• Corpus ID: 39113496

New Aspects of Sterol Carrier Protein 2 ( Non-specific Lipid-transfer Protein ) in Fusion Proteins and in Peroxisomes ( Running title : New Aspects of SCP 2 )

@inproceedings{Masanori2008NewAO,
  title={New Aspects of Sterol Carrier Protein 2 ( Non-specific Lipid-transfer Protein ) in Fusion Proteins and in Peroxisomes ( Running title : New Aspects of SCP 2 )},
  author={Masanori and Bun-ya and Yoshitaka and Mum and Toshiro and Niki and Jun Kondo and Tatsuyuki and Kamiryo},
  year={2008}
}
Sterol carrier protein 2 (SCP2) is a 14-kDa peroxisomal protein, identical to nonspecific lipid-transfer protein, and stimulates various steps of cholesterol metabolism in vitro. Although the name is reminiscent of acyl carrier protein involved in fatty acid synthesis, SCP2 does not bind to lipids specifically or stoichiometrically. This protein is expressed either as a small precursor or as a large fusion (termed SCPx) that carries at its C-terminal the complete sequence of SCP2. SCPx exhibits… 

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TLDR
These findings suggest that SCPx is a previously undescribed peroxisomal 3-ketoacyl-CoA thiolase (EC 2.3.1.16) with intrinsic sterol carrier and lipid transfer activity (suggested name: SCP2/3-oxoACYl- CoA thiolaase).
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TLDR
The data show, that SCPx, a 58 kDa protein with both thiolase and sterol carrier protein activity but unknown function so far, readily reacts with 3-oxopristanoyl-CoA, and plays a central role in branched chain fatty acid beta-oxidation in peroxisomes.
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TLDR
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TLDR
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TLDR
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