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Information on EC 3.1.2.20 - acyl-CoA hydrolase

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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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Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q7BUF9
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Word Map
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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an acyl-CoA
+
H2O
=
CoA
+
a carboxylate
+
=
+
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
type II thioesterase
-
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
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-RifM1 + H2O
?
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
decanoyl-CoA + H2O
CoA + decanoate
show the reaction diagram
-
-
-
?
hexanoyl-CoA + H2O
CoA + hexanoate
show the reaction diagram
-
-
-
?
isobutyryl-CoA + H2O
CoA + isobutyrate
show the reaction diagram
-
-
-
?
malonyl-CoA + H2O
CoA + malonate
show the reaction diagram
-
-
-
?
methylmalonyl-CoA + H2O
CoA + methylmalonate
show the reaction diagram
-
-
-
?
methylmalonyl-RifM1 + H2O
?
show the reaction diagram
-
-
-
?
octanoyl-CoA + H2O
CoA + octanoate
show the reaction diagram
-
-
-
?
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
-
-
-
?
propionyl-RifM1 + H2O
?
show the reaction diagram
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q7BUF9_AMYMD
259
0
28166
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
in solution, gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by hanging drop vapor diffusion at 4°C. Two RifR polypeptides in the asymmetric unit (P2(1): a=39.5 A, b=94.6 A, c=63.2 A, beta=90.55°)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S94A
thioesterase activity is effectively eliminated for all substrates except with isobutyryl-CoA and propionyl-CoA. No breakdown of [14C]acyl-S639A RifM1 substrates
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50 mM HEPES buffer, pH 7.5, 50 mM NaCl, 1 mM EDTA, 1 mM tris-(2-carboxyethyl)phosphine, 10% (v/v) glycerol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration and metal affinity column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21 StarTM
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Claxton, H.B.; Akey, D.L.; Silver, M.K.; Admiraal, S.J.; Smith, J.L.
Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway
J. Biol. Chem.
284
5021-5029
2009
Amycolatopsis mediterranei (Q7BUF9), Amycolatopsis mediterranei
Manually annotated by BRENDA team