To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC 1.23.1.1

Accepted Name
(+)-pinoresinol reductase.
Alternative Name(s)
(+)-pinoresinol-(+)-lariciresinol reductase.
(+)-pinoresinol/(+)-lariciresinol.
Pinoresinol-lariciresinol reductases.
Pinoresinol/lariciresinol reductase.
Reaction catalysed
(+)-lariciresinol + NADP(+) <=> (+)-pinoresinol + NADPH
Comment(s)
  • 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.
Cross-references
BRENDA1.23.1.1
EC2PDB1.23.1.1
ExplorEnz1.23.1.1
PRIAM enzyme-specific profiles1.23.1.1
KEGG Ligand Database for Enzyme Nomenclature1.23.1.1
IUBMB Enzyme Nomenclature1.23.1.1
IntEnz1.23.1.1
MEDLINEFind literature relating to 1.23.1.1
MetaCyc1.23.1.1
UniProtKB/Swiss-Prot
Q9FVQ6, PILR1_ARATH;  P93143, PILR1_FORIN;  Q4R0I0, PILR1_LINAL;  
B5KRH5, PILR1_LINCY;  A3R052, PILR1_LINPE;  Q9LD14, PILR1_THUPL;  
E6Y2X0, PILR2_LINUS;  Q9LD13, PILR2_THUPL;  Q9LD12, PILR4_THUPL;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.23.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.23.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-