Leucoanthocyanidin reductase
| Leucoanthocyanidin reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.17.1.3 | ||||||||
| CAS number | 93389-48-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
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
- ↑ 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. PMID 20138891. doi:10.1016/j.jmb.2010.02.002.
Further reading
- Tanner GJ, Kristiansen KN (1993). "Synthesis of 3,4-cis-[3H]leucocyanidin and enzymatic reduction to catechin". Anal. Biochem. 209 (2): 274–7. PMID 8470799. doi:10.1006/abio.1993.1119.
- 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 (34): 31647–56. PMID 12788945. doi:10.1074/jbc.M302783200.
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