Separation of stereoisomers of C27-bile acid CoA esters by liquid chromatography and its application to the study of the stereospecificities of D- and L-bifunctional proteins in bile acid biosynthesis

Kurosawa, Takao; Inoue, Kazuki; Yoshimura, Teizo; Tohma, Masahiko; Jiang, Ling; Hashimoto, Takashi

doi:10.1016/s0003-2670(97)00601-6

Cited by 13 publications

(8 citation statements)

References 16 publications

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“…This peak was not formed when reaction mixtures lacked ATP, CoA, or cholate, suggesting that the peak is choloyl-CoA (data not shown). The retention time of this peak was similar to that reported for authentic choloyl-CoA chromatographed under similar conditions (18). To verify that the reaction product was truly choloyl-CoA, we added a known quantity of authentic choloyl-CoA to hVLCS-H2-containing reaction mixtures prior to injection onto the HPLC column and observed a single peak on chromatograms (Fig.…”

Section: Resultssupporting

confidence: 73%

The Human Liver-specific Homolog of Very Long-chain Acyl-CoA Synthetase Is Cholate:CoA Ligase

Steinberg¹,

Mihalik²,

Kim³

et al. 2000

Journal of Biological Chemistry

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Unconjugated bile acids must be activated to their CoA thioesters before conjugation to taurine or glycine can occur. A human homolog of very long-chain acylCoA synthetase, hVLCS-H2, has two requisite properties of a bile acid:CoA ligase, liver specificity and an endoplasmic reticulum subcellular localization. We investigated the ability of this enzyme to activate the primary bile acid, cholic acid, to its CoA derivative. When expressed in COS-1 cells, hVLCS-H2 exhibited cholate:CoA ligase (choloyl-CoA synthetase) activity with both nonisotopic and radioactive assays. Other long-and very long-chain acyl-CoA synthetases were incapable of activating cholate. Endogenous choloyl-CoA synthetase activity was also detected in liver-derived HepG2 cells but not in kidney-derived COS-1 cells. Our results are consistent with a role for hVLCS-H2 in the re-activation and re-conjugation of bile acids entering liver from the enterohepatic circulation rather than in de novo bile acid synthesis.

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Section: Resultssupporting

confidence: 73%

The Human Liver-specific Homolog of Very Long-chain Acyl-CoA Synthetase Is Cholate:CoA Ligase

Steinberg¹,

Mihalik²,

Kim³

et al. 2000

Journal of Biological Chemistry

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“…Acetyl-CoA and butyryl-CoA were purchased from Sigma. Other acyl-CoAs were synthesized and purified from free acid and CoA hydrate trilithium salt according to the method of Kurosawa et al (10). The purity of acyl-CoAs, as evaluated by HPLC, was 88% for octanoyl-CoA, 89% for lauroyl-CoA, 93% for oleoyl-CoA, 91% for nonanoyl-CoA, 83% for decanoyl-CoA, and 90% for 8-methyl-nonanoyl-CoA.…”

Section: Methodsmentioning

confidence: 99%

The Peroxisomal Acyl-CoA Thioesterase Pte1p from Saccharomyces cerevisiae Is Required for Efficient Degradation of Short Straight Chain and Branched Chain Fatty Acids

Maeda

Delessert

Hasegawa

et al. 2006

Journal of Biological Chemistry

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The role of the Saccharomyces cerevisae peroxisomal acyl-coenzyme A (acyl-CoA) thioesterase (Pte1p) in fatty acid ␤-oxidation was studied by analyzing the in vitro kinetic activity of the purified protein as well as by measuring the carbon flux through the ␤-oxidation cycle in vivo using the synthesis of peroxisomal polyhydroxyalkanoate (PHA) from the polymerization of the 3-hydroxyacylCoAs 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 pte1⌬ 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 pte1⌬ strain compared with wild type. The poor catabolism of 8-methyl-nonanoic acid via ␤-oxidation in pte1⌬ 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 pte1⌬ 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 ␤-oxidation cycle.

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“…The solvent was evaporated and the residue was purifi ed using silica gel column chromatography silica gel 10 g ; hexane/ethyl acetate 10/1 v/v to obtain amorphous trans-2-hexadecenoic acid 170 mg, 668 mmol . The trans-2-hexadecenoic acid was further reacted to yield the corresponding CoA ester in accordance with a previously reported method 22 . Compounds 3 R -and 3 S -hydroxyhexadecanoyl -CoA were synthesized as described in our previous article 20 .…”

Section: Coa Estersmentioning

confidence: 99%

Analysis of Enoyl-Coenzyme A Hydratase Activity and Its Stereospecificity Using High-Performance Liquid Chromatography Equipped with Chiral Separation Column

et al. 2011

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Separation of stereoisomers of C27-bile acid CoA esters by liquid chromatography and its application to the study of the stereospecificities of D- and L-bifunctional proteins in bile acid biosynthesis

Cited by 13 publications

References 16 publications

The Human Liver-specific Homolog of Very Long-chain Acyl-CoA Synthetase Is Cholate:CoA Ligase

The Human Liver-specific Homolog of Very Long-chain Acyl-CoA Synthetase Is Cholate:CoA Ligase

The Peroxisomal Acyl-CoA Thioesterase Pte1p from Saccharomyces cerevisiae Is Required for Efficient Degradation of Short Straight Chain and Branched Chain Fatty Acids

Analysis of Enoyl-Coenzyme A Hydratase Activity and Its Stereospecificity Using High-Performance Liquid Chromatography Equipped with Chiral Separation Column

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