Information on EC 2.3.1.176 - propanoyl-CoA C-acyltransferase

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY
2.3.1.176
-
RECOMMENDED NAME
GeneOntology No.
propanoyl-CoA C-acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bile acid biosynthesis, neutral pathway
-
-
bile acid biosynthesis, neutral pathway
-
-
cholesterol degradation to androstenedione I (cholesterol oxidase)
-
-
cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
-
-
Metabolic pathways
-
-
Primary bile acid biosynthesis
-
-
sitosterol degradation to androstenedione
-
-
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 [4].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MsSCP-x/SCP-2 protein
D8VD26, D8VD27
-
non-specific lipid transfer protein
-
-
nsLTP
-
-
peroxisomal thiolase 2
-
-
peroxisomal thiolase 2
-
-
propanoyl-CoA C-acyltransferase
-
-
PTE-2
-
ambiguous
PTE-2
-
ambiguous
SCP-2
D8VD27
-
SCP-2
-
-
SCP-x
D8VD26
-
SCPc
-
-
sterol carrier protein-2
D8VD27
-
sterol carrier protein-2
-
-
sterol carrier protein-c
-
-
sterol carrier protein-c
-
-
sterol carrier protein-x
D8VD26
-
sterol carrier protein-x/sterol carrier protein-2
K7NSY9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sterol carrier protein-x/sterol carrier protein-2 gene, SCP-x/SCP-2
UniProt
Manually annotated by BRENDA team
sterol carrier protein 2, SCP-2; sterol carrier protein-2, SCP-2, gene
UniProt
Manually annotated by BRENDA team
sterol carrier protein 2/3-oxoacyl-CoA thiolase, SCP-x; sterol carrier protein-x/the sterol carrier protein-2, MsSCP-x/SCP-2, gene
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
K7NSY9
HaSCP-x/SCP-2 is a member of the SCP-2 gene family
physiological function
D1GJ60
overexpression enhances cholesterol uptakeinto Spli-221 cells
physiological function
K7NSY9
HaSCPx/2 gene is important for normal development and fertility in Helicoverpa armigera
physiological function
D8VD26, D8VD27
MsSCP-2 may function as a lipid carrier protein in vivo, MsSCP-2 is involved in cholesterol uptake in vivo, overview
evolution
-
the MsSCP-x/SCP-2 protein has a high degree of homology in the SCP-2 domain to other insect SCP-2
additional information
K7NSY9
effects of dsRNA interference of HaSCP-x/SCP-2 transcripts on larval development and fecundity in adults, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
additional information
?
-
-
SCP-2, significantly enhances disruption of the dihydroergosterol microcrystalline structure when in the presence of excess cholesterol. In experiments with model membranes containing 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, cholesterol, and 1,2-dioleoylsn-glycero-3-[phospho-L-serine], SCP-2 enhances exchange of sterol between microcrystals and large unilamellar vesicles nearly 92fold more in the initial rate than the spontaneous exchange
-
-
-
additional information
?
-
D8VD26, D8VD27
recombinant MsSCP-2 binds to NBD-cholesterol with high affinity, which is suppressed by sterol carrier protein-2 inhibitors
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-mangostin
K7NSY9
SCPI-1 or mangostin-treatment cause most death on day-3 and day-4 after the treatment started when larvae in control groups were all alive and molting from 1st to 2nd instars
N-(4-{[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]amino}phenyl)acetamide
K7NSY9
i.e. SCPI-1, SCPI-1 or mangostin-treatment cause most death on day-3 and day-4 after the treatment started when larvae in control groups were all alive and molting from 1st to 2nd instars
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
highly expressed in tissues involved in cholesterol trafficking and oxidation
Manually annotated by BRENDA team
additional information
-
MsSCP-x and MsSCP-2, semi-quantitative RT-PCR expression analysis, overview
Manually annotated by BRENDA team
additional information
K7NSY9
tissue and stage expression profiles of HaSCP-2 in larvae of different stages, overview. The highest level of HaSCP-2 expression is in the midgut, whereas the epidermis and the hindgut express the lowest levels
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13000
-
SCP-2
685342
15000
-
SCP-2 precursor
685342
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
D1GJ60
x * 16000, SDS-PAGE
?
-
x * 15401, proSCP-2, x * 13246, SCP-2, mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
SCP-2 is encoded as a precursor protein with a 20-amino acid N-terminal presequence. The presequence alters SCP-2 secondary structure, tertiary structure, ligand binding site, selectivity for interaction with anionic phospholipid-rich membranes, interaction with a peroxisomal import protein, and intracellular targeting in living and fixed cells
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene SCP-x/SCP-2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, detailed overview
K7NSY9
gene MsSCP-x/SCP-2, from larval fat body and midgut, cDNA and amino acid sequence determination and analysis, sequence comparison; gene SCP-2, from larval fat body and midgut, cDNA and amino acid sequence determination and analysis, sequence comparison
D8VD26, D8VD27
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
P32020
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
D8VD26, D8VD27
targeting insect SCP-2 may be a viable approach for the development of insecticides
nutrition
P32020
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
-
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