5G4K

Phloroglucinol reductase from Clostridium sp. apo-form

Summary for 5G4K

• Entry DOI: 10.2210/pdb5g4k/pdb
• Related: 5G4L
• Descriptor: OXIDOREDUCTASE, SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY PROTEIN (3 entities in total)
• Functional Keywords: oxidoreductase, flavonoid degradation, enzyme catalysis, dearomatisation reaction, short-chain dehydrogenases/reductases, nadph dependent enzyme
• Biological source: CLOSTRIDIUM SP.; More
• Total number of polymer chains: 2
• Total formula weight: 62266.49

Authors

Conradt, D.,Hermann, B.,Gerhardt, S.,Einsle, O.,Mueller, M. (deposition date: 2016-05-13, release date: 2016-12-07, Last modification date: 2024-01-10)

Primary citation

Conradt, D.,Hermann, B.,Gerhardt, S.,Einsle, O.,Mueller, M.
Biocatalytic Properties and Structural Analysis of Phloroglucinol Reductases.
Angew.Chem.Int.Ed.Engl., 55:15531-, 2016

PubMed Abstract: Phloroglucinol reductases (PGRs) are involved in anaerobic degradation in bacteria, in which they catalyze the dearomatization of phloroglucinol into dihydrophloroglucinol. We identified three PGRs, from different bacterial species, that are members of the family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDRs). In addition to catalyzing the reduction of the physiological substrate, the three enzymes exhibit activity towards 2,4,6-trihydroxybenzaldehyde, 2,4,6-trihydroxyacetophenone, and methyl 2,4,6-trihydroxybenzoate. Structural elucidation of PGRcl and comparison to known SDRs revealed a high degree of conservation. Several amino acid positions were identified as being conserved within the PGR subfamily and might be involved in substrate differentiation. The results enable the enzymatic dearomatization of monoaromatic phenol derivatives and provide insight into the functional diversity that may be found in families of enzymes displaying a high degree of structural homology.

PubMed: 27874239
DOI: 10.1002/ANIE.201607494

Experimental method

X-RAY DIFFRACTION (1.74 Å)