Lactaldehyde reductase

From Wikipedia, the free encyclopedia

In enzymology, lactaldehyde reductase (EC 1.1.1.77) is an enzyme that catalyzes two chemical reactions

 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
 
 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
 

Each individual reaction is stereospecific so that when the substrate of the enzyme is (R)-propane-1,2-diol it produces (R)-lactaldehyde but the enantiomeric substrate (S)-propane-1,2-diol gives only (S)-lactaldehyde. The enzyme's cofactor is nicotinamide adenine dinucleotide (NAD+), which is converted to NADH, and also releases a proton.[1][2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase. Other names in common use include propanediol:nicotinamide adenine dinucleotide (NAD+) oxidoreductase, and L-lactaldehyde:propanediol oxidoreductase. This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1RRM, 2BI4, and 2BL4.

References

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