PDBsum entry 3zph

Isomerase

PDB id: 3zph

Contents

Protein chains

260 a.a.

282 a.a.

Ligands

GOL ×5

Metals

_CL ×4

Waters ×1062

PDB id:

3zph

Name:

Isomerase

Title:

Bacterial chalcone isomerase in closed conformation from eubacterium ramulus at 2.8 a resolution

Structure:

Chalcone isomerase. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Eubacterium ramulus. Organism_taxid: 39490. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta

Resolution:

2.80Å R-factor: 0.250 R-free: 0.297

Authors:

M.Thomsen,G.J.Palm,W.Hinrichs

Key ref:

M.Gall et al. (2014). Enzymatic conversion of flavonoids using bacterial chalcone isomerase and enoate reductase. Angew Chem Int Ed Engl, 53, 1439-1442. PubMed id: 24459060 DOI: 10.1002/anie.201306952

Date:

27-Feb-13 Release date: 15-Jan-14

Protein chains

U2Q8X2  (U2Q8X2_EUBRA) -  Chalcone isomerase N-terminal domain-containing protein from Eubacterium ramulus ATCC 29099

Seq: 283 a.a.

Struc: 260 a.a.*

Protein chain

U2Q8X2  (U2Q8X2_EUBRA) -  Chalcone isomerase N-terminal domain-containing protein from Eubacterium ramulus ATCC 29099

Seq: 283 a.a.

Struc: 282 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, C, D, E, F: E.C.5.5.1.6 - chalcone isomerase.
• Pathway: Flavonoid Biosynthesis
• Reaction: a chalcone = a flavanone

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1002/anie.201306952

Angew Chem Int Ed Engl 53:1439-1442 (2014)

PubMed id: 24459060

Enzymatic conversion of flavonoids using bacterial chalcone isomerase and enoate reductase.

M.Gall, M.Thomsen, C.Peters, I.V.Pavlidis, P.Jonczyk, P.P.Grünert, S.Beutel, T.Scheper, E.Gross, M.Backes, T.Geissler, J.P.Ley, J.M.Hilmer, G.Krammer, G.J.Palm, W.Hinrichs, U.T.Bornscheuer.

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.