Structural highlights
Function
S5TUM1_9BACT
Publication Abstract from PubMed
L-Proline hydroxylase is a member of the non-heme Fe(2+)/alpha-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.
Structures of L-proline trans-hydroxylase reveal the catalytic specificity and provide deeper insight into AKG-dependent hydroxylation.,Hu X, Huang X, Liu J, Zheng P, Gong W, Yang L Acta Crystallogr D Struct Biol. 2023 Apr 1;79(Pt 4):318-325. doi: , 10.1107/S2059798323001936. Epub 2023 Mar 28. PMID:36974966[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hu X, Huang X, Liu J, Zheng P, Gong W, Yang L. Structures of L-proline trans-hydroxylase reveal the catalytic specificity and provide deeper insight into AKG-dependent hydroxylation. Acta Crystallogr D Struct Biol. 2023 Apr 1;79(Pt 4):318-325. PMID:36974966 doi:10.1107/S2059798323001936
