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Information on EC 2.3.1.16 - acetyl-CoA C-acyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q56WD9
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2.3.1.16 acetyl-CoA C-acyltransferaseIUBMB 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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Word Map
- 2.3.1.16
- peroxisomal
-
beta-oxidation
-
polyunsaturated
-
pufas
-
hydratase
- enoyl-coa
- 3-hydroxyacyl-coa
-
elovls
-
docosahexaenoic
- polyhydroxyalkanoate
-
monounsaturated
-
lc-pufas
- carnitine
-
desaturases
-
lipogenesis
-
trifunctional
-
desaturation
-
lipogenic
-
eicosapentaenoic
- eutropha
-
ralstonia
- stearoyl-coa
-
thiolytic
- acylcarnitine
- zellweger
- trimetazidine
-
hadhb
-
siganus
- punctata
-
chondrodysplasia
-
poly3-hydroxybutyrate
- srebp-1
-
rhizomelic
- glyoxysomal
-
phytanic
-
acetoacetyl-coenzyme
- 3-hydroxybutyrate
- adrenoleukodystrophy
- plasmalogens
-
antianginal
-
very-long-chain
- poly-beta-hydroxybutyrate
-
linseed
-
ketoacidotic
-
palmitoleic
- acaca
- medicine
- agriculture
- synthesis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
elovl6, elovl5, 3-ketoacyl-coa thiolase, beta-ketothiolase, 3-oxoacyl-coa thiolase, acaa2, 3-ketothiolase, elovl-6, thiolase i, thiolase a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
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pro-3-ketoacyl-CoA thiolase
-
-
-
-
SCP2/3-oxoacyl-CoA thiolase
-
-
-
-
thiloase B
-
-
-
-
thiolase A
-
-
-
-
thiolase I
-
-
-
-
thiolase II
-
-
-
-
thiolase III
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
the active site involves residues Cys138, in loop beta4alpha3 on domain I, His393 on the segment linking alpha10 and alpha11 of domain III, and Cys425 at the C-terminal end of beta12, detailed reaction mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
alpha-Linolenic acid metabolism, Benzoate degradation, Biosynthesis of secondary metabolites, Biosynthesis of unsaturated fatty acids, Ethylbenzene degradation, Fatty acid degradation, Fatty acid elongation, Geraniol degradation, Microbial metabolism in diverse environments, Valine, leucine and isoleucine degradation
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9029-97-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
metabolism in the peroxisome influences metabolism in the lipid body
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
enzyme catalyses step of fatty acid beta-oxidation
-
-
?
additional information
?
-
the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview
-
-
?
additional information
?
-
-
the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
metabolism in the peroxisome influences metabolism in the lipid body
-
-
?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
enzyme catalyses step of fatty acid beta-oxidation
-
-
?
additional information
?
-
the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview
-
-
?
additional information
?
-
-
the peroxisomal isozyme is a biodegradative type 1 thiolase showing potential for redox control of peroxisomal fatty acid beta-oxidation, KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
in presence of 20 mM cysteamine, full activity is maintained for more than 12 h
-
additional information
-
in presence of 20 mM cysteamine, full activity is maintained for more than 12 h
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoform KAT2 positively regulates abscisic acid signaling in all the major abscisic acid responses, including abscisic acid-induced inhibition of seed germination and post-germination growth arrest, and abscisic acid-induced stomatal closure and stomatal opening inhibition in Arabidopsis thaliana. KAT2 is shown to be important for reactive oxygen species production in response to abscisic acid. Additionally, KAT2 may function downstream of transcription repressor WRKY40, which may link KAT2 with abscisic acid receptor ABAR/CHLH-mediated signaling
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). THIK2_ARATH
462
0
48579
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
crystal structure analysis, secondary structure, the enzyme shows a combination of two similar alpha/beta domains capped with a loop domain, comparison to the structure of the enzyme from Saccharomyces cerevisiae, overview
additional information
-
crystal structure analysis, secondary structure, the enzyme shows a combination of two similar alpha/beta domains capped with a loop domain, comparison to the structure of the enzyme from Saccharomyces cerevisiae, overview
additional information
enzyme interacts with the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling
additional information
-
enzyme interacts with the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
processing of the peroxisomal precursor protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml of protein solution is mixed with 0.002 ml reservoir solution containing 0.1 M TrisHCl, pH 8.5, 300 mM MgCl2, and 25% w/v polyethylene glycol 4000, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution
to 1.5 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
in the absence of both cystamine and cysteamine isoform KAT2 spontaneously inactivates with a half-life
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged truncated enzyme lacking the N-terminal peroxisomal targeting sequence of 34 amino acid residues from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, His-tag removal by thrombin, to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of a His-tagged truncated enzyme lacking the N-terminal peroxisomal targeting sequence of 34 amino acid residues in Escherichia coli strain BL21(DE3)
expression of KAT gene on chromosome 2 mutant lacking the putative N-terminal peroxisomal targeting sequence in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Germain, V.; Rylott, E.L.; Larson, T.R.; Sherson, S.M.; Bechtold, N.; Carde, J.P.; Bryce, J.H.; Graham, I.A.; Smith, S.M.
Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings
Plant J.
28
1-12
2001
Arabidopsis thaliana (Q56WD9), Arabidopsis thaliana
Sundaramoorthy, R.; Micossi, E.; Alphey, M.S.; Germain, V.; Bryce, J.H.; Smith, S.M.; Leonard, G.A.; Hunter, W.N.
The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation
J. Mol. Biol.
359
347-357
2006
Arabidopsis thaliana (Q56WD9), Arabidopsis thaliana
Pye, V.E.; Christensen, C.E.; Dyer, J.H.; Arent, S.; Henriksen, A.
Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch
J. Biol. Chem.
285
24078-24088
2010
Arabidopsis thaliana (Q56WD9), Arabidopsis thaliana, Helianthus annuus (Q6W6X6), Helianthus annuus
EXTERNAL LINKS (specific for EC-Number 2.3.1.16)
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