Title : Structure, biochemistry, and gene expression patterns of the proline biosynthetic enzyme pyrroline-5-carboxylate reductase (PYCR), an emerging cancer therapy target.

Pub. Date : 2021 Dec

PMID : 34003320






5 Functional Relationships(s)
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1 Structure, biochemistry, and gene expression patterns of the proline biosynthetic enzyme pyrroline-5-carboxylate reductase (PYCR), an emerging cancer therapy target. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens
2 Structure, biochemistry, and gene expression patterns of the proline biosynthetic enzyme pyrroline-5-carboxylate reductase (PYCR), an emerging cancer therapy target. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens
3 Here we focus on the last enzyme of proline biosynthesis, Delta1-pyrroline-5-carboxylate reductase, known as PYCR in humans. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens
4 PYCR catalyzes the NAD(P)H-dependent reduction of Delta1-pyrroline-5-carboxylate to proline and forms the reductive half of the proline metabolic cycle. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens
5 PYCR catalyzes the NAD(P)H-dependent reduction of Delta1-pyrroline-5-carboxylate to proline and forms the reductive half of the proline metabolic cycle. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens