Information on EC 2.3.1.176 - propanoyl-CoA C-acyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.176
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RECOMMENDED NAME
GeneOntology No.
propanoyl-CoA C-acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bile acid biosynthesis, neutral pathway
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cholesterol degradation to androstenedione I (cholesterol oxidase)
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cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
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sitosterol degradation to androstenedione
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bile acid biosynthesis, neutral pathway
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Primary bile acid biosynthesis
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Metabolic pathways
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
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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-
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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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-
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-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-mangostin
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
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
SCPI-1
i.e. N-(4-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]amino]phenyl)acetamide hydrobromide
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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mRNA is strongly expressed in differentiated epithelial structures of the pronephric kidney
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
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SCP-2
15000
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SCP-2 precursor
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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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
NMR spectroscopy and docking simulations reveal that the folds of alpha-helices and beta-sheets interact together to form a hydrophobic cavity with putative entrance and exit openings, which serves as a tunnel for accommodation and transport of lipids
C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2, to 2.1 A resolution. Space group P3121 (or P3221), with unit-cell parameters a = b = 70.4, c = 60.6 A,  alpha = beta = 90°, gamma = 120°
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
gene SCP-x/SCP-2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, detailed overview
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F110W
reduced ability to bind with cholesterol
F53A
reduced ability to bind with cholesterol
F53W
strongly reduced ability to bind with cholesterol
F89A
reduced ability to bind with cholesterol
I117M
reduced ability to bind with cholesterol
Q131A
reduced ability to bind with cholesterol
Y51A
reduced ability to bind with cholesterol
Y51W
reduced ability to bind with cholesterol
additional information
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 hide
LITERATURE
drug development
targeting insect SCP-2 may be a viable approach for the development of insecticides
medicine
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
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