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Article

Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.

The Journal of biological chemistry - 28 Apr 2017

Christensen Emily M, Patel Sagar M, Korasick David A, Campbell Ashley C, Krause Kurt L, Becker Donald F, Tanner John J

Abstract excerpt

Pyrroline-5-carboxylate reductase (PYCR) is the final enzyme in proline biosynthesis, catalyzing the NAD(P)H-dependent reduction of Δ1-pyrroline-5-carboxylate (P5C) to proline. Mutations in the PYCR1 gene alter mitochondrial function and cause the connective tissue disorder cutis laxa. Furthermore, PYCR1 is overexpressed in multiple cancers, and the PYCR1 knock-out suppresses tumorigenic growth, suggesting that...

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Identifiers

PMID: 28258219
DOI: 10.1074/jbc.M117.780288
PMCID: PMC5409489

Genes

PYCR1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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