KEGG   ENZYME: 1.23.1.3Help
Entry
EC 1.23.1.3                 Enzyme                                 

Name
(-)-pinoresinol reductase;
pinoresinol/lariciresinol reductase;
pinoresinol-lariciresinol reductases;
(-)-pinoresinol-(-)-lariciresinol reductase;
PLR
Class
Oxidoreductases;
Reducing C-O-C group as acceptor;
With NADH or NADPH as donor
BRITE hierarchy
Sysname
(-)-lariciresinol:NADP+ oxidoreductase
Reaction(IUBMB)
(-)-lariciresinol + NADP+ = (-)-pinoresinol + NADPH + H+ [RN:R10227]
Reaction(KEGG)
Substrate
(-)-lariciresinol [CPD:C20454];
NADP+ [CPD:C00006]
Product
(-)-pinoresinol [CPD:C20455];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The reaction is catalysed 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, (-)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3].
History
EC 1.23.1.3 created 2013
Reference
1  [PMID:9872995]
  Authors
Fujita M, Gang DR, Davin LB, Lewis NG
  Title
Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions.
  Journal
J. Biol. Chem. 274 (1999) 618-27.
  Sequence
Reference
2  [PMID:17257599]
  Authors
Hemmati S, Schmidt TJ, Fuss E
  Title
(+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B.
  Journal
FEBS. Lett. 581 (2007) 603-10.
Reference
3  [PMID:18347017]
  Authors
Nakatsubo T, Mizutani M, Suzuki S, Hattori T, Umezawa T
  Title
Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis.
  Journal
J. Biol. Chem. 283 (2008) 15550-7.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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