Information on EC 2.3.1.154 - propionyl-CoA C2-trimethyltridecanoyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.3.1.154
-
RECOMMENDED NAME
GeneOntology No.
propionyl-CoA C2-trimethyltridecanoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = CoA + 3-oxopristanoyl-CoA
show the reaction diagram
active on medium and long straight chain 3-oxoacyl-CoAs and 2-methyl-branched 3-oxoacyl-CoAs
-
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = CoA + 3-oxopristanoyl-CoA
show the reaction diagram
SCP-2 enhances the translocation of cholesterol from the ER to the plasmamembrane
-
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = CoA + 3-oxopristanoyl-CoA
show the reaction diagram
SCP-2 regulates multiple lipid signaling pathways in lipid raft/caveolae microdomains of the plasma membrane, SCP-2 selectively redistributes signaling lipids between lipid rafts/caveolae and intracellular sites, SCP-2 forms molecular complexes with sphingomyelin, dihexosylceramide, monohexosylceramide, ganglioside M1, phosphatidylinositol and cholesterol, SCP-2 exhibits high affinity for fatty acids, binds fatty acids, fatty acyl CoAs, lysophosphatidic acid, phosphatidylinositols, sphingomyelin, ceramide, glucosylceramide, galactosylceramide, lactosylceramide, globoside, ganglioside and cholesterol, SCP-x serves as a peroxisomal 3-ketoacyl-CoA thiolase in oxidation of branched-chain lipids
-
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = CoA + 3-oxopristanoyl-CoA
show the reaction diagram
acts as lipid binding protein, binds cholesterol and palmitic acid, transcription of AeSCP-2L1 and -2L2 genes are regulated differently through the mosquito life cycle
-
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = CoA + 3-oxopristanoyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
transfer of 3-oxoacyl-CoA
-
-
-
-
transfer of 3-oxoacyl-CoA
-
-
SYSTEMATIC NAME
IUBMB Comments
4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA C2-4,8,12-trimethyltridecanoyltransferase
The peroxisomal protein sterol carrier protein X (SCPx) combines this thiolase activity with its carrier function, and is involved in branched chain fatty acid beta-oxidation in peroxisomes. It also acts on 3-oxopalmitoyl-CoA as a substrate but differs from EC 2.3.1.16 (acetyl-CoA C-acyltransferase), which has little activity towards the 3-oxoacyl-CoA esters of 2-methyl-branched chain fatty acids such as 3-oxopristanoyl-CoA.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-oxopristanoyl-CoA hydrolase
-
-
-
-
3-oxopristanoyl-CoA thiolase
-
-
-
-
oxopristanoyl-CoA thiolase
-
-
-
-
peroxisomal 3-oxoacyl coenzyme A thiolase
-
-
-
-
peroxisome sterol carrier protein thiolase
-
-
-
-
SCP-2
-
AeSCP-2L1, AeSCP-2L2, 2 genes are identified
SCP-2
-
-
SCP-2/thiolase
-
-
SCP-x
-
-
SCP-x
-
-
SCP-x
Rattus norvegicus Sprague-Dawley
-
-
-
SCPx
-
-
-
-
sterol carrier protein 2/3-oxoacyl-CoA thiolase
-
-
sterol carrier protein x
-
-
-
-
sterol carrier protein-2
-
-
sterol carrier protein-2
-
-
sterol carrier protein-x
-
arises from an alternate transcription site
CAS REGISTRY NUMBER
COMMENTARY
195740-63-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
alternative splicing of gene results in two types of transcripts. SCPx is a protein of 536 amino acids which contains a thiolase domain and a SCP2 domain. SCP2 consists of 146 amino acids and contains only a SCP2 domain
-
-
Manually annotated by BRENDA team
translation products of the SCP-x/pro-SCP-2 gene have additional transcriptional and transcription-regulatory functions
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
P80547
SCP2 is involved in lipid traffic. Fatty acids are transferred by a collision-mediated mechanism, and negative charges on the membrane surface are important for establishing a collisional complex. Phospholipids induce special effects on the rates of transfer
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-oxo-(2R)-methylpalmitoyl-CoA + CoA
tetradecanoyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
3-oxo-(2R)-methylpalmitoyl-CoA + CoA
tetradecaneoyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
3-oxodecanoyl-CoA + CoA
octanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3-oxododecanoyl-CoA + CoA
decanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3-oxohexadecanoyl-CoA + CoA
tetradecanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3-oxohexanoyl-CoA + CoA
butanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3-oxooctanoyl-CoA + CoA
hexanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
3-oxooctanoyl-CoA + CoA
hexanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
3-oxooctanoyl-CoA + CoA
hexanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
3-oxooctanoyl-CoA + CoA
hexanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3-oxooctanoyl-CoA + CoA
hexanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
3-oxooctanoyl-CoA + CoA
hexanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
3-oxopalmitoyl-CoA + CoA
tetradecanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
3-oxopalmitoyl-CoA + CoA
tetradecanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
3-oxopalmitoyl-CoA + CoA
tetradecanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3-oxopentanoyl-CoA + CoA
propanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3-oxopristanoyl-CoA + CoA
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
3-oxopristanoyl-CoA + CoA
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
3-oxotetradecanoyl-CoA + CoA
didecanoyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
3alpha,7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoyl-CoA + CoA
choloyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
3alpha,7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoyl-CoA + CoA
choloyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
-
-
3alpha,7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoyl-CoA + CoA
choloyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
acetoacetyl-CoA + CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
-
-
acetoacetyl-CoA + CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-oxo-(2R)-methylpalmitoyl-CoA + CoA
tetradecaneoyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
3alpha,7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoyl-CoA + CoA
choloyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
3alpha,7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoyl-CoA + CoA
choloyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
-
-
3alpha,7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoyl-CoA + CoA
choloyl-CoA + propanoyl-CoA
show the reaction diagram
-
-
-
r
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
-
competitive to CoA, non-competitive to 3-oxoacyl-CoA
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
lauric acid induces SCPx mRNA levels in rat liver and in rat hepatoma H4IIE cells, enhanced protein levels of SCPx only in H4IIE cells
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.003
-
3-oxo-2-methylpalmitoyl-CoA
-
-
0.01
-
3-oxodecanoyl-CoA
-
-
0.0093
-
3-oxododecanoyl-CoA
-
-
0.0029
-
3-oxohexadecanedioyl-CoA
-
-
-
0.028
-
3-Oxohexanoyl-CoA
-
-
0.0046
-
3-Oxooctanoyl-CoA
-
-
0.0054
-
3-Oxooctanoyl-CoA
-
-
0.0083
-
3-Oxooctanoyl-CoA
-
-
0.0088
-
3-Oxooctanoyl-CoA
-
-
0.08
-
3-Oxooctanoyl-CoA
-
-
0.004
-
3-oxopalmitoyl-CoA
-
-
0.0079
-
3-oxopalmitoyl-CoA
-
-
0.059
-
3-oxopentanoyl-CoA
-
-
0.0028
-
3alpha,7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoyl-CoA
-
-
0.0081
-
acetoacetyl-CoA
-
-
0.093
-
acetoacetyl-CoA
-
-
0.0029
-
CoA
-
0.0025 mM 3-oxooctanoyl-CoA
0.0063
-
CoA
-
0.01 mM 3-oxooctanoyl-CoA
0.04
-
CoA
-
liver homogenate
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000214
-
-
skin fibroblasts culture of patients with Zellweger syndrome
0.00074
-
-
skin fibroblasts culture
0.04
-
-
whole peroxisomes, 3-oxopristanoyl-CoA as substrate
2.5
-
-
acetoacetyl-CoA as substrate
16
-
-
3-oxoacyl-CoA thiolase activity of mitochondrial long-chain trifunctional enzyme, 3-oxopalmitoyl-CoA as substrate
26.7
-
-
3-oxostearoyl-CoA as substrate
33.3
-
-
3-oxooleoyl-CoA as substrate
41
-
-
3-oxotetradecanoyl-CoA as substrate
61.5
-
-
3-oxooctanoyl-CoA as substrate
120
-
-
3-oxooctanoyl-CoA as substrate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
-
3-oxooctanoyl-CoA as substrate
9.5
-
-
liver homogenate
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
expression in all tissues and developmental stages analyzed, with the highest levels in floral tissues and in maturing seed
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
expression in all tissues and developmental stages analyzed, with the highest levels in floral tissues and in maturing seed
Manually annotated by BRENDA team
-
strong expression of both transcripts SCPx and SCP2 during last instar larvae
Manually annotated by BRENDA team
additional information
-
transcript SCP2 is found in all tissues analyzed
Manually annotated by BRENDA team
additional information
-
expression in all tissues and developmental stages analyzed, with the highest levels in floral tissues and in maturing seed. Expression is highly correlated with the multifunctional protein MFP2 involved in beta-oxidation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
SCP-2 50% peroxisomal, 50% cytoplasm, SCP-x exclusively peroxisomal
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
11670
-
-
AeSCP-2L2, SDS-PAGE, mass spectrometry
11900
-
-
AeSCP-2L1, SDS-PAGE, mass spectrometry
15400
-
-
SCP-2, short form
58000
-
-
SDS-PAGE, Western blot
58900
-
-
SCP-x, long form
86000
-
-
gel filtration
90000
110000
-
three isoforms, homo- and heterodimeric combinations of 58- and 46 kDa subunits, 58 kDa polypeptide is SCP2/thiolase, 46 kDa polypeptide is the thiolase domain of SCP2/thiolase, gel filtration, cross-linking, immunochemical
98000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
alpha,alpha, 2 * 46000, beta,beta, 2 * 58000, alpha,beta, 1 * 46000 + 1 * 58000, three isoforms, gel filtration, chemical cross-linking, immunochemical
dimer
-
alpha,alpha, 2 * 45000, SDS-PAGE
dimer
-
alpha,alpha, 2 * 43000, SDS-PAGE
dimer
-
SAXS and cross-linking experiments suggest that SCP2 dimerises at about 70 microM concentration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
sterol carrier protein SCP-x is processed on the peroxisomal surface to liberate a short C-terminal product of 12.9 kDa. This fragment has DNA-binding activity in vivo and in vitro
proteolytic modification
-
SPX is processed on the peroxisomal surface to liberate a short C-terminal product of 12.9 kDa. This fragment has DNA binding activity and is found in the nucleus, SCP-2 acts as competitive inhibitor of SCP-x processing
proteolytic modification
-
increase in post-translational processing of SCPx in response to lauric acid treatment in H4IIE cells
proteolytic modification
Rattus norvegicus Sprague-Dawley
-
increase in post-translational processing of SCPx in response to lauric acid treatment in H4IIE cells
-
additional information
-
both SCPx and SCP2 translation products have a putative peroxisomal targeting signal in the C-terminal region
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3D structure model built by homology
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20, 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
of the recombinant protein using GST affinity column chromatography
-
recombinant protein with His-tag, expressed in Escherichia coli, affinty chromatography with Ni2+
-
DEAE Sepharose, Cellulofine GCL, 17fold purification
-
coding sequence expressed in Escherichia coli
-
GST-SCPx fusion protein expressed in Escherichia coli, glutathione-Sepharose 4B, thrombin cleavage
-
phosphocellulose, ammonium sulfate, calcium phosphate gel/cellulose, Sephadex G-100, isoelectric focusing
-
phosphocellulose, DEAE-Sepharose, hydroxylapatite, Blue-Sepharose, chromatofocusing, yield: 0.7%
-
ammonium sulfate precipitation, phosphocellulose, matrix gel Red A, hydroxylapatite, 308fold purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli as GST tag fusion protein
-
full-length cDNA expressed in Escherichia coli, His-tagged
-
transfection into CHO cells and into human neuroglioma H4 cells
-
full-length cDNA expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Atscp2-1 plants deficient in AtSCP2 show altered seed morphology, a delayed germination, and are dependent on an exogenous carbon source to avoid a delayed seedling establishment
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
urea-induced unfolding is a three-step process. The first steps, between 1 and 2 M urea, have well-defined cooperative character and are related to the break down of most of the tertiary and secondary structure. The third step, at higher urea concentrations, is characterised by the disruption of residual interactions involving the single tryptophan
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
sterol carrier protein SCP-x is processed on the peroxisomal surface to liberate a short C-terminal product of 12.9 kDa. This fragment regulates the transcription of CD147, the regulatory subunit of the Alzheimer’s disease gamma-secretase
medicine
-
SCP-x fragment is a transcription factor that regulates CD147, the regulatory subunit of the Alzheimer disease gamma-secretase
medicine
-
induction of diabetes in rats causes an increase in hepatic SCPx protein levels, insulin directly affects lauric acid-dependent activation of the SCPx gene, administration of insulin to diabetic animals reduces SCPx protein levels
medicine
Rattus norvegicus Sprague-Dawley
-
induction of diabetes in rats causes an increase in hepatic SCPx protein levels, insulin directly affects lauric acid-dependent activation of the SCPx gene, administration of insulin to diabetic animals reduces SCPx protein levels
-