Structures of l-proline trans-hydroxylase reveal the catalytic specificity and provide deeper insight into AKG-dependent hydroxylation

l-Proline hydroxylase is a member of the non-heme Fe2+/ α -ketoglutarate (AKG)-dependent hydroxylase family that catalyzes the reaction from l-proline to hydroxy-l-proline, which is widely used in drug synthesis, biochemistry, food supplementation and cosmetic industries. Here, the first crystal structure of l-proline trans-hydroxylase and its complexes with substrate and product are reported, which reveal the structural basis of trans – cis proline hydroxylation selectivity. Structure comparison with other AKG-dependent hydroxylases identifies conserved amino acid residues, which may serve as signatures of in-line or off-line AKG binding modes in the AKG-dependent enzyme family.

Source: Acta Crystallographica Section D - March 28, 2023 Category: Biochemistry Authors: Hu, X. Huang, X. Liu, J. Zheng, P. Gong, W. Yang, L. Tags: AKG-dependent hydroxylases hydroxy-l-proline l-proline trans-hydroxylases – cis proline hydroxylation selectivity catalytic specificity AKG binding modes research papers Source Type: research