9TM7

Unspecific Peroxygenase from Daldinia childiae

Summary for 9TM7

• Entry DOI: 10.2210/pdb9tm7/pdb
• Descriptor: Unspecific Peroxygenase, MAGNESIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, heme, unspecific peroxygenase
• Biological source: Daldinia childiae
• Total number of polymer chains: 2
• Total formula weight: 62484.05

Authors

McKenzie, A.,Clark, C.,Melling, B.,Domenech, J.,Grogan, G. (deposition date: 2025-12-12, release date: 2026-07-29)

Primary citation

McKenzie, A.,Clark, C.,Cornish, K.A.S.,Li, J.,Domenech, J.,Melling, B.,Ralston, M.P.H.,Cartwright, J.,Mulholland, N.P.,Unsworth, W.P.,Grogan, G.
Structure, characterisation and application of an unspecific peroxygenase from Daldinia childiae.
Rsc Chem Biol, 2026

PubMed Abstract: Unspecific peroxygenases (UPOs) have emerged as useful biocatalysts for the scalable and selective oxygenation of a large variety of organic molecules. UPOs have been divided into family I and family II enzymes, dependent upon sequence similarity and molecular weight, with family I being shorter in sequence. Here we report the characterisation and application of the family I UPO from (UPO). The enzyme was expressed in both and , yielding protein for kinetic and structural studies and biocatalytic application respectively. The structure of the enzyme revealed notable differences in the active site tunnel, compared with the well-studied family I artUPO, including F79 for V69 and F171 for I160. Notably, these differences were manifested in selectivity divergent from other UPOs when UPO was applied to preparative biotransformations; for example, (-)-menthol was converted exclusively into -6-hydroxymenthol in contrast to artUPO, which gave exclusively the tertiary alcohol 2,8-menthanediol.

PubMed: 42328014
DOI: 10.1039/d6cb00141f

Experimental method

X-RAY DIFFRACTION (1.88 Å)