epub 2014 Jan 28. PMID:24467670 doi:https://dx.doi.org/10.1111/nph.12701
- ↑ Nakayama T, Al-Maawali A, El-Quessny M, Rajab A, Khalil S, Stoler JM, Tan WH, Nasir R, Schmitz-Abe K, Hill RS, Partlow JN, Al-Saffar M, Servattalab S, LaCoursiere CM, Tambunan DE, Coulter ME, Elhosary PC, Gorski G, Barkovich AJ, Markianos K, Poduri A, Mochida GH. Mutations in PYCR2, Encoding Pyrroline-5-Carboxylate Reductase 2, Cause Microcephaly and Hypomyelination. Am J Hum Genet. 2015 May 7;96(5):709-19. doi: 10.1016/j.ajhg.2015.03.003. Epub, 2015 Apr 9. PMID:25865492 doi:https://dx.doi.org/10.1016/j.ajhg.2015.03.003
- ↑ Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z. Crystal structure of human pyrroline-5-carboxylate reductase. J Mol Biol. 2006 Jun 23;359(5):1364-77. Epub 2006 May 11. PMID:16730026 doi:10.1016/j.jmb.2006.04.053
