MSC08 4670, Department of Biochemistry and Molecular Biology, University of New Mexico Health Sciences Center, Albuquerque, NM, 87131-0001, USA.
Amino Acids. 2021 Dec;53(12):1835-1840. doi: 10.1007/s00726-021-03048-x. Epub 2021 Jul 22.
Δ-Pyrroline-5-carboxylate (P5C) reductase (PYCR or P5CR) catalyzes the conversion of P5C to L-proline (Pro) with concomitant oxidation of a cofactor, NADPH or NADH. Mammalian PYCR have been studied since 1950' and currently three isozymes of human PYCR, 1, 2, and L, have been identified and characterized and their roles in genetic diseases and cancer biology have been keenly investigated. These three isozymes are encoded by three different genes localized at three different chromosomes, and catalyze NAD(P)H-dependent reduction of P5C to Pro important for the transfer of oxidizing potential across the mitochondrion and cell. The review summarizes the current understanding of these three human PYCR isozymes and their roles in diseases with a focus on cancer.
Δ-吡咯啉-5-羧酸（P5C）还原酶（PYCR 或 P5CR）催化 P5C 转化为 L-脯氨酸（Pro），同时氧化辅因子 NADPH 或 NADH。自 1950 年以来，哺乳动物的 PYCR 一直受到研究，目前已鉴定并表征了人类 PYCR 的三种同工酶 1、2 和 L，它们在遗传疾病和癌症生物学中的作用已被深入研究。这三种同工酶由三个不同的基因编码，位于三个不同的染色体上，并催化 P5C 在 NAD（P）H 依赖性还原为 Pro，这对于氧化还原势在线粒体和细胞之间的转移很重要。该综述总结了目前对这三种人类 PYCR 同工酶及其在疾病中的作用的理解，重点是癌症。
