Leucoanthocyanidin reductase

Enzyme From Wikipedia, the free encyclopedia

Leucoanthocyanidin reductase (EC 1.17.1.3) (LAR, aka leucocyanidin reductase or LCR) is an enzyme that catalyzes several related chemical reduction steps in flavonoid biosynthesis. For example, it converts leucocyanidin to catechin.[1]

+ NADPH
 
 
H+
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
+ NADP+
 

The three substrates of this enzyme are leucocyanidin, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and a proton. Its products are catechin, oxidised NADP+, and water.[2][3]

This enzyme is an oxidoreductase, with the systematic name (2R,3S)-catechin:NADP+ 4-oxidoreductase. It is also called leucocyanidin reductase.

Other reactions catalysed

The enzyme also converts leucopelargonidin to afzelechin and leucodelphinidin to gallocatechol:[1][2]

+ NADPH
 
 
H+
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
+ NADP+
 
+ NADPH
 
 
H+
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
+ NADP+
 

It can be found in the plant Hedysarum sulphurescens and in Vitis vinifera (grape).[4]

References

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