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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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This record set is specific for:
UNIPROT: Q9HU04
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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
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
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?
Q9HU04_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
147
0
16464
TrEMBL
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
experimental data and theoretical predictions, gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of Se-Met-substituted protein or of the native protein obtained by hanging-drop vapor diffusion, to 1.9 A resolution. Usage of additives (ATP, 4-(2-hydroxyethyl)-1-piperazinepropanesulfonic acid, 2-(N-morpholino)ethanesulfonic acid at pH 5.9, 3-(N-morpholino)propanesulfonic acid, HEPES at pH 7.0, sodium diphosphate, glucose-6-phosphate, nondetergent sulfobetaines 201 or 256, sodium CoA, lithium myristoyl-CoA, lithium benzoyl-CoA and lithium acetyl-CoA), yielding new crystal forms. The PA5185 protein crystallizes in four different forms. Crystal growth of PA5185 optimized by applying additives with chemical similarity to a fragment of a putative PA5185 substrate (CoA or its derivative). Application of function-biased additives can be used as a standard optimization protocol for producing improved diffraction, or new crystal forms, which may lead to better understanding of the biological functions of proteins like PA5185
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
native protein expressed using a modified pET-15b plasmid transformed into B834-(DE3)pLysS Escherichia coli cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chruszcz, M.; Zimmerman, M.D.; Wang, S.; Koclega, K.D.; Zheng, H.; Evdokimova, E.; Kudritska, M.; Cymborowski, M.; Savchenko, A.; Edwards, A.; Minor, W.
Function-Biased Choice of Additives for Optimization of Protein Crystallization: The Case of the Putative Thioesterase PA5185 from Pseudomonas aeruginosa PAO1
Cryst. Growth Des.
8
4054-4061
2008
Pseudomonas aeruginosa PAO1, Pseudomonas aeruginosa PAO1 (Q9HU04)
Manually annotated by BRENDA team