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Information on EC 3.1.2.20 - acyl-CoA hydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P41903

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.20 acyl-CoA hydrolase
IUBMB Comments
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P41903
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
acyl-coa hydrolase, them2, type ii thioesterase, them1, acot11, them4, acot13, thioesterase superfamily member 2, te ii, thioesterase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA hydrolase
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
CAS REGISTRY NUMBER
COMMENTARY hide
37270-64-7
EC 3.1.2.2
9025-87-0
EC 3.1.2.20
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
involved in fatty acid metabolism
-
?
decanoyl-CoA + H2O
CoA + decanoate
show the reaction diagram
-
-
-
?
8-methyl-nonanoyl-CoA + H2O
8-methylnonanoate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
-
-
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
-
the enzyme is required for efficient degradation of short straight chain and branched chain fatty acids
-
-
?
butanoyl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
highest specific activity of the substrates tested
-
-
?
decanoyl-CoA + H2O
decanoate + CoA
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + H2O
dodecanoate + CoA
show the reaction diagram
-
-
-
-
?
nonanoyl-CoA + H2O
nonanoate + CoA
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + H2O
octanoate + CoA
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + H2O
oleate + CoA
show the reaction diagram
-
-
-
-
?
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
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
involved in fatty acid metabolism
-
?
8-methyl-nonanoyl-CoA + H2O
8-methylnonanoate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
-
-
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
-
the enzyme is required for efficient degradation of short straight chain and branched chain fatty acids
-
-
?
butanoyl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
highest specific activity of the substrates tested
-
-
?
decanoyl-CoA + H2O
decanoate + CoA
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + H2O
dodecanoate + CoA
show the reaction diagram
-
-
-
-
?
nonanoyl-CoA + H2O
nonanoate + CoA
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + H2O
octanoate + CoA
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + H2O
oleate + CoA
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoASH
-
IC50: 0.03 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oleate
induces enzyme expression in peroxisomes
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
8-methylnonanoyl-CoA
-
pH 8.0
0.0764
acetyl-CoA
-
pH 8.0
0.0352
butanoyl-CoA
-
pH 8.0
0.0271
decanoyl-CoA
-
pH 8.0
0.0104
dodecanoyl-CoA
-
pH 8.0
0.0218
nonanoyl-CoA
-
pH 8.0
0.0175
octanoyl-CoA
-
pH 8.0
0.0059
oleoyl-CoA
-
pH 8.0
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
CoASH
Saccharomyces cerevisiae
-
IC50: 0.03 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
activity with octanoyl-CoA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.3
-
pH 7.0: about 30% of maximal activity, pH 8.3: about 65% of maximal activity, activity with octanoyl-CoA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43400
-
x * 43400, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 43400, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YJR019C, DNA sequence determination and analysis, subcloning in Escherichia coli, expression fused to maltose-binding-protein in Escherichia coli strain DH10B
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jones, J.M.; Nau, K.; Geraghty, M.T.; Erdmann, R.; Gould, S.J.
Identification of peroxisomal acyl-CoA thioesterases in yeast and humans
J. Biol. Chem.
274
9216-9223
1999
Homo sapiens (O14734), Saccharomyces cerevisiae (P41903)
Manually annotated by BRENDA team
Maeda, I.; Delessert, S.; Hasegawa, S.; Seto, Y.; Zuber, S.; Poirier, Y.
The peroxisomal acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids
J. Biol. Chem.
281
11729-11735
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team