Recombinant Human P5CS protein (His-DHFR tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Pyrroline-5-carboxylate synthetase (P5CS) also known as ALDH18A1 plays an important role in proline biosynthesis. This enzyme catalyzes the conversion of glutamate to pyrroline-5-carboxylate. The P5CS protein has a molecular mass of approximately 87 kDa and is mainly expressed in tissues with high rates of protein synthesis such as the liver and kidney. It has significant expression in the mitochondria reinforcing its function in energy metabolism and amino acid biosynthesis.

Biological function summary

P5CS influences cellular responses to oxidative stress due to its role in proline metabolism and redox balance. As part of the proline synthesis pathway P5CS contributes to the production of proline a critical amino acid for protein synthesis. Proline acts as an osmoprotectant and plays a role in cellular structure. P5CS operates within a complex pathway regulating amino acids acting cooperatively with other proteins involved in synthesis processes.

Pathways

P5CS is integral to the proline biosynthetic pathway and is linked to the glutamate pathway. Its activity closely coordinates with the functioning of enzymes like pyrroline-5-carboxylate reductase which converts pyrroline-5-carboxylate to proline. This relationship ensures the continuous supply of proline vital for collagen synthesis and also intersects with pathways involving protein metabolism and cellular stress responses.

Altered P5CS function associates with conditions like cutis laxa and hyperprolinemia. Mutations in the P5CS gene can lead to dysfunction in proline metabolism resulting in elastic skin joint and bone issues and mental retardation in some individuals. The enzyme's interaction with proteins such as the collagen metabolism enzymes highlights its relevance in dermatological and connective tissue disorders.