Leucoanthocyanidin reductase explained
| Leucoanthocyanidin reductase |
| Ec Number: | 1.17.1.3 |
| Cas Number: | 93389-48-1 |
| Go Code: | 0033788 |
In enzymology, a leucoanthocyanidin reductase (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]
Further reading
- Tanner GJ, Kristiansen KN . 1993 . Synthesis of 3,4-cis-[3H]leucocyanidin and enzymatic reduction to catechin . Anal. Biochem. . 209 . 274 - 7 . 8470799 . 10.1006/abio.1993.1119 . 2 .
- Tanner GJ, Francki KT, Abrahams S, Watson JM, Larkin PJ, Ashton AR . 2003 . Proanthocyanidin biosynthesis in plants. Purification of legume leucoanthocyanidin reductase and molecular cloning of its cDNA . J. Biol. Chem. . 278 . 31647 - 56 . 12788945 . 10.1074/jbc.M302783200 . 34 . free .
Notes and References
- Maugé C, Granier T, d'Estaintot BL, Gargouri M, Manigand C, Schmitter JM, Chaudière J, Gallois B . Crystal Structure and Catalytic Mechanism of Leucoanthocyanidin Reductase from Vitis vinifera . J. Mol. Biol. . 397 . 4 . 1079–91 . April 2010 . 20138891 . 10.1016/j.jmb.2010.02.002 .
