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Leucoanthocyanidin reductase

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Leucoanthocyanidin reductase
Identifiers
EC no.1.17.1.3
CAS no.93389-48-1
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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 {\displaystyle \rightleftharpoons } 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).

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

Other oxidoreductases (EC 1.15–1.21)
1.15: Acting on superoxide as acceptor
1.16: Oxidizing metal ions
1.17: Acting on CH or CH2 groups
1.18: Acting on iron–sulfur proteins as donors
1.19: Acting on reduced flavodoxin as donor
1.20: Acting on phosphorus or arsenic in donors
1.21: Acting on X-H and Y-H to form an X-Y bond
Enzymes
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