7YCF
HYDROXYNITRILE LYASE FROM THE MILLIPEDE, Oxidus gracilis IN ACETONITRILE
Summary for 7YCF
| Entry DOI | 10.2210/pdb7ycf/pdb |
| Descriptor | Hydroxynitrile lyase, 2-HYDROXY-2-METHYLPROPANENITRILE, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | lyase |
| Biological source | Oxidus gracilis |
| Total number of polymer chains | 4 |
| Total formula weight | 83903.63 |
| Authors | Chaikaew, S.,Watanabe, Y.,Zheng, D.,Motojima, F.,Asano, Y. (deposition date: 2022-07-01, release date: 2024-01-24, Last modification date: 2024-10-23) |
| Primary citation | Chaikaew, S.,Watanabe, Y.,Zheng, D.,Motojima, F.,Yamaguchi, T.,Asano, Y. Structure-Based Site-Directed Mutagenesis of Hydroxynitrile Lyase from Cyanogenic Millipede, Oxidus gracilis for Hydrocyanation and Henry Reactions. Chembiochem, 25:e202400118-e202400118, 2024 Cited by PubMed Abstract: Hydroxynitrile lyase (HNL) from the cyanogenic millipede Oxidus gracillis (OgraHNL) is a crucial enzyme in the cyanogenesis pathway. Here, the crystal structures of OgraHNL complexed with sulfate, benzaldehyde (BA), (R)-mandelonitrile ((R)-Man), (R)-2-chloromandelonitrile ((R)-2-Cl-Man), and acetone cyanohydrin (ACN) were solved at 1.6, 1.7, 2.3, 2.1, and 2.0 Å resolutions, respectively. The structure of OgraHNL revealed that it belonged to the lipocalin superfamily. Based on this structure, positive variants were designed to further improve the catalytic activity and enantioselectivity of the enzyme for asymmetric hydrocyanation and Henry reactions. PubMed: 38526556DOI: 10.1002/cbic.202400118 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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