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Information on EC 2.3.1.176 - propanoyl-CoA C-acyltransferase and Organism(s) Mus musculus and UniProt Accession P32020

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IUBMB Comments
Also acts on dihydroxy-5beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase .
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This record set is specific for:
Mus musculus
UNIPROT: P32020
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
scp-2, nsltp, sterol carrier protein-2, non-specific lipid transfer protein, scp-x, sterol carrier protein x, sterol carrier protein-x, scp-2/thiolase, tgscp2, hascp-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sterol carrier protein-2
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sterol carrier protein-x
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3-oxopristanoyl-CoA hydrolase
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-
-
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3-oxopristanoyl-CoA thiolase
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-
-
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non-specific lipid transfer protein
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nsLTP
-
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oxopristanoyl-CoA thiolase
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-
-
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peroxisomal 3-oxoacyl coenzyme A thiolase
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-
-
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peroxisome sterol carrier protein thiolase
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-
-
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propanoyl-CoA C-acyltransferase
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SCP-2
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sterol carrier protein x
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-
-
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sterol carrier protein-2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
SYSTEMATIC NAME
IUBMB Comments
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA:propanoyl-CoA C-acyltransferase
Also acts on dihydroxy-5beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA
CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA
CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
testicular interstitial tissue
Manually annotated by BRENDA team
additional information
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highly expressed in tissues involved in cholesterol trafficking and oxidation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
role of SCPX and SCP2 in intracellular cholesterol transport. Sterol carrier protein-2 is a nonspecific lipid-transfer protein in intracellular cholesterol trafficking in testicular Leydig cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SCP2_MOUSE
547
0
59126
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
-
SCP-2
15000
-
SCP-2 precursor
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
wild-type mice fed a cholesterol-rich diet show increased weight gain, hepatic lipid, and bileacid accumulation. SCP-2 overexpression further exacerbates hepatic lipid accumulation in cholesterol-fed females and males. Primarily in female mice, hepatic cholesterol accumulation induced by SCP-2 overexpression is associated with increased levels of LDL receptor, HDL-receptor scavenger receptor SR-B1, liver fatty acid binding protein L-FABP, and 3alpha-hydroxysteroid dehydrogenase, without alteration of other proteins involved in cholesterol uptake, esterification, efflux, or oxidation/transport of bile salts. The effects of SCP-2 overexpression and cholesterol-rich diet are downregulation of proteins involved in cholesterol transport like L-FABP and SR-B1, cholesterolsynthesis related to sterol regulatory element binding protein 2 and HMG-CoA reductase, and bile acid oxidation/transport
pharmacology
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although SCP-2 was established as a protein that transfers cholesterol and phospholipids decades ago, recent findings with lipid rafts/caveolae and SCP-2 suggest that they may provide a conceptual link to metabolic processes that might be regulated through the respective signaling pathways
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schroeder, F.; Atshaves, B.P.; McIntosh, A.L.; Gallegos, A.M.; Storey, S.M.; Parr, R.D.; Jefferson, J.R.; Ball, J.M.; Kier, A.B.
Sterol carrier protein-2: new roles in regulating lipid rafts and signaling
Biochim. Biophys. Acta
1771
700-718
2007
Mus musculus
Manually annotated by BRENDA team
Atshaves, B.P.; McIntosh, A.L.; Martin, G.G.; Landrock, D.; Payne, H.R.; Bhuvanendran, S.; Landrock, K.K.; Lyuksyutova, O.I.; Johnson, J.D.; Macfarlane, R.D.; Kier, A.B.; Schroeder, F.
Overexpression of sterol carrier protein-2 differentially alters hepatic cholesterol accumulation in cholesterol-fed mice
J. Lipid Res.
50
1429-1447
2009
Mus musculus (P32020), Mus musculus
Manually annotated by BRENDA team
Li, N.C.; Fan, J.; Papadopoulos, V.
Sterol carrier protein-2, a nonspecific lipid-transfer protein, in intracellular cholesterol trafficking in testicular Leydig cells
PLoS ONE
11
e0149728
2016
Mus musculus (P32020), Mus musculus
Manually annotated by BRENDA team