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 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]

Related Research Articles

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<span class="mw-page-title-main">Leucoanthocyanidin</span> Chemical compound

Leucoanthocyanidin (flavan-3,4-diols) are colorless chemical compounds related to anthocyanidins and anthocyanins. Leucoanthocyanins can be found in Anadenanthera peregrina and in several species of Nepenthes including N. burbidgeae, N. muluensis, N. rajah, N. tentaculata, and N. × alisaputrana.

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Leucocyanidin is a colorless chemical compound that is a member of the class of natural products known as leucoanthocyanidins.

<span class="mw-page-title-main">Leucopelargonidin</span> Chemical compound

Leucopelargonidin is a colorless chemical compound related to leucoanthocyanins. It can be found in Albizia lebbeck, in the fruit of Anacardium occidentale (Cashew), in the fruit of Areca catechu, in the fruit of Hydnocarpus wightiana, in the rhizome of Rumex hymenosepalus, in Zea mays (Corn) and in Ziziphus jujuba.

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