8RPG
Crystal structure of an alcohol oxidase from Streptomyces hiroshimensis
Summary for 8RPG
| Entry DOI | 10.2210/pdb8rpg/pdb |
| Descriptor | Alcohol oxidase, FLAVIN-ADENINE DINUCLEOTIDE, TRIETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | alcohol oxidase, streptomyces hiroshimensis, oxidoreductase, flavoprotein |
| Biological source | Streptomyces hiroshimensis |
| Total number of polymer chains | 1 |
| Total formula weight | 58217.86 |
| Authors | Martinez-Julvez, M.,Ferreira, P.,Cinca-Fernando, P. (deposition date: 2024-01-15, release date: 2024-11-13) |
| Primary citation | Cinca-Fernando, P.,Ascaso-Alegre, C.,Sevilla, E.,Martinez-Julvez, M.,Mangas-Sanchez, J.,Ferreira, P. Discovery, characterization, and synthetic potential of two novel bacterial aryl-alcohol oxidases. Appl.Microbiol.Biotechnol., 108:498-498, 2024 Cited by PubMed Abstract: The search for novel synthetic tools to prepare industrial chemicals in a safer and greener manner is a continuing challenge in synthetic chemistry. In this manuscript, we report the discovery, characterization, and synthetic potential of two novel aryl-alcohol oxidases from bacteria which are able to oxidize a variety of aliphatic and aromatic alcohols with efficiencies up to 4970 min mM. Both enzymes have shown a reasonable thermostability (thermal melting temperature values of 50.9 and 48.6 °C for ShAAO and SdAAO, respectively). Crystal structures revealed an unusual wide-open entrance to the active-site pockets compared to that previously described for traditional fungal aryl-alcohol oxidases, which could be associated with differences observed in substrate scope, catalytic efficiency, and other functional properties. Preparative-scale reactions and the ability to operate at high substrate loadings also demonstrate the potential of these enzymes in synthetic chemistry with total turnover numbers > 38000. Moreover, their availability as soluble and active recombinant proteins enabled their use as cell-free extracts which further highlights their potential for the large-scale production of carbonyl compounds. KEY POINTS: • Identification and characterization of two novel bacterial aryl-alcohol oxidases • Crystal structures reveal wide-open active-site pockets, impacting substrate scope • Total turnover numbers and cell-free extracts demonstrate the synthetic potential. PubMed: 39470785DOI: 10.1007/s00253-024-13314-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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