Enzymes
UniProtKB help_outline | 1,484 proteins |
Reaction participants Show >> << Hide
- Name help_outline 7-dehydrocholesterol Identifier CHEBI:17759 (Beilstein: 2224615; CAS: 434-16-2) help_outline Charge 0 Formula C27H44O InChIKeyhelp_outline UCTLRSWJYQTBFZ-DDPQNLDTSA-N SMILEShelp_outline [H][C@@]1(CC[C@@]2([H])C3=CC=C4C[C@@H](O)CC[C@]4(C)[C@@]3([H])CC[C@]12C)[C@H](C)CCCC(C)C 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:62960 | RHEA:62961 | RHEA:62962 | RHEA:62963 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity.
Seedorf U., Brysch P., Engel T., Schrage K., Assmann G.
Sterol carrier protein 2 (SCP2; also called nonspecific lipid transfer protein) is a small basic sterol carrier and lipid transfer protein assumed to participate in the intracellular transport of sterols and certain other lipids. Upon cloning and sequencing SCP2-encoding cDNAs, we and others found ... >> More
Sterol carrier protein 2 (SCP2; also called nonspecific lipid transfer protein) is a small basic sterol carrier and lipid transfer protein assumed to participate in the intracellular transport of sterols and certain other lipids. Upon cloning and sequencing SCP2-encoding cDNAs, we and others found cDNAs containing unexpected in-frame 5'-extensions of up to 1,250 nucleotides upstream of the initiator ATG of the cDNA encoding pre-SCP2. The corresponding transcripts are primarily expressed in the liver and are predicted to encode a previously undescribed fusion protein containing a 143-amino acid C-terminal domain completely identical to pre-SCP2 and a 404-amino acid N-terminal domain with unknown biochemical activity or function (named sterol carrier protein x, SCPx). Here, we show that purified recombinant SCPx cleaves 3-oxoacyl(n)-CoA to yield acetyl-CoA and acyl(n-2)-CoA. Like SCP2, recombinant SCPx also stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol from small unilamellar vesicles to acceptor membranes in vitro. Furthermore, SCPx epitopes are primarily detected within peroxisomes. 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 thiolase). << Less
J. Biol. Chem. 269:21277-21283(1994) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.