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Information on EC 2.3.1.16 - acetyl-CoA C-acyltransferase and Organism(s) Mus musculus and UniProt Accession Q921H8

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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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This record set is specific for:
Mus musculus
UNIPROT: Q921H8
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Word Map
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The taxonomic range for the selected organisms is: Mus musculus
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 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
-
-
-
-
ELOVL5
-
-
fatty acid elongase 5
-
-
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 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-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
-
-
-
?
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6,6-dimethyl-3-[5-methyl-3-oxo-1-[4-(trifluoromethoxy)phenyl]-2,3-dihydro-1H-pyrazol-4-yl]-1-phenyl-3-(trifluoromethyl)-3,5,6,7-tetrahydro-1H-indole-2,4-dione
-
inhibitor shows sustained plasma exposure and good liver penetrability. After oral administration, it potently inhibits ELOVL6 activity in liver
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3-ketoacyl-CoA thiolase A
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
very low expression
Manually annotated by BRENDA team
thiolasae A is mainly expressed in liver and intestine
Manually annotated by BRENDA team
thiolasae A is mainly expressed in liver and intestine
Manually annotated by BRENDA team
very low expression
Manually annotated by BRENDA team
very low expression of thiolase B
Manually annotated by BRENDA team
weak expression of thiolase B
Manually annotated by BRENDA team
weak expression of thiolase B
Manually annotated by BRENDA team
very low expression of thiolase B
Manually annotated by BRENDA team
weak expression of thiolase B
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
ACAA2 resides in the nucleus in significant concentrations and harbors an nuclear localization signal that mediates nuclear import
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THIKA_MOUSE
424
0
43953
Swiss-Prot
Mitochondrion (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
3-ketoacyl-CoA thiolase A and B
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
liver X Receptor LXRalpha and sterol regulatory binding protein SREBP-1c regulate hepatic Elovl5 expression. The up-regulation of Elovl5 expression by LXR agonist is likely secondary to the induction of SREBP-1c. C18-20 polyunsaturated fatty acids repress expression of SREBP-1c and Elovl5, but when combined with LXR ligand stimulation, which increases SREBP-1c mRNA and nuclear SREBP-1c, Elovl5 mRNA levels are restored to normal
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chevillard, G.; Clemencet, M.C.; Etienne, P.; Martin, P.; Pineau, T.; Latruffe, N.; Nicolas-Frances, V.
Molecular cloning, gene structure and expression profile of two mouse peroxisomal 3-ketoacyl-CoA thiolase genes
BMC Biochem.
5
3
2004
Mus musculus (Q8VCH0), Mus musculus (Q921H8), Mus musculus
Manually annotated by BRENDA team
Qin, Y.; Dalen, K.T.; Gustafsson, J.A.; Nebb, H.I.
Regulation of hepatic fatty acid elongase 5 by LXRalpha-SREBP-1c
Biochim. Biophys. Acta
1791
140-147
2009
Mus musculus
Manually annotated by BRENDA team
Takahashi, T.; Nagase, T.; Sasaki, T.; Nagumo, A.; Shimamura, K.; Miyamoto, Y.; Kitazawa, H.; Kanesaka, M.; Yoshimoto, R.; Aragane, K.; Tokita, S.; Sato, N.
Synthesis and evaluation of a novel indoledione class of long chain fatty acid elongase 6 (ELOVL6) inhibitors
J. Med. Chem.
52
3142-3145
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fidaleo, M.; Arnauld, S.; Clemencet, M.C.; Chevillard, G.; Royer, M.C.; De Bruycker, M.; Wanders, R.J.; Athias, A.; Gresti, J.; Clouet, P.; Degrace, P.; Kersten, S.; Espeel, M.; Latruffe, N.; Nicolas-Frances, V.; Mandard, S.
A role for the peroxisomal 3-ketoacyl-CoA thiolase B enzyme in the control of PPAR?-mediated upregulation of SREBP-2 target genes in the liver
Biochimie
93
876-891
2011
Mus musculus
Manually annotated by BRENDA team
Choi, S.; Pfleger, J.; Jeon, Y.; Yang, Z.; He, M.; Shin, H.; Sayed, D.; Astrof, S.; Abdellatif, M.
Oxoglutarate dehydrogenase and acetyl-CoA acyltransferase 2 selectively associate with H2A.Z-occupied promoters and are required for histone modifications
Biochim. Biophys. Acta
1862
194436
2019
Homo sapiens (P42765), Homo sapiens, Mus musculus (Q8BWT1), Mus musculus
Manually annotated by BRENDA team