3ZPH

Bacterial chalcone isomerase in closed conformation from Eubacterium ramulus at 2.8 A resolution

Summary for 3ZPH

• Entry DOI: 10.2210/pdb3zph/pdb
• Descriptor: CHALCONE ISOMERASE, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: isomerase, flavonoid degradation
• Biological source: EUBACTERIUM RAMULUS
• Total number of polymer chains: 6
• Total formula weight: 195042.70

Authors

Thomsen, M.,Palm, G.J.,Hinrichs, W. (deposition date: 2013-02-27, release date: 2014-01-15, Last modification date: 2023-12-20)

Primary citation

Gall, M.,Thomsen, M.,Peters, C.,Pavlidis, I.V.,Jonczyk, P.,Grunert, P.P.,Beutel, S.,Scheper, T.,Gross, E.,Backes, M.,Geissler, T.,Ley, J.P.,Hilmer, J.M.,Krammer, G.,Palm, G.J.,Hinrichs, W.,Bornscheuer, U.T.
Enzymatic conversion of flavonoids using bacterial chalcone isomerase and enoate reductase.
Angew.Chem.Int.Ed.Engl., 53:1439-1442, 2014

PubMed Abstract: Flavonoids are a large group of plant secondary metabolites with a variety of biological properties and are therefore of interest to many scientists, as they can lead to industrially interesting intermediates. The anaerobic gut bacterium Eubacterium ramulus can catabolize flavonoids, but until now, the pathway has not been experimentally confirmed. In the present work, a chalcone isomerase (CHI) and an enoate reductase (ERED) could be identified through whole genome sequencing and gene motif search. These two enzymes were successfully cloned and expressed in Escherichia coli in their active form, even under aerobic conditions. The catabolic pathway of E. ramulus was confirmed by biotransformations of flavanones into dihydrochalcones. The engineered E. coli strain that expresses both enzymes was used for the conversion of several flavanones, underlining the applicability of this biocatalytic cascade reaction.

PubMed: 24459060
DOI: 10.1002/anie.201306952

Experimental method

X-RAY DIFFRACTION (2.8 Å)