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Information on EC 2.3.1.176 - propanoyl-CoA C-acyltransferase and Organism(s) Homo sapiens and UniProt Accession P22307

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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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Homo sapiens
UNIPROT: P22307
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The taxonomic range for the selected organisms is: Homo sapiens
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 type 2
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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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oxopristanoyl-CoA thiolase
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-
-
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peroxisomal 3-oxoacyl coenzyme A thiolase
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peroxisomal thiolase 2
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peroxisome sterol carrier protein thiolase
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-
-
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PTE-2
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ambiguous
SCPc
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sterol carrier protein x
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-
-
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sterol carrier protein-c
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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
additional information
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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
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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SCP2 is a binding protein for endocannbinoids N-arachidonylethanolamine and 2-arachidonoylglycerol. N-arachidonylethanolamine and 2-arachidonoylglycerol associate with SCP2 at a putative cholesterol binding pocket with DeltaG values of -3.6 and -4.6 kcal per mol, respectively. SCP2-mediated transfer of cholesterol in vitro is inhibited by micromolar concentrations of N-arachidonylethanolamine, and heterologous expression of SCP2 in HEK-293 cells increases time-related accumulation of N-arachidonylethanolamine in a temperature-dependent fashion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SCP2_HUMAN
547
0
58994
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13246
x * 15401, proSCP-2, x * 13246, SCP-2, mass spectrometry
15401
x * 15401, proSCP-2, x * 13246, SCP-2, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 15401, proSCP-2, x * 13246, SCP-2, mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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°
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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SCP2 is a binding protein for endocannbinoids N-arachidonylethanolamine and 2-arachidonoylglycerol. N-arachidonylethanolamine and 2-arachidonoylglycerol associate with SCP2 at a putative cholesterol binding pocket with DeltaG values of ?3.6 and ?4.6 kcal per mol, respectively. SCP2-mediated transfer of cholesterol in vitro is inhibited by micromolar concentrations of N-arachidonylethanolamine, and heterologous expression of SCP2 in HEK-293 cells increases time-related accumulation of N-arachidonylethanolamine in a temperature-dependent fashion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Falany, C.N.; Johnson, M.R.; Barnes, S.; Diasio, R.B.
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
J. Biol. Chem.
269
19375-19379
1994
Homo sapiens
Manually annotated by BRENDA team
Martin, G.G.; Hostetler, H.A.; McIntosh, A.L.; Tichy, S.E.; Williams, B.J.; Russell, D.H.; Berg, J.M.; Spencer, T.A.; Ball, J.; Kier, A.B.; Schroeder, F.
Structure and function of the sterol carrier protein-2 N-terminal presequence
Biochemistry
47
5915-5934
2008
Homo sapiens (P22307)
Manually annotated by BRENDA team
McIntosh, A.L.; Atshaves, B.P.; Gallegos, A.M.; Storey, S.M.; Reibenspies, J.H.; Kier, A.B.; Meyer, E.; Schroeder, F.
Structure of dehydroergosterol monohydrate and interaction with sterol carrier protein-2
Lipids
43
1165-1184
2008
Homo sapiens (P22307)
Manually annotated by BRENDA team
Cheng, Z.; Li, Y.; Sui, C.; Sun, X.; Xie, Y.
Synthesis, purification and crystallographic studies of the C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2
Acta Crystallogr. Sect. F
71
901-905
2015
Homo sapiens (P22307), Homo sapiens
Manually annotated by BRENDA team
Liedhegner, E.S.; Vogt, C.D.; Sem, D.S.; Cunningham, C.W.; Hillard, C.J.
Sterol carrier protein-2: binding protein for endocannabinoids
Mol. Neurobiol.
50
149-158
2014
Homo sapiens
Manually annotated by BRENDA team