Enzyme

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     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.176
Description:Propanoyl-CoA C-acyltransferase.
Alternative Name: Sterol carrier protein-X.
Sterol carrier protein-chi.
SCP-X.
SCP(chi).
PTE-2.
Propionyl-CoA C(2)-trimethyltridecanoyltransferase.
Peroxisomal thiolase 2.
3-oxopristanoyl-CoA thiolase.
3-oxopristanoyl-CoA hydrolase.
Prosite: PDOC00092;
PDB:
PDBScop
Cath: 3.30.1050.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.176
BRENDA Enzyme Link: BRENDA 2.3.1.176
KEGG Enzyme Link: KEGG2.3.1.176
BioCyc Enzyme Link: BioCyc 2.3.1.176
ExPASy Enzyme Link: ExPASy2.3.1.176
EC2PDB Enzyme Link: EC2PDB 2.3.1.176
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.176
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.176
IntEnz Enzyme Link: IntEnz 2.3.1.176
MEDLINE Enzyme Link: MEDLINE 2.3.1.176
MSA:

2.3.1.176;

Phylogenetic Tree:

2.3.1.176;

Uniprot:
M-CSA:
RHEA:16865 choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[*:6])-[S;H0;+0:7]-[*:8]>>[*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:5](=[*:4])-[*:6].[*:8]-[SH;+0:7]
Reaction
Core-to-Core More
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase purified from normal rat liver peroxisomes. Sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates.Antonenkov VD, Van Veldhoven PP, Waelkens E, Mannaerts GP1997 Oct 109325339
A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein x but lacks the sequence of sterol carrier protein 2.Bun-Ya M, Maebuchi M, Hashimoto T, Yokota S, Kamiryo T1997 Apr 159151950
Conversion of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestanoic acid into cholic acid by rat liver peroxisomes.Pedersen JI, Gustafsson J1980 Dec 17461136
Formation of cholic acid from 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestanoic acid by rat liver peroxisomes.Kase F, Björkhem I, Pedersen JI1983 Dec6668450
Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method.Ferdinandusse S, Denis S, van Berkel E, Dacremont G, Wanders RJ2000 Mar10706581
Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase.Falany CN, Johnson MR, Barnes S, Diasio RB1994 Jul 298034703
The enzymes, regulation, and genetics of bile acid synthesis.Russell DW200312543708

RHEA:10408 4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-oxopristanoyl-CoA + CoA
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[*:6])-[S;H0;+0:7]-[*:8]>>[*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:5](=[*:4])-[*:6].[*:8]-[SH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Sterol carrier protein X (SCPx) is a peroxisomal branched-chain beta-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes.Wanders RJ, Denis S, Wouters F, Wirtz KW, Seedorf U1997 Jul 309245689