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Asymmetric acyloin condensation catalysed by phenylpyruvate decarboxylase. Part 2: Substrate specificity and purification of the enzyme
- Source :
- Tetrahedron: Asymmetry. 12:571-577
- Publication Year :
- 2001
- Publisher :
- Elsevier BV, 2001.
-
Abstract
- Phenylpyruvate decarboxylase from Achromobacter eurydice was used to catalyse the asymmetric acyloin condensation of phenylpyruvate 1 with various aldehydes 2 to produce optically active acyloins PhCH2COCH(OH)R 3. The specific activity of the phenylpyruvate decarboxylase enzyme was increased by a factor of 332 after its purification. The molecular weight of the purified enzyme was shown to be 150 kDa by gel filtration chromatography, while SDS gel electrophoresis showed two sub-units with molecular weights of 90 and 40 kDa. The acyloin condensation yield decreased with increasing chain length for straight chain aliphatic aldehydes from 76% for acetaldehyde to 24% for valeraldehyde. The e.e.s of the acyloin products were 87–98%. Low yields of acyloin products were obtained with chloroacetaldehyde (13%) and glycoaldehyde (16%). Indole-3-pyruvate was a substrate of the enzyme and provided acyloin condensation product 3-hydroxy-1-(3-indolyl)-2-butanone 5 with acetaldehyde in 19% yield, while benzoylformate was not a substrate for the enzyme.
- Subjects :
- chemistry.chemical_classification
Phenylpyruvate decarboxylase
Chemistry
Acyloin condensation
Organic Chemistry
Size-exclusion chromatography
Acetaldehyde
Substrate (chemistry)
Catalysis
Inorganic Chemistry
chemistry.chemical_compound
Enzyme
Yield (chemistry)
Organic chemistry
Physical and Theoretical Chemistry
Polyacrylamide gel electrophoresis
Subjects
Details
- ISSN :
- 09574166
- Volume :
- 12
- Database :
- OpenAIRE
- Journal :
- Tetrahedron: Asymmetry
- Accession number :
- edsair.doi...........ae65c0eb073abe1b4813a52ffa07239d