Leucoanthocyanidin reductase

Leucoanthocyanidin reductase
Identifiers
EC no.1.17.1.3
CAS no.93389-48-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Leucoanthocyanidin reductase (EC 1.17.1.3) (LAR, aka leucocyanidin reductase or LCR) is an enzyme that catalyzes several related chemical reduction steps in flavonoid biosynthesis. For example, it converts leucocyanidin to catechin.[1]

+ NADPH
 
 
H+
H2O
 
 
 
+ NADP+
 

The three substrates of this enzyme are leucocyanidin, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and a proton. Its products are catechin, oxidised NADP+, and water.[2][3]

This enzyme is an oxidoreductase, with the systematic name (2R,3S)-catechin:NADP+ 4-oxidoreductase. It is also called leucocyanidin reductase.

Other reactions catalysed

The enzyme also converts leucopelargonidin to afzelechin and leucodelphinidin to gallocatechol:[1][2]

+ NADPH
 
 
H+
H2O
 
 
 
+ NADP+
 
+ NADPH
 
 
H+
H2O
 
 
 
+ NADP+
 

It can be found in the plant Hedysarum sulphurescens and in Vitis vinifera (grape).[4]

References

  1. ^ a b Tanner, Gregory J.; Francki, Kathy T.; Abrahams, Sharon; Watson, John M.; Larkin, Philip J.; Ashton, Anthony R. (2003). "Proanthocyanidin Biosynthesis in Plants". Journal of Biological Chemistry. 278 (34): 31647–31656. doi:10.1074/jbc.M302783200. PMID 12788945.
  2. ^ a b Enzyme 1.17.1.3 at KEGG Pathway Database.
  3. ^ Tanner, G.J.; Kristiansen, K.N. (1993). "Synthesis of 3,4-cis-[3H]Leucocyanidin and Enzymatic Reduction to Catechin". Analytical Biochemistry. 209 (2): 274–277. doi:10.1006/abio.1993.1119. PMID 8470799.
  4. ^ Maugé, Chloé; Granier, Thierry; d'Estaintot, Béatrice Langlois; Gargouri, Mahmoud; Manigand, Claude; Schmitter, Jean-Marie; Chaudière, Jean; Gallois, Bernard (2010). "Crystal Structure and Catalytic Mechanism of Leucoanthocyanidin Reductase from Vitis vinifera". Journal of Molecular Biology. 397 (4): 1079–1091. doi:10.1016/j.jmb.2010.02.002. PMID 20138891.