PDBsum entry 3wfi

Oxidoreductase

PDB id: 3wfi

Contents

Protein chains

311 a.a.

Waters ×322

PDB id:

3wfi

Name:

Oxidoreductase

Title:

The crystal structure of d-mandelate dehydrogenase

Structure:

2-dehydropantoate 2-reductase. Chain: a, b. Engineered: yes

Source:

Enterococcus faecium. Organism_taxid: 1352. Strain: iam10071. Gene: plg1-0150. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.187 R-free: 0.224

Authors:

A.Miyanaga,S.Fujisawa,N.Furukawa,K.Arai,M.Nakajima,H.Taguchi

Key ref:

A.Miyanaga et al. (2013). The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem Biophys Res Commun, 439, 109-114. PubMed id: 23954635 DOI: 10.1016/j.bbrc.2013.08.019

Date:

19-Jul-13 Release date: 23-Jul-14

Protein chains

E3USM3  (E3USM3_ENTFC) -  2-dehydropantoate 2-reductase from Enterococcus faecium

Seq: 312 a.a.

Struc: 311 a.a.

Enzyme reactions

• Enzyme class: E.C.1.1.1.169 - 2-dehydropantoate 2-reductase.
• Pathway: Coenzyme A Biosynthesis (early stages)
• Reaction: (R)-pantoate + NADP⁺ = 2-dehydropantoate + NADPH + H⁺

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

reference

DOI no: 10.1016/j.bbrc.2013.08.019

Biochem Biophys Res Commun 439:109-114 (2013)

PubMed id: 23954635

The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.

A.Miyanaga, S.Fujisawa, N.Furukawa, K.Arai, M.Nakajima, H.Taguchi.

ABSTRACT

D-Mandelate dehydrogenases (D-ManDHs), belonging to a new d-2-hydroxyacid dehydrogenase family, catalyze the conversion between benzoylformate and d-mandelate using NAD as a coenzyme. We determined the first D-ManDH structure, that of ManDH2 from Enterococcus faecalis IAM10071. The overall structure showed ManDH2 has a similar fold to 2-ketopantoate reductase (KPR), which catalyzes the conversion of 2-ketopantoate to d-pantoate using NADP as a coenzyme. They share conserved catalytic residues, indicating ManDH2 has the same reaction mechanism as KPR. However, ManDH2 exhibits significant structural variations in the coenzyme and substrate binding sites compared to KPR. These structural observations could explain their different coenzyme and substrate specificities.