Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism (Q22009362)

Gene Ontology release 2020-05-02

Gene Ontology ID

GO:0070251

Solute carrier family 27 member 2

1 reference

methyl-branched fatty acid metabolic process

GOA release 2020-03-11

1 reference

Solute carrier family 27 (fatty acid transporter), member 2

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

S J Steinberg

1

S J

Steinberg

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7 February 2023

S J Wang

2

S J

Wang

1 reference

7 February 2023

D G Kim

3

D G

Kim

1 reference

7 February 2023

S J Mihalik

4

S J

Mihalik

1 reference

7 February 2023

P A Watkins

5

P A

Biochemical and Biophysical Research Communications

Watkins

1 reference

7 February 2023

language of work or name

English

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publication date

13 April 1999

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published in

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volume

257

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issue

2

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page(s)

615-21

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cites work

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Distinct long chain and very long chain fatty acyl CoA synthetases in rat liver peroxisomes and microsomes

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Peroxisomal fatty acid beta-oxidation in HepG2 cells

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Characteristics and subcellular localization of pristanoyl-CoA synthetase in rat liver

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Phytanic acid must be activated to phytanoyl-CoA prior to its alpha-oxidation in rat liver peroxisomes

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Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein

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cDNA cloning and mRNA distribution of a mouse very long-chain acyl-CoA synthetase

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Involvement of microsomal fatty aldehyde dehydrogenase in the alpha-oxidation of phytanic acid.

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Fatty acid activation

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Topographical localization of peroxisomal acyl-CoA ligases: differential localization of palmitoyl-CoA and lignoceroyl-CoA ligases

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The metabolism of phytanic acid and pristanic acid in man: a review

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Evidence that peroxisomal acyl-CoA synthetase is located at the cytoplasmic side of the peroxisomal membrane

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Topography of very-long-chain-fatty-acid-activating activity in peroxisomes from rat liver

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Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase

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Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids

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Disruption of the Saccharomyces cerevisiae FAT1 gene decreases very long-chain fatty acyl-CoA synthetase activity and elevates intracellular very long-chain fatty acid concentrations

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