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EC Number
General Information
Commentary
Reference
evolution
the enzyme belongs to the AKR13D subfamily of the aldo-keto reductases, evolutionary relationship of AKR13D from Rauvolfia serpentina to annotated AKR families and subfamilies
more
the active site is formed by the catalytic tetrad Asp52, Tyr57, Lys84, and His126 at the center of the (alpha/beta)8-barrel structure. Upon NADPH binding, dramatic conformational changes and movements are observed: two additional beta-strands in the C terminus become ordered to form one alpha-helix, and a movement of up to 24 A occurs. This conformational change creates a large space that allows the binding of substrates of variable size for PR and enhances the enzyme activity
physiological function
perakine reductase catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis
Results 1 - 3 of 3