Enzymes
UniProtKB help_outline | 4 proteins |
Reaction participants Show >> << Hide
- Name help_outline (25S)-3α,7α,12α-trihydroxy-5β-cholestan-26-oyl-CoA Identifier CHEBI:77251 Charge -4 Formula C48H76N7O20P3S InChIKeyhelp_outline MNYDLIUNNOCPHG-SEGQUPMDSA-J SMILEShelp_outline C[C@H](CCC[C@H](C)C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@H]1CC[C@H]2[C@@H]3[C@H](O)C[C@@H]4C[C@H](O)CC[C@]4(C)[C@H]3C[C@H](O)[C@]12C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (24E)-3α,7α,12α-trihydroxy-5β-cholest-24-en-26-oyl-CoA Identifier CHEBI:59879 Charge -4 Formula C48H74N7O20P3S InChIKeyhelp_outline QVDPWQVOSKJUES-JMOYVIBVSA-J SMILEShelp_outline [H][C@@](C)(CC\C=C(/C)C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@]1([H])CC[C@@]2([H])[C@]3([H])[C@H](O)C[C@]4([H])C[C@H](O)CC[C@]4(C)[C@@]3([H])C[C@H](O)[C@]12C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O2 Identifier CHEBI:16240 (Beilstein: 3587191; CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 426 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:46728 | RHEA:46729 | RHEA:46730 | RHEA:46731 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Publications
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Substrate stereospecificity in oxidation of (25S)-3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestanoyl-CoA by peroxisomal trihydroxy-5 beta-cholestanoyl-CoA oxidase.
Pedersen J.I., Veggan T., Bjorkhem I.
Partly purified 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestanoyl-CoA oxidase from rabbit liver peroxisomes was found to convert the 25S-but not the 25R diastereoisomer of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestan-27-oyl-CoA into (24E)-3 alpha, 7 alpha, 12 alpha-trihydroxy-5 b ... >> More
Partly purified 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestanoyl-CoA oxidase from rabbit liver peroxisomes was found to convert the 25S-but not the 25R diastereoisomer of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestan-27-oyl-CoA into (24E)-3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholest-24-en-27-oic acid. In the presence of a peroxisomal THCA-CoA racemase, however, also the 25R isomer was oxidized. Since the mitochondrial steroid-27-hydroxylase, responsible for formation of THCA, is 25R specific a racemase seems to be obligatory for formation of cholic acid by the normal peroxisomal-dependent pathway. << Less
Biochem Biophys Res Commun 224:37-42(1996) [PubMed] [EuropePMC]
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Molecular cloning and expression of cDNA encoding 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase from rabbit liver.
Pedersen J.J., Eggertsen G., Hellman U., Andersson U., Bjoerkhem I.
The steroid side chain cleavage in bile acid formation is catalyzed by liver peroxisomal enzymes (Pedersen, J. I. and Gustafsson, J. (1980) FEBS Lett. 121, 345-348; Kase, F., Björkhem, I., and Pedersen, J. I. (1983) J. Lipid Res. 24, 1560-1567). We here describe the cloning and sequencing of a cDN ... >> More
The steroid side chain cleavage in bile acid formation is catalyzed by liver peroxisomal enzymes (Pedersen, J. I. and Gustafsson, J. (1980) FEBS Lett. 121, 345-348; Kase, F., Björkhem, I., and Pedersen, J. I. (1983) J. Lipid Res. 24, 1560-1567). We here describe the cloning and sequencing of a cDNA coding the first of these enzymes, a 3alpha,7alpha,12alpha-trihydroxy-5beta-choles tanoyl-CoA oxidase (THCA-CoA oxidase) from rabbit liver peroxisomes. After tryptic digestion of purified protein in a polyacrylamide gel, five peptides were isolated and sequenced. Using two oligonucleotides deduced from the amino acid sequence data, two overlappping clones were isolated from a rabbit liver cDNA library, which together made up a unique cDNA sequence of 2139 base pairs. It contained an open reading frame of 2046 base pairs encoding a protein of 681 amino acids with a molecular mass of 76,209 daltons. All five peptides could be localized within the sequence. Transfection of COS cells with the coding part of the cDNA resulted in a significant expression of THCA-CoA oxidase activity. We were not able to demonstrate 3alpha, 7alpha-dihydroxy-5beta-cholestanoyl-CoA oxidase activity under the same conditions. The obtained sequence showed 73.6% similarity with a proposed rat THCA-CoA oxidase and 81% similarity with a recently reported human branched chain acyl-CoA oxidase, indicating that these three proteins represent the same enzyme. The similarity with rat palmitoyl-CoA oxidase was 41.8%. The C-terminal tripeptide of the protein was SNL, a previously undescribed variant of the main class of peroxisomal targeting signals. Northern blot analysis revealed that the gene is transcribed in liver and kidney, and the major mRNA fraction had a size of approximately 2.6 kilobase pairs. << Less
J. Biol. Chem. 272:18481-18489(1997) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.