1.1.1.317: perakine reductase
This is an abbreviated version!
For detailed information about perakine reductase, go to the full flat file.
Reaction
Synonyms
AKR13D1
ECTree
1.1.1.317 perakine reductaseAdvanced search results
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General Information on EC 1.1.1.317 - perakine reductase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
additional information
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
evolution
the enzyme is a member of aldo-ketone reductase (AKR) 13D family
additional information
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
additional information
molecular modeling of the reaction mechansim. In the model, the oxygen atom of the product's hydroxy group approaches the carboxamide group of NADPH, located within a hydrogen-bond distance of the gamma-N of the imidazole ring of His126. Substrate binding analysis: the large pocket is formed by the surface of residues Ile56, Ile87, Ile 90, His126, and Arg127, the three clustered Ile residues contributing to the hydrophobic property of the pocket may facilitate substrate binding, the small pocket comprises the surface of the Met21, Tyr57, and Lys84 residues, together with the nicotinamide riboside component of NADPH
