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Information on EC 3.1.2.2 - palmitoyl-CoA hydrolase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8GYW7
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3.1.2.2 palmitoyl-CoA hydrolaseIUBMB Comments
Also hydrolyses CoA thioesters of other long-chain fatty acids.
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Word Map
- 3.1.2.2
- acyl-coas
- polyketide
- thioesters
-
nonribosomal
- acyltransferase
- synthetases
-
cyclization
- palmitate
- acyl-acps
-
macrocyclization
-
medium-chain
-
beta-oxidation
-
6-deoxyerythronolide
-
enoyl
-
beta-ketoacyl
-
macrolactone
-
nrpss
-
depalmitoylation
- malonyl-coa
- coash
- 4'-phosphopantetheine
-
tyrocidine
- orlistat
- palmitoyl-protein
- lipofuscinosis
- cuphea
-
transacylase
-
surfactin
-
ceroid
-
chain-length
-
uropygial
-
s-acylated
-
ketosynthase
-
chain-terminating
-
didomains
- 4-chlorobenzoate
- enterobactin
- saccharopolyspora
-
12-membered
- phosphopantetheine
- biotechnology
- n-acetylcysteamine
- ketoreductase
-
acyl-carrier
- myristoyl-coa
-
off-loading
- erythraea
- mallard
-
macrolactamization
-
offload
-
triketide
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
thioesterase, palmitoyl-coa hydrolase, acot7, thioesterase ii, acot1, type ii fas, acot2, thioesterase i, mte-i, cte-i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACH1
-
-
-
-
ACH2
-
-
-
-
ACT
-
-
-
-
acyl CoA hydrolase
-
-
-
-
acyl coenzyme A hydrolase
-
-
-
-
acyl coenzyme A thioesterase
-
-
-
-
acyl-CoA thioesterase
brain acyl-CoA hydrolase
-
-
-
-
fatty acyl thioesterase I
-
-
-
-
HIV-Nef associated acyl coA thioesterase
-
-
-
-
hydrolase, acyl coenzyme A
-
-
-
-
hydrolase, palmitoyl coenzyme A
-
-
-
-
LACH1
-
-
-
-
LACH2
-
-
-
-
long chain acyl-CoA hydrolase
-
-
-
-
long chain acyl-CoA thioesterase
-
-
-
-
long chain fatty-acyl-CoA hydrolase
-
-
-
-
long chain fatty-acyl-CoA thioesterase
-
-
-
-
mitochondrial acyl-CoA thioesterase
-
-
-
-
palmitoyl coenzyme A hydrolase
-
-
-
-
palmitoyl thioesterase
-
-
-
-
palmitoyl-CoA deacylase
-
-
-
-
palmitoyl-CoA hydrolase
-
-
-
-
palmityl coenzyme A deacylase
-
-
-
-
palmityl thioesterase
-
-
-
-
palmityl thioesterase I
-
-
-
-
palmityl thioesterase II
-
-
-
-
TE
-
-
-
-
TE-II
-
-
-
-
thioesterase B
-
-
-
-
thioesterase II
-
-
-
-
very long chain acyl-CoA thioesterase
-
-
-
-
ZAP128
-
-
-
-
acyl-CoA thioesterase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + H2O = CoA + palmitate
catalytic triad D337-Q409-S359
Q8GYW7
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA hydrolase
Also hydrolyses CoA thioesters of other long-chain fatty acids.
CAS REGISTRY NUMBER
COMMENTARY
37270-64-7
EC 3.1.2.2
9025-87-0
-
9025-87-0
EC 3.1.2.20
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
palmitoleoyl-CoA + H2O
CoA + palmitoleate
Q8GYW7
activity of ACH2 is not linked to fatty acid oxidation
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
Q8GYW7
prefers unsaturated acyl-CoA
-
?
acyl-CoA + H2O
CoA + a carboxylate
Q8GYW7
long-chain fatty-acyl-CoA
-
?
acyl-CoA + H2O
CoA + a carboxylate
Q8GYW7
enzyme is not linked to fatty acid oxidation
-
?
additional information
?
-
-
broad substrate specificity, preference for long-chain unsaturated fatty acids
-
?
additional information
?
-
Q8GYW7
broad substrate specificity, preference for long-chain unsaturated fatty acids
-
?
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
palmitoleoyl-CoA + H2O
CoA + palmitoleate
Q8GYW7
activity of ACH2 is not linked to fatty acid oxidation
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
Q8GYW7
enzyme is not linked to fatty acid oxidation
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acyl-CoA
Q8GYW7
e.g. lauroyl-CoA, at 0.005 mM, can be overcome by addition of bovine serum albumin or alpha-casein
CoASH
Q8GYW7
feedback inhibition of recombinant enzyme at concentrations above 0.1 mM
additional information
-
reversible substrate inhibition by long-chain acyl-CoAs at concentration 0.005 mM, reversibel by bovine serum albumin and alpha-casein
-
additional information
Q8GYW7
reversible substrate inhibition by long-chain acyl-CoAs at concentration 0.005 mM, reversibel by bovine serum albumin and alpha-casein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
Q8GYW7
pH 7.5: about 40% of maximal activity, pH 9.5: about 40% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a AtACH5 gene knock-out mutant shows no altered phenotype
additional information
-
AtACH5 knockout mutants do not have an altered phenotype
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 6.0, activity of recombinant His-tagged enzyme remains constant for 3 days
Q8GYW7
4°C, pH 6.0, fully stable for 3 days, 90% remaining activity at pH 8.0 after 3 days
Q8GYW7
4°C, pH 8.0, 3 days, recombinant His-tagged enzyme retains 90% of the original activity
Q8GYW7
4°C, purified recombinant HIs-tagged enzyme, pH 6.0, no loss of activity after 3 days
Q8GYW7
4°C, purified recombinant HIs-tagged enzyme, pH 8.0, 90% remaining activity after 3 days
Q8GYW7
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification of recombinant ACH2 overexpressed in Escherichia coli
-
partially, recombinant isozyme AtACH2 fused to maltose-binding protein from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli BL-21(DE3) as a His-tagged protein
Q8GYW7
DNA sequence determination and analysis of isolated and commercial clone, overexpression of His-tagged isozyme ACH2 in Escherichia coli BL21(DE3) cells
Q8GYW7
functional overexpression of AtACH2 in Escherichia coli, overexpression of AtACH5 fused to the green fluorescent protein in Escherichia coli
-
gene ACH2, DNA and amino acid sequence determination and analysis, overexpression as C-terminally His-tagged protein in Escherichia coli BL21(DE3)
Q8GYW7
overexpression of isozymes AtACH5and AtACH2 in Escherichia coli , AtACH2 fused to maltose-binding protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
enzyme is involved in fatty acid biosynthesis and may be a good target for improvement of special oil production in transgenic plants
biotechnology
-
enzyme can be used for bioengineering of transgenic plants to produce oils with desired properties
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Poupon, V.; Begue, B.; Gagnon, J.; Dautry-Varsat, A.; Cerf-Bensussan, N.; Benmerah, A.
Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase
J. Biol. Chem.
274
19188-19194
1999
Arabidopsis thaliana, Bacillus subtilis, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus (Q9R0X4), Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
Tilton, G.B.; Shockey, J.M.; Browse, J.
Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from arabidopsis thaliana
J. Biol. Chem.
279
7487-7494
2004
Arabidopsis thaliana, Arabidopsis thaliana (Q8GYW7)
EXTERNAL LINKS (specific for EC-Number 3.1.2.2)
Transporter Classification Database (TCDB): 4.C.3.1.1
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Release 2023.1 (January 2023)
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