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Information on EC 2.3.1.16 - acetyl-CoA C-acyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P27796

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EC Tree
IUBMB Comments
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
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Saccharomyces cerevisiae
UNIPROT: P27796
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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acyl-CoA
+
acetyl-CoA
=
CoA
+
3-oxoacyl-CoA
+
=
+
Synonyms
elovl6, elovl5, 3-ketoacyl-coa thiolase, beta-ketothiolase, 3-oxoacyl-coa thiolase, acaa2, 3-ketothiolase, elovl-6, thiolase i, thiolase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-ketoacyl CoA thiolase
-
-
-
-
3-ketoacyl coenzyme A thiolase
-
-
-
-
3-ketoacyl thiolase
-
-
-
-
3-ketoacyl-CoA thiolase
-
-
-
-
3-ketothiolase
-
-
-
-
3-oxoacyl-CoA thiolase
-
-
-
-
3-oxoacyl-coenzyme A thiolase
-
-
-
-
6-oxoacyl-CoA thiolase
-
-
-
-
acetoacetyl-CoA beta-ketothiolase
-
-
-
-
acetyl-CoA acyltransferase
-
-
-
-
acyltransferase, acetyl coenzyme A
-
-
-
-
beta-ketoacyl coenzyme A thiolase
-
-
-
-
beta-ketoacyl-CoA thiolase
-
-
-
-
beta-ketoadipyl coenzyme A thiolase
-
-
-
-
beta-ketoadipyl-CoA thiolase
-
-
-
-
beta-ketothiolase
-
-
-
-
KAT
-
-
-
-
ketoacyl-CoA acyltransferase
-
-
-
-
ketoacyl-coenzyme A thiolase
-
-
-
-
long-chain 3-oxoacyl-CoA thiolase
-
-
-
-
oxoacyl-coenzyme A thiolase
-
-
-
-
pro-3-ketoacyl-CoA thiolase
-
-
-
-
SCP2/3-oxoacyl-CoA thiolase
-
-
-
-
thiloase B
-
-
-
-
thiolase A
-
-
-
-
thiolase I
-
-
-
-
thiolase II
-
-
-
-
thiolase III
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
reaction mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetyl-CoA C-acyltransferase
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-97-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
additional information
?
-
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
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
enzyme catalyses the last step in the beta-oxidation cycle
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
anti-thiolase-antibody
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-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is synthesized in the cytosol and subsequently imported into the peroxisome
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
2 * 45000, SDS-PAGE
86000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
the high sequence similarity between the tetrameric and dimeric thiolases suggests that the tetrameric thiolases are assemble as a dimer of two thiolase dimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, stable
-
frequent freeze and thaw results in a gradual loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
mutation in the thiolase gene causes severe health problems, such as ketoacidic attacks at the age of six months followed by severe retardation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Middleton, B.
3-Oxoacyl-coenzyme A thiolases and L-3-hydroxyacyl-coenzyme A dehydrogenases
Biochem. Soc. Trans.
6
80-83
1978
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Erdmann, R.; Kunau, W.H.
Purification and immunolocalization of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae
Yeast
10
1173-1182
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zeelen, J.P.; Wierenga, R.K.; Erdmann, R.; Kunau, W.H.
Crystallographic studies of 3-ketoacylCoA thiolase from yeast Saccharomyces cerevisiae
J. Mol. Biol.
215
211-213
1990
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mathieu, M.; Zeelen, J.P.; Pauptit, R.A.; Erdmann, R.; Kunau, W.H.; Wierenga, R.K.
The 2.8 ANG. crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha,beta,alpha,beta,alpha structure constructed from two core domains of identical topology
Structure
2
797-808
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mathieu, M.; Modis, Y.; Zeelen, J.P.; Engel, C.K.; Abagyan, R.A.; Ahlberg, A.; Rasmussen, B.; Lamzin, V.S.; Kunau, W.H.; Wierenga, R.K.
The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism
J. Mol. Biol.
273
714-728
1997
Saccharomyces cerevisiae (P27796)
Manually annotated by BRENDA team