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The peroxisomal Acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids.
J Biol Chem. 2006 Apr 28; 281(17):11729-35.JB

Abstract

The role of the Saccharomyces cerevisae peroxisomal acyl-coenzyme A (acyl-CoA) thioesterase (Pte1p) in fatty acid beta-oxidation was studied by analyzing the in vitro kinetic activity of the purified protein as well as by measuring the carbon flux through the beta-oxidation cycle in vivo using the synthesis of peroxisomal polyhydroxyalkanoate (PHA) from the polymerization of the 3-hydroxyacyl-CoAs as a marker. The amount of PHA synthesized from the degradation of 10-cis-heptadecenoic, tridecanoic, undecanoic, or nonanoic acids was equivalent or slightly reduced in the pte1Delta strain compared with wild type. In contrast, a strong reduction in PHA synthesized from heptanoic acid and 8-methyl-nonanoic acid was observed for the pte1Delta strain compared with wild type. The poor catabolism of 8-methyl-nonanoic acid via beta-oxidation in pte1Delta negatively impacted the degradation of 10-cis-heptadecenoic acid and reduced the ability of the cells to efficiently grow in medium containing such fatty acids. An increase in the proportion of the short chain 3-hydroxyacid monomers was observed in PHA synthesized in pte1Delta cells grown on a variety of fatty acids, indicating a reduction in the metabolism of short chain acyl-CoAs in these cells. A purified histidine-tagged Pte1p showed high activity toward short and medium chain length acyl-CoAs, including butyryl-CoA, decanoyl-CoA and 8-methyl-nonanoyl-CoA. The kinetic parameters measured for the purified Pte1p fit well with the implication of this enzyme in the efficient metabolism of short straight and branched chain fatty acyl-CoAs by the beta-oxidation cycle.

Authors+Show Affiliations

Department of Bioproductive Science, Faculty of Agriculture, Utsunomiya University, 350 Minemachi, Utsunomiya 321-8505, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16490786

Citation

Maeda, Isamu, et al. "The Peroxisomal Acyl-CoA Thioesterase Pte1p From Saccharomyces Cerevisiae Is Required for Efficient Degradation of Short Straight Chain and Branched Chain Fatty Acids." The Journal of Biological Chemistry, vol. 281, no. 17, 2006, pp. 11729-35.
Maeda I, Delessert S, Hasegawa S, et al. The peroxisomal Acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids. J Biol Chem. 2006;281(17):11729-35.
Maeda, I., Delessert, S., Hasegawa, S., Seto, Y., Zuber, S., & Poirier, Y. (2006). The peroxisomal Acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids. The Journal of Biological Chemistry, 281(17), 11729-35.
Maeda I, et al. The Peroxisomal Acyl-CoA Thioesterase Pte1p From Saccharomyces Cerevisiae Is Required for Efficient Degradation of Short Straight Chain and Branched Chain Fatty Acids. J Biol Chem. 2006 Apr 28;281(17):11729-35. PubMed PMID: 16490786.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The peroxisomal Acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids. AU - Maeda,Isamu, AU - Delessert,Syndie, AU - Hasegawa,Seiko, AU - Seto,Yoshiaki, AU - Zuber,Sophie, AU - Poirier,Yves, Y1 - 2006/02/20/ PY - 2006/2/24/pubmed PY - 2006/7/6/medline PY - 2006/2/24/entrez SP - 11729 EP - 35 JF - The Journal of biological chemistry JO - J Biol Chem VL - 281 IS - 17 N2 - The role of the Saccharomyces cerevisae peroxisomal acyl-coenzyme A (acyl-CoA) thioesterase (Pte1p) in fatty acid beta-oxidation was studied by analyzing the in vitro kinetic activity of the purified protein as well as by measuring the carbon flux through the beta-oxidation cycle in vivo using the synthesis of peroxisomal polyhydroxyalkanoate (PHA) from the polymerization of the 3-hydroxyacyl-CoAs as a marker. The amount of PHA synthesized from the degradation of 10-cis-heptadecenoic, tridecanoic, undecanoic, or nonanoic acids was equivalent or slightly reduced in the pte1Delta strain compared with wild type. In contrast, a strong reduction in PHA synthesized from heptanoic acid and 8-methyl-nonanoic acid was observed for the pte1Delta strain compared with wild type. The poor catabolism of 8-methyl-nonanoic acid via beta-oxidation in pte1Delta negatively impacted the degradation of 10-cis-heptadecenoic acid and reduced the ability of the cells to efficiently grow in medium containing such fatty acids. An increase in the proportion of the short chain 3-hydroxyacid monomers was observed in PHA synthesized in pte1Delta cells grown on a variety of fatty acids, indicating a reduction in the metabolism of short chain acyl-CoAs in these cells. A purified histidine-tagged Pte1p showed high activity toward short and medium chain length acyl-CoAs, including butyryl-CoA, decanoyl-CoA and 8-methyl-nonanoyl-CoA. The kinetic parameters measured for the purified Pte1p fit well with the implication of this enzyme in the efficient metabolism of short straight and branched chain fatty acyl-CoAs by the beta-oxidation cycle. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/16490786/The_peroxisomal_Acyl_CoA_thioesterase_Pte1p_from_Saccharomyces_cerevisiae_is_required_for_efficient_degradation_of_short_straight_chain_and_branched_chain_fatty_acids_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(19)46677-5 DB - PRIME DP - Unbound Medicine ER -