6533b861fe1ef96bd12c4e98
RESEARCH PRODUCT
Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants
Joachim StöckigtJoachim StöckigtCindy RosenthalSantosh PanjikarYu ZhaoMartin RuppertLianli SunLianli SunUwe Muellersubject
endocrine systemStereochemistryAldo-Keto ReductasesBiophysicsAlcohol oxidoreductaseReductaseCrystallography X-Raymedicine.disease_causeBiochemistryRauwolfiachemistry.chemical_compoundBiosynthesisAldehyde ReductaseStructural BiologyRauvolfia serpentinaGeneticsmedicineEscherichia colichemistry.chemical_classificationAldo-keto reductasebiologyCondensed Matter Physicsbiology.organism_classificationAlcohol OxidoreductasesEnzymeBiochemistrychemistryCrystallization CommunicationsHeterologous expressionCrystallizationdescription
Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C222(1) and diffract to 2.0 A, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 A.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2006-09-22 | Acta Crystallographica Section F Structural Biology and Crystallization Communications |