CATH Domain 1qydD01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.50	Rossmann fold
	3.40.50.720	NAD(P)-binding Rossmann-like Domain

Domain Context

CATH Clusters

Superfamily	NAD(P)-binding Rossmann-like Domain
Functional Family	Bifunctional pinoresinol-lariciresinol reductase 1

Enzyme Information

1.23.1.3	(-)-pinoresinol reductase. based on mapping to UniProt Q9LD14 (-)-lariciresinol + NADP(+) = (-)-pinoresinol + NADPH. -!- The reaction is catalyzed in vivo in the opposite direction to that shown. -!- A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol (EC 1.23.1.4). -!- Isolated from the plants Thuja plicata (western red cedar), Linum perenne (perennial flax) and Arabidopsis thaliana (thale cress).
1.23.1.4	(-)-lariciresinol reductase. based on mapping to UniProt Q9LD14 (+)-secoisolariciresinol + NADP(+) = (-)-lariciresinol + NADPH. -!- The reaction is catalyzed in vivo in the opposite direction to that shown. -!- A multifunctional enzyme that also reduces (-)-pinoresinol (EC 1.23.1.3). -!- Isolated from the plants Thuja plicata (western red cedar) and Linum corymbulosum.
1.23.1.1	(+)-pinoresinol reductase. based on mapping to UniProt Q9LD14 (+)-lariciresinol + NADP(+) = (+)-pinoresinol + NADPH. -!- The reaction is catalyzed in vivo in the opposite direction to that shown. -!- A multifunctional enzyme that further reduces the product to the lignan (-)-secoisolariciresinol (EC 1.23.1.2). -!- Isolated from the plants Forsythia intermedia, Thuja plicata (western red cedar), Linum perenne (perennial flax) and Linum corymbulosum. -!- The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol.

UniProtKB Entries (1)

PILR1_THUPL

Thuja plicata

Bifunctional pinoresinol-lariciresinol reductase 1

PDB Structure

PDB	1QYD
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. Min, T., Kasahara, H., Bedgar, D.L., Youn, B., Lawrence, P.K., Gang, D.R., Halls, S.C., Park, H., Hilsenbeck, J.L., Davin, L.B., Lewis, N.G., Kang, C. J.Biol.Chem.