8OF7

Cyc15 Diels Alderase

8OF7 の概要

• エントリーDOI: 10.2210/pdb8of7/pdb
• 分子名称: Rhs family protein, IMIDAZOLE, DI(HYDROXYETHYL)ETHER, ... (8 entities in total)
• 機能のキーワード: diels alderase, cyclase, dimer, ligase
• 由来する生物種: Streptomyces sp. NL15-2K
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35680.01

構造登録者

Back, C.R.,Barringer, R.W.L.,Zorn, K.,Manzo-Ruiz, M.,Race, P.R. (登録日: 2023-03-14, 公開日: 2023-06-21, 最終更新日: 2024-06-19)

主引用文献

Zorn, K.,Back, C.R.,Barringer, R.,Chadimova, V.,Manzo-Ruiz, M.,Mbatha, S.Z.,Mobarec, J.C.,Williams, S.E.,van der Kamp, M.W.,Race, P.R.,Willis, C.L.,Hayes, M.A.
Interrogation of an Enzyme Library Reveals the Catalytic Plasticity of Naturally Evolved [4+2] Cyclases.
Chembiochem, 24:e202300382-e202300382, 2023

PubMed Abstract: Stereoselective carbon-carbon bond forming reactions are quintessential transformations in organic synthesis. One example is the Diels-Alder reaction, a [4+2] cycloaddition between a conjugated diene and a dienophile to form cyclohexenes. The development of biocatalysts for this reaction is paramount for unlocking sustainable routes to a plethora of important molecules. To obtain a comprehensive understanding of naturally evolved [4+2] cyclases, and to identify hitherto uncharacterised biocatalysts for this reaction, we constructed a library comprising forty-five enzymes with reported or predicted [4+2] cycloaddition activity. Thirty-one library members were successfully produced in recombinant form. In vitro assays employing a synthetic substrate incorporating a diene and a dienophile revealed broad-ranging cycloaddition activity amongst these polypeptides. The hypothetical protein Cyc15 was found to catalyse an intramolecular cycloaddition to generate a novel spirotetronate. The crystal structure of this enzyme, along with docking studies, establishes the basis for stereoselectivity in Cyc15, as compared to other spirotetronate cyclases.

PubMed: 37305956
DOI: 10.1002/cbic.202300382

実験手法

X-RAY DIFFRACTION (1.66 Å)