Changing stereochemistry for a metabolic pathway in vivo: experiments with the peroxisomal beta-oxidation in yeast

The biosphere is inherently built of chiral molecules, and once their metabolism is established, the stereochemical course of the reactions involved is seen to remain highly conserved. However, by replacing the yeast peroxisomal multifunctional enzyme (MFE), which catalyzes the second and third reac...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-11, Vol.270 (46), p.27453-27457
Main Authors: Filppula, S.A. (University of Oulu, Oulu, Finland.), Sormunen, R.T, Hartig, A, Kunau, W.H, Hiltunen, J.K
Format: Article
Language:English
Subjects:
3-Hydroxyacyl CoA Dehydrogenases
ACIDE OLEIQUE
ACIDO OLEICO
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
ALCOHOL DESHIDROGENASA
ALCOOL DESHYDROGENASE
Amino Acid Sequence
Animals
Base Sequence
CHIMIE
Enoyl-CoA Hydratase
Genetic Complementation Test
GENETICA
GENETIQUE
IMMUNOLOGIE
INMUNOLOGIA
Isomerases
Kinetics
LIASAS
LYASE
Microbodies - metabolism
Microscopy, Immunoelectron
Molecular Sequence Data
Multienzyme Complexes - analysis
Multienzyme Complexes - biosynthesis
Multienzyme Complexes - metabolism
Oligodeoxyribonucleotides
ORGANITE CELLULAIRE
ORGANULOS CITOPLASMICOS
OXIDACION
Oxidation-Reduction
OXYDATION
Peroxisomal Bifunctional Enzyme
PLASMIDE
PLASMIDIOS
Plasmids
QUIMICA
RAT
RATA
Rats
Recombinant Proteins - analysis
Recombinant Proteins - biosynthesis
Recombinant Proteins - metabolism
Restriction Mapping
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Stereoisomerism
Substrate Specificity
TRANSFERENCIA DE GENES
TRANSFERT DE GENE
TRANSFORMACION GENETICA
TRANSFORMATION GENETIQUE
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Summary:The biosphere is inherently built of chiral molecules, and once their metabolism is established, the stereochemical course of the reactions involved is seen to remain highly conserved. However, by replacing the yeast peroxisomal multifunctional enzyme (MFE), which catalyzes the second and third reactions of beta-oxidation of fatty acids via D-3-hydroxyacyl-CoA intermediates, with rat peroxisomal MFE, which catalyzes the same reactions via L-3-hydroxy intermediates, it was possible to change the chiralities of the intermediates in a major metabolic pathway in vivo. Both stereochemical alternatives allowed the yeast cells to grow on oleic acid, implying that when the beta-oxidation pathways evolved, the overall function was the determining factor for the acquisition of MFEs and not the stereospecificities of the reactions themselves
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.46.27453