6AGZ

Crystal structure of Old Yellow Enzyme from Pichia sp. AKU4542

Summary for 6AGZ

• Entry DOI: 10.2210/pdb6agz/pdb
• Descriptor: Old Yellow Enzyme, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: tim barrel motif, dehydrogenase, flavoprotein, oxidoreductase
• Biological source: Pichia
• Total number of polymer chains: 2
• Total formula weight: 91448.70

Authors

Horita, S.,Kataoka, M.,Kitamura, N.,Nakagawa, T.,Miyakawa, T.,Ohtsuka, J.,Nagata, K.,Shimizu, S.,Tanokura, M. (deposition date: 2018-08-15, release date: 2019-06-26, Last modification date: 2024-03-27)

Primary citation

Horita, S.,Kataoka, M.,Kitamura, N.,Miyakawa, T.,Ohtsuka, J.,Maejima, Y.,Shimomura, K.,Nagata, K.,Shimizu, S.,Tanokura, M.
Structural basis of different substrate preferences of two old yellow enzymes from yeasts in the asymmetric reduction of enone compounds.
Biosci.Biotechnol.Biochem., 83:456-462, 2019

PubMed Abstract: Old yellow enzymes (OYEs) are potential targets of protein engineering for useful biocatalysts because of their excellent asymmetric reductions of enone compounds. Two OYEs from different yeast strains, Candida macedoniensis AKU4588 OYE (CmOYE) and Pichia sp. AKU4542 OYE (PsOYE), have a sequence identity of 46%, but show different substrate preferences; PsOYE shows 3.4-fold and 39-fold higher catalytic activities than CmOYE toward ketoisophorone and (4S)-phorenol, respectively. To gain insights into structural basis of their different substrate preferences, we have solved a crystal structure of PsOYE, and compared its catalytic site structure with that of CmOYE, revealing the catalytic pocket of PsOYE is wider than that of CmOYE due to different positions of Phe (PsOYE)/Phe (CmOYE) in static Loop 5. This study shows a significance of 3D structural information to explain the different substrate preferences of yeast OYEs which cannot be understood from their amino acid sequences. Abbreviations: OYE: Old yellow enzymes, CmOYE: Candida macedoniensis AKU4588 OYE, PsOYE: Pichia sp. AKU4542 OYE.

PubMed: 30445889
DOI: 10.1080/09168451.2018.1543014

Experimental method

X-RAY DIFFRACTION (2 Å)