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

In enzymology, a leucoanthocyanidin reductase (EC 1.17.1.3) (LAR, aka leucocyanidin reductase or LCR) is an enzyme that catalyzes the chemical reaction

(2R,3S)-catechin + NADP+ + H2O 2,3-trans-3,4-cis-leucocyanidin + NADPH + H+

The 3 substrates of this enzyme are (2R,3S)-catechin, NADP+, and H2O, whereas its 3 products are 2,3-trans-3,4-cis-leucocyanidin, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2R,3S)-catechin:NADP+ 4-oxidoreductase. This enzyme is also called leucocyanidin reductase. This enzyme participates in flavonoid biosynthesis.

The enzyme can be found in the plant Hedysarum sulphurescens and in Vitis vinifera (grape).[1]

References

  1. Maugé C, Granier T, d'Estaintot BL, Gargouri M, Manigand C, Schmitter JM, Chaudière J, Gallois B (April 2010). "Crystal Structure and Catalytic Mechanism of Leucoanthocyanidin Reductase from Vitis vinifera". J. Mol. Biol. 397 (4): 1079–91. doi:10.1016/j.jmb.2010.02.002. PMID 20138891.

Further reading


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