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Information on EC 6.2.1.1 - acetate-CoA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q01574

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.1 acetate-CoA ligase
IUBMB Comments
Also acts on propanoate and propenoate.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q01574
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
acyl-coa synthetase, acetyl-coa synthetase, acss2, acetyl-coa synthase, acetyl coa synthetase, acetyl-coenzyme a synthetase, codh/acs, acecs2, acetyl coenzyme a synthetase, acecs1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AceCS
-
-
-
-
Acetate thiokinase
-
-
-
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Acetate--CoA ligase
-
-
-
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Acetic thiokinase
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-
-
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Acetyl activating enzyme
-
-
-
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Acetyl CoA ligase
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-
-
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Acetyl CoA synthase
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-
-
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Acetyl coenzyme A synthetase
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-
-
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Acetyl-CoA synthase
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-
-
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Acetyl-CoA synthetase
acetyl-CoA synthetase 2
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Acetyl-coenzyme A synthase
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-
-
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acetyl-coenzyme A synthetase
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Acyl-activating enzyme
-
-
-
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Short chain fatty acyl-CoA synthetase
-
-
-
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Short-chain acyl-coenzyme A synthetase
-
-
-
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Synthetase, acetyl coenzyme A
-
-
-
-
additional information
-
acetyl-CoA synthetase belongs to the superfamily of adenylate-forming enzymes, whose three-dimensional structures are analogous to one another
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
show the reaction diagram
ordered bi uni uni bi ping-pong mechanism with ordered substrate addition and release
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetate:CoA ligase (AMP-forming)
Also acts on propanoate and propenoate.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-31-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3-bromopropanoate + CoA
AMP + diphosphate + 3-bromopropanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 3-chloropropanoate + CoA
AMP + diphosphate + 3-chloropropanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acetate + CoA
?
show the reaction diagram
-
enzyme form Acs1p is primarily responsible for acetate activation during gluconeogenic growth. Enzyme form Acs2p is likely to be the major producer of cytosolic acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
show the reaction diagram
ATP + acrylate + CoA
AMP + diphosphate + acryloyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + fluoroacetate + CoA
AMP + diphosphate + fluoroacetyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + methacrylic acid + CoA
AMP + diphosphate + methacryloyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
show the reaction diagram
ATP + tetrapolyphosphate
adenosine 5'-pentaphosphate
show the reaction diagram
-
-
-
?
ATP + tripolyphosphate
adenosine 5'-tetraphosphate
show the reaction diagram
-
-
-
?
additional information
?
-
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
ATP + acetate + CoA
?
show the reaction diagram
-
enzyme form Acs1p is primarily responsible for acetate activation during gluconeogenic growth. Enzyme form Acs2p is likely to be the major producer of cytosolic acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
show the reaction diagram
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
show the reaction diagram
-
nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Acs2p is the major acetyl-CoA source for HATs in glucose
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-
?
additional information
?
-
-
may contribute to the adenosine 5'-tetraphosphate synthesis and adenosine 5'-pentaphosphate synthesis during yeast sporulation
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
10 mM, 38% of the activity relative to Mg2+. Progressive inactivation of the enzyme by MnCl2 is not reversible by subsequent addition of MgCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Allicin
-
reversible noncovalent specific inhibitor of acetyl-CoA synthetase
bicarbonate
-
-
monovalent cations
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at 200 mM
-
palmitoyl-CoA
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
-
stimulates adenosine 5´-tetraphosphate synthesis
SIR2 protein
-
short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.208 - 0.513
acetate
1.8
acetyl-CoA
-
-
17
Acrylate
-
-
0.16 - 1.2
ATP
0.035 - 0.238
CoA
31.2
fluoroacetate
-
-
8.3 - 10
propanoate
4.7
tripolyphosphate
-
synthesis of adenosine 5´-tetraphosphate
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
adenosine tetraphosphate synthesis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.8
-
about 50% of maximal activity at pH 6.8 and 8.8
7.3 - 8.1
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90% of maximal activity at pH 7.3 and 8.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoform ACS2 is localized primarily to the nucleus, with a minor amount in the cytosol
Manually annotated by BRENDA team
-
aerobic isoenzyme
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
151000
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sedimentation equilibrium analysis
250000
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low speed sedimentation without reaching equilibrium
251200
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gel filtration
261800
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ultracentrifugal studies, sedimentation equilibrium absorption optics
58000
-
gel filtration
78000
-
x * 78000, SDS-PAGE
80500
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x * 80500, SDS-PAGE, aerobic isoenzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
3 * 82500-83500, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, 2.3 A resolution, residues 72-713 of ACS (subcloned into expression vector pET28a and expressed in Escherichia coli) in complex with AMP
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP and AMP stabilize
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freezing and thawing causes loss of activity
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more than 90% loss of activity in solutions of low ionic strength, for 20 min, at 0-4°C or at room temperature
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storage stability is enhanced by high salt and protein concentration
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.5 M potassium phosphate, pH 7.5, 7 mM 2-mercaptoethanol and 0.5 mM EDTA, protein concentration above 5 mg/ml, no loss of activity after 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
residues 72-713 of ACS are subcloned into expression vector pET28a and expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Patel, S.S.; Walt, D.R.
Substrate specificity of acetyl coenzyme A synthetase
J. Biol. Chem.
262
7132-7134
1987
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Frenkel, E.P.; Kitchens, R.L.
Acetyl-CoA synthetase from bakers yeast (Saccharomyces cerevisiae)
Methods Enzymol.
71
317-324
1981
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Satyanarayana, T.; Chervenka, C.H.; Klein, H.P.
Subunit specificity of the two acetyl-CoA synthetases of yeast as revealed by an immunological approach
Biochim. Biophys. Acta
614
601-606
1980
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
Manually annotated by BRENDA team
Frenkel, E.P.; Kitchens, R.L.
Purification and properties of acetyl coenzyme A synthetase from bakers yeast
J. Biol. Chem.
252
504-507
1977
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Satyanarayana, T.; Klein, H.P.
Studies on the aerobic acetyl-coenzyme A synthetase of Saccharomyces cerevisiae: purification, crystallization, and physical properties of the enzyme
Arch. Biochem. Biophys.
174
480-490
1976
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
Manually annotated by BRENDA team
Satyanarayana, T.; Mandel, A.D.; Klein, H.P.
Evidence for two immunologically distinct acetyl-coenzyme A synthetases in yeast
Biochim. Biophys. Acta
341
396-401
1974
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
Manually annotated by BRENDA team
Satyanarayana, T.; Klein, H.P.
Studies on acetyl-coenzyme A synthetase of yeast: inhibition by long-chain acyl-coenzyme A esters
J. Bacteriol.
115
600-606
1973
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
Manually annotated by BRENDA team
Focke, M.; Feld, A.; Lichtenthaler, H.K.
Allicin, a naturally occuring antibiotic from garlic, specifically inhibits acetyl-CoA synthetase
FEBS Lett.
261
106-108
1990
Bos taurus, Saccharomyces cerevisiae, Hordeum vulgare
Manually annotated by BRENDA team
Van den Berg, M.A.; de Jong-Gubbels, P.; Kortland, C.J.; van Dijken, J.P.; Pronk, J.T.; Steensma, H.Y.
The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation
J. Biol. Chem.
271
28953-28959
1996
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Guranowski, A.; Gunther Sillero, M.A.; Sillero, A.
Adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate are synthesized by yeast acetyl coenzyme A synthetase
J. Bacteriol.
176
2986-2990
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Klein, H.P.; Jahnke, L.
Effects of aeration on formation and localization of the acetyl coenzyme A synthetases of Saccharomyces cerevisiae
J. Bacteriol.
137
179-184
1979
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Starai, V.J.; Takahashi, H.; Boeke, J.D.; Escalante-Semerena, J.C.
Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae
Genetics
163
545-555
2003
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Jogl, G.; Tong, L.
Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP
Biochemistry
43
1425-1431
2004
Saccharomyces cerevisiae (Q01574), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Takahashi, H.; McCaffery, J.M.; Irizarry, R.A.; Boeke, J.D.
Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription
Mol. Cell
23
207-217
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Abe, T.; Hashimoto, Y.; Hosaka, H.; Tomita-Yokotani, K.; Kobayashi, M.
Discovery of amide (peptide) bond synthetic activity in acyl-CoA synthetase
J. Biol. Chem.
283
11312-11321
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Falcon, A.A.; Chen, S.; Wood, M.S.; Aris, J.P.
Acetyl-coenzyme A synthetase 2 is a nuclear protein required for replicative longevity in Saccharomyces cerevisiae
Mol. Cell. Biochem.
333
99-108
2010
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mirzaei, H.; Longo, V.D.
Acetyl-CoA synthetase is a conserved regulator of autophagy and life span
Cell Metab.
19
555-557
2014
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ding, J.; Holzwarth, G.; Penner, M.H.; Patton-Vogt, J.; Bakalinsky, A.T.
Overexpression of acetyl-CoA synthetase in Saccharomyces cerevisiae increases acetic acid tolerance
FEMS Microbiol. Lett.
362
1-7
2015
Saccharomyces cerevisiae (P52910), Saccharomyces cerevisiae
Manually annotated by BRENDA team