Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.2.2 - palmitoyl-CoA hydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P41903

for references in articles please use BRENDA:EC3.1.2.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.2 palmitoyl-CoA hydrolase
IUBMB Comments
Also hydrolyses CoA thioesters of other long-chain fatty acids.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P41903
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
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
thioesterase, palmitoyl-coa hydrolase, acot7, thioesterase ii, acot1, type ii fas, acot2, thioesterase i, mte-i, cte-i, 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
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA hydrolase
Also hydrolyses CoA thioesters of other long-chain fatty acids.
CAS REGISTRY NUMBER
COMMENTARY hide
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) 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
-
-
-
?
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
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oleate
induces enzyme expression in peroxisomes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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), Homo sapiens, Saccharomyces cerevisiae (P41903), Saccharomyces cerevisiae
Manually annotated by BRENDA team