BRENDA - Enzyme Database
show all sequences of 3.1.2.1

A cold-labile acetyl-coenzyme-A hydrolase from the supernatant fraction of rat liver. Reactivation and reconstitution of the active species from the inactive monomer

Isohashi, F.; Nakanishi, Y.; Matsunaga, T.; Sakamoto, Y.; Eur. J. Biochem. 142, 177-181 (1984)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
acetyl-CoA
at time of rewarming 0.5 mM acetyl-CoA restores the activity about 50%
Rattus norvegicus
albumin
albumin enhances the reactivation of the monomeric form
Rattus norvegicus
ATP
at time of rewarming ATP greatly enhances the restoration of the activity, 2 mM ATP restores the enzyme activity about 70%
Rattus norvegicus
diphosphate
450 mM pyrophosphate restores the activity about 80% at time of rewarming
Rattus norvegicus
phosphate
920 mM phosphate restores the activity about 80% at time of rewarming
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
extramitochondrial
Rattus norvegicus
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
135000
-
-
Rattus norvegicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Rattus norvegicus
Renatured (Commentary)
Commentary
Organism
from cold inactivation
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Subunits
Subunits
Commentary
Organism
monomer
sucrose density gradient centrifugation
Rattus norvegicus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
warming at 37°C after cold exposure is optimal for reactivation
Rattus norvegicus
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7
8
purified dimeric enzyme fairly stable in potassium phosphate buffer of pH 7.0-8.0
Rattus norvegicus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
acetyl-CoA
at time of rewarming 0.5 mM acetyl-CoA restores the activity about 50%
Rattus norvegicus
albumin
albumin enhances the reactivation of the monomeric form
Rattus norvegicus
ATP
at time of rewarming ATP greatly enhances the restoration of the activity, 2 mM ATP restores the enzyme activity about 70%
Rattus norvegicus
diphosphate
450 mM pyrophosphate restores the activity about 80% at time of rewarming
Rattus norvegicus
phosphate
920 mM phosphate restores the activity about 80% at time of rewarming
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
extramitochondrial
Rattus norvegicus
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
135000
-
-
Rattus norvegicus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Rattus norvegicus
Renatured (Commentary) (protein specific)
Commentary
Organism
from cold inactivation
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
sucrose density gradient centrifugation
Rattus norvegicus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
warming at 37°C after cold exposure is optimal for reactivation
Rattus norvegicus
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7
8
purified dimeric enzyme fairly stable in potassium phosphate buffer of pH 7.0-8.0
Rattus norvegicus
Other publictions for EC 3.1.2.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
749835
Yu
-
Exploring succinic acid produ ...
Yarrowia lipolytica, Yarrowia lipolytica W29
Biochem. Eng. J.
139
51-56
2018
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1
1
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750619
Ronowska
The regulatory effects of ace ...
Rattus norvegicus
Front. Cell. Neurosci.
12
169
2018
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732790
Laurieri
From arylamine N-acetyltransfe ...
Homo sapiens, Mus musculus
PLoS ONE
9
e96370
2014
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731079
Khandokar
Expression, purification and c ...
Neisseria meningitidis
Acta Crystallogr. Sect. F
69
1303-1306
2013
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732297
Horibata
Enzymatic and transcriptional ...
Mus musculus, Rattus norvegicus
J. Lipid Res.
54
2049-2059
2013
4
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1
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1
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4
3
2
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4
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3
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1
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708570
Fleck
Re-characterisation of Sacchar ...
Saccharomyces cerevisiae
Fungal Genet. Biol.
46
473-485
2009
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692135
Carman
Role of acetyl coenzyme A synt ...
Candida albicans, Saccharomyces cerevisiae, Saccharomyces cerevisiae SC5314
Eukaryot. Cell
7
1733-1741
2008
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7
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664215
Yamashita
Acetate generation in rat live ...
Rattus norvegicus
Biochim. Biophys. Acta
1761
17-23
2006
1
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2
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1
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2
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1
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6
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1
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6
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3
1
1
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1
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677296
Suematsu
Molecular cloning and function ...
Homo sapiens
Acta Biochim. Pol.
53
553-561
2006
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1
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666604
Bender-Machado
Expression of a yeast acetyl C ...
Saccharomyces cerevisiae
Plant Mol. Biol.
55
645-662
2004
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652385
Buu
Functional characterization an ...
Saccharomyces cerevisiae
J. Biol. Chem.
278
17203-17209
2003
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2
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649087
Suematsu
Mouse cytosolic acetyl-CoA hyd ...
Mus musculus
Acta Biochim. Pol.
49
937-945
2002
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650340
Yamashita
Production of acetate in the l ...
Rattus norvegicus
Biochim. Biophys. Acta
1532
79-87
2001
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1
1
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651098
Suematsu
Molecular cloning and function ...
Rattus norvegicus
Eur. J. Biochem.
268
2700-2709
2001
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1
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2
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94485
Mack
Conversion of glutaconate CoA- ...
Acidaminococcus fermentans
FEBS Lett.
405
209-212
1997
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94487
De Mata
-
Acetyl-CoA hydrolase activity ...
Ascaris suum
Comp. Biochem. Physiol. B
166
379-383
1997
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94489
Lee
Acetyl-CoA hydrolase involved ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1297
105-109
1996
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94490
Garras
Subcellular localisation and i ...
Rattus norvegicus
Biochim. Biophys. Acta
1255
154-160
1995
5
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94491
Grahame
Substrate and accessory protei ...
Methanosarcina barkeri
Biochemistry
34
4617-4624
1995
1
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94492
Nakanishi
Effects of chronic administrat ...
Rattus norvegicus
Biochem. Pharmacol.
45
1403-1407
1993
2
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94494
Connerton
An acetate-sensitive mutant of ...
Neurospora crassa
J. Gen. Microbiol.
138
1797-1800
1992
1
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94493
Hovik
Metabolism of acetyl-CoA by is ...
Rattus norvegicus
J. Lipid Res.
32
993-999
1991
2
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1
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94486
Lee
A glucose-repressible gene enc ...
Saccharomyces cerevisiae
J. Biol. Chem.
265
7413-7418
1990
3
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94488
Zeiher
Identification and characteriz ...
Cucumis sativus, Panicum sp., Pisum sativum, Ricinus communis, Solanum tuberosum, Spinacia oleracea, Zea mays
Plant Physiol.
94
20-27
1990
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1
1
7
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9
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7
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6
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7
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6
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1
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94484
Chabtree
Evidence that the production o ...
Rattus norvegicus
Biochem. J.
257
673-678
1989
1
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1
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2
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94495
Preston
Acetate-activating enzymes of ...
Bradyrhizobium japonicum, Glycine max
Appl. Environ. Microbiol.
55
165-170
1989
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-
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3
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3
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1
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1
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94482
Nakanishi
Binding of nucleotides to an e ...
Rattus norvegicus
Biochemistry
27
4822-4826
1988
2
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7
-
1
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1
1
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2
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7
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2
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2
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94483
Barker
Enzymatic reactions in the deg ...
Anaerocolumna aminovalerica
J. Biol. Chem.
262
8994-9003
1987
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1
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94479
Söling
On the regulation of cold-labi ...
Rattus norvegicus
Eur. J. Biochem.
147
111-117
1985
4
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4
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4
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4
1
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2
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1
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3
2
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94480
Nakanishi
Oxidative inactivation of an e ...
Rattus norvegicus
Eur. J. Biochem.
152
337-342
1985
1
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5
-
1
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1
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94481
Matsunaga
Physiological changes in the a ...
Rattus norvegicus
Eur. J. Biochem.
152
331-336
1985
3
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1
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3
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3
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94477
Isohashi
A cold-labile acetyl-coenzyme- ...
Rattus norvegicus
Eur. J. Biochem.
142
177-181
1984
5
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1
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1
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1
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1
1
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5
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1
1
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1
1
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1
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-
-
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94478
Bronfman
Carnitine acyltransferase and ...
Homo sapiens, Rattus norvegicus
Biochem. J.
224
721-730
1984
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3
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2
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1
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9
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1
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9
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94475
Isohashi
Effects of nucleotides on a co ...
Rattus norvegicus
Biochemistry
22
584-590
1983
1
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2
1
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3
1
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3
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1
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2
1
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2
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3
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1
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2
1
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3
1
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1
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1
-
2
2
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3
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94476
Isohashi
Factors affecting the cold ina ...
Rattus norvegicus
Eur. J. Biochem.
134
447-452
1983
1
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1
2
1
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1
1
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5
2
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1
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1
1
1
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-
5
2
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1
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-
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94474
Namboodiri
Activation of pineal acetyl co ...
Rattus norvegicus
J. Biol. Chem.
257
10030-10032
1982
9
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1
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9
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1
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-
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1
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-
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94472
Prass
Purification and characterizat ...
Bos taurus, Cavia porcellus, Gallus gallus, Mesocricetus auratus, Mus musculus, Platyrrhini, Rattus norvegicus
J. Biol. Chem.
255
5215-5223
1980
1
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5
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1
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3
1
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8
-
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1
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8
2
1
6
1
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2
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1
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1
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1
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8
2
1
6
1
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2
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-
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94473
Namboodiri
Rapid and reversible activatio ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
96
188-195
1980
6
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1
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1
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6
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1
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94471
Grigat
Acetyl-coenzyme A deacylase ac ...
Rattus norvegicus
Biochem. J.
177
71-79
1979
-
-
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2
4
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1
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1
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4
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4
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1
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1
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4
-
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-
-
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94470
Snoswell
Deacylation of acetyl-coenzyme ...
Ovis aries
Biochem. J.
171
299-303
1978
-
-
-
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1
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1
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3
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7
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7
-
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-
-
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94467
Klein
The enzymic hydrolysis of acet ...
Crithidia fasciculata, Trypanosoma brucei brucei, Trypanosoma cruzi, Trypanosoma dionisii, Trypanosoma vespertilionis
Biochem. Soc. Trans.
4
285-287
1976
6
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2
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5
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5
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6
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5
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94468
Robinson
Studies on rat brain acyl-coen ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
71
959-965
1976
4
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1
5
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1
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2
1
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1
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1
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10
1
1
8
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1
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4
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1
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5
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1
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1
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10
1
1
8
-
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-
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1
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-
-
-
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94469
Bernson
Acetyl-CoA hydrolase; activity ...
Mesocricetus auratus, Rattus norvegicus
Eur. J. Biochem.
67
403-410
1976
1
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5
1
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2
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3
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1
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1
2
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-
81013
Gergely
-
Succinyl and acetyl coenzyme A ...
Sus scrofa
J. Biol. Chem.
198
323-334
1952
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1
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