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Enzyme Nomenclature
Information on EC 6.2.1.1 - acetate-CoA ligase
for references in articles please use BRENDA:EC6.2.1.1
Word Map on EC 6.2.1.1
- 6.2.1.1
-
synthetases
- glyoxylate
- isocitrate
-
a-cluster
-
deacetylation
- acetaldehyde
-
codhs
- phosphotransacetylase
-
methanogen
- thermoaceticum
-
sirtuins
-
glucose-limited
-
moorella
-
acetogens
- propionyl-coa
-
wood-ljungdahl
-
atp-citrate
- corrinoid
-
1-14cacetate
- methanosarcina
- acetoacetyl-coa
-
alpha2beta2
-
methanogenesis
-
acetate-induced
- ac-coa
- cubane
- medicine
- analysis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
6.2.1.1
-
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RECOMMENDED NAME
GeneOntology No.
acetate-CoA ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
-
-
-
-
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
ordered bi uni uni bi ping-pong mechanism with ordered substrate addition and release
-
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
reaction mechanism involving ([Fe4S4]2+ Nip2+ Nid2+) cluster
-
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
the ACD reaction follows a four-step mechanism including transient phosphorylation of two active site histidine residues, structure and reaction mechanism of ACD
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acetate:CoA ligase (AMP-forming)
Also acts on propanoate and propenoate.
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CAS REGISTRY NUMBER
COMMENTARY
9012-31-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
specific activity of the enzyme is high in cells grown with limited H2 and CO2 supply. It is low in exponentially grown cells
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-
2 enzyme forms Acs1p and Acs2p. Under anaerobic glucose-limited conditions only the ACS2 gene is expressed. During carbon-limited growth on glucose, ethanol, and acetate under aerobic conditions both the ACS1 gene and the ACS2 gene are expressed
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-
; different isoenzymes are elaborated under aerobic and nonaerobic conditions
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; two immunologically distinct enzyme forms are elaborated under aerobic and under nonaerobic conditions
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different isoenzymes are elaborated under aerobic and nonaerobic conditions
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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the metalloprotein acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, ACS/CODH, is a bifunctional metalloenzyme found in anaerobic archaea and bacteria that grow hemoautotrophically on CO or CO2, and is significant for biological carbon fixation and understanding the origin of life
malfunction
metabolism
physiological function
additional information
-
growth arrest is caused by elevated Acs activity, while overproduction of ADP-forming Ac-CoA synthesizing systems, EC 6.2.1.13, do not affect the growth behaviour of acetylation-deficient or acetylation-proficient strains, effects of Acs on growth of different strains, also sirtuin-dependent protein acylation/deacylation system-defective strains, overview. Increased CoA biosynthesis partially alleviates the negative effect caused by high Acs activity, regulation, overview
malfunction
-
growth on 10 mM acetate causes an acs+ induction in a Salmonella enterica strain, that cannot acetylate, i.e. inactivate Acs, leads to growth arrest, a condition that correlates with a drop in energy charge in the acetylation-deficient strain, relative to the energy charge in the acetylation-proficient strain. Acs-dependent depletion of ATP, coupled with the rise in AMP levels, prevents the synthesis of ADP needed to replenish the pool of ATP
malfunction
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deletion of individual and multiple subunits of acetyl-CoA synthetase decreases CoA release activity for several different CoA ester substrates. Deletion of acetyl-CoA synthetases I and II increases production of 3-hydroxypropionate by the metabolically-engineered hyperthermophile Pyrococcus furiosus (containing three enzymes from the CO2 fixation cycle of the thermoacidophilic archaeon Metallosphaerasedula)
metabolism
-
acetyl-CoA synthase, a subunit of the bifunctional CO dehydrogenase/acetyl-CoA synthase, CODH/ACS, complex of Moorella thermoacetica requires reductive activation in order to catalyze acetyl-CoA synthesis and related partial reactions, including the CO/acetyl-CoA exchange reaction. Ferredoxin(II), which harbors two [4Fe-4S] clusters and is an electron acceptor for CODH, serves as a redox activator of ACS. Ferredoxin interfaces with an internal redox shuttle in acetyl-CoA synthase during reductive activation and catalysis. The midpoint reduction potential for the catalytic one-electron redoxactive species in the CO/acetyl-CoAexchange reaction is -511 mV. Incubation of ACS with Fd-II and CO leads to the formation of the NiFeC species. Mechanism, overview
metabolism
-
activation of weak organic acids by acyl-CoA synthetases is costly to cells, since it requires 2 mol of ATP per mol of substrate; 1 mol of ATP is consumed to activate the organic acid, while the second mol of ATP is needed to convert AMP to ADP, the immediate precursor of ATP. Further loss of energy resources during the course of the Acs reaction is caused by the hydrolysis of diphosphate to monophosphate through pyrophosphate phosphohydrolase, EC 3.6.1.1
physiological function
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tumor cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
physiological function
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an acs2 deletion strain has a reduced replicative life span compared to wild-type and isoform acs1 deletion strains. Replicatively aged acs2 deletion cells contain elevated levels of extrachromosomal rDNA circles, and silencing at the rDNA locus is impaired in an acs2 deletion strain
physiological function
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acetyl-coenzyme A synthetase activates acetate into acetyl-coenzyme A in most cells. Salmonella enterica requires Acs activity for growth on acetate. The sirtuin-dependent protein acylation/deacylation system, SDPADS, controls the activity of Acs
physiological function
activation of acetate in energy metabolism
physiological function
-
activation of acetate in energy metabolism
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-bromopropanoate + CoA
AMP + diphosphate + 3-bromopropanoyl-CoA
-
-
-
-
-
ATP + 3-chloropropanoate + CoA
AMP + diphosphate + 3-chloropropanoyl-CoA
-
-
-
-
-
ATP + 3-methylvalerate + CoA
AMP + diphosphate + 3-methylvaleryl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + 4-methylvalerate + CoA
AMP + diphosphate + 4-methylvaleryl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + formate + CoA
AMP + diphosphate + formyl-CoA
-
27% of the activity with acetate
-
-
?
ATP + isobutyrate + CoA
AMP + diphosphate + isobutyryl-CoA
-
28% of the activity with acetate
-
-
?
ATP + methacrylic acid + CoA
AMP + diphosphate + methacryloyl-CoA
-
-
-
-
-
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + pentanoate + CoA
AMP + diphosphate + pentanoyl-CoA
-
6.7% of the activity relative to acetate
-
-
-
CheY + acetyl-CoA + ATP
acetyl-CheY + CoA + AMP + diphosphate
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CheY is the the excitatory response regulator in the chemotaxis system of Escherichia coli, acetyl-CoA synthetase-catalyzed transfer of acetyl groups from acetate to CheY and autocatalyzed transfer from AcCoA, mechanism, overview
-
-
?
ADP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
20% of the activity relative to ATP
-
-
-
ADP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
37% of the activity relative to ATP
-
-
-
ATP + acetate + CoA
?
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enzyme plays an important role in the oxidative part of the aceticlastic reaction
-
-
-
ATP + acetate + CoA
?
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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
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-
-
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
highly specific for ATP
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-
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
gene acs encoding the enzyme is regulated by quorum sensing, and acs regulation plays a role in symbiosis, overview
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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gene acs encoding the enzyme is regulated by quorum sensing, and acs regulation plays a role in symbiosis, overview
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?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
no relationship between the enzyme level and the capacity of the plants to incorporate CO2 into labeled fatty acids. Very limited role of the enzyme in the biosynthesis of lipids
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
acetate-CoA ligase is a key enzyme for conversion of acetate to acetyl-CoA
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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AF-ACS2 has 2.3fold higher affinity and catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
neither glutathione nor pantetheine can substitute for CoA as acyl acceptor
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-
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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enzyme is involved in pathway of acetate activation. Cells induce acs transcription, and thus the ability to assimilate acetate, in response to rising cAMP levels, falling oxygen partial pressure, and the flux of carbon through pathways associated with acetate metabolism
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
the enzyme activates acetate so that it can be used for lipid synthesis or for energy generation. The acetyl-CoA synthetase mRNA, and hence the ability of cells to activate acetate, is regulated by sterol regulatory element-binding proteins in parallel with fatty acid synthesis in animal cells
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
AceCS2 is reversibly acetylated at Lys642 in the active site of the enzyme. A mammalian sirtuin directly controls the activity of a metabolic enzyme by means of reversible lysine acetylation
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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-
-
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-
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
acetate-CoA ligase is a key enzyme for conversion of acetate to acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
MT-ACS1 is limited to acetate and propionate as acyl substrates. MT-ACS1 has nearly 11fold higher affinity and 14fold higher catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
important role for motif III (498YTAGD502) in catalysis. The highly conserved Tyr in the first position may play a key role in active-site architecture through interaction with a highly conserved active-site Gln. The invariant Asp in the fifth position plays a critical role in ATP binding and catalysis through interaction with the 2'- and 3'-OH groups of the ribose moiety of ATP
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
activation of acetate in energy metabolism
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
activity with propionate is 1% compared to the reactivity with acetate. Butyrate does not serve as a substrate
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
activation of acetate in energy metabolism
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
activity with propionate is 1% compared to the reactivity with acetate. Butyrate does not serve as a substrate
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase is a key enzyme in the Wood-Ljungdahl pathway of carbon fixation
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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proposed mechanism of the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase
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?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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the ACS reaction is catalyzed at the alpha-subunit A-cluster, an [Fe4S4] cubane bridged to a dinickel [NipNid] subcomponent, overview
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
reaction of acetylated ACS with CoA and Fd-II, a step of the catalytic cycle in which the acetylated ACS reacts with CoA to form acetyl-CoA
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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lipogenic enzyme, gene is highly induced by SREBP-1a, SREBP-1c and SREBP-2. The enzyme might also play an important role in basic cellular energy metabolism
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
specific for acetate, no activity with other short-chain fatty acids
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-
-
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
acetyl-CoA synthetase from Pseudomonas putida U is the only acyl-CoA activating enzyme induced by acetate in this bacterium
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-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
formation of enzyme-bound acetyl phosphate and enzyme phosphorylation at His257alpha, respectively. The phosphoryl group is transferred from the His257alpha to ADP via transient phosphorylation of a second conserved histidine residue in the beta-subunit, His71beta
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ir
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
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-
-
-
-
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
-
ATP + acrylate + CoA
AMP + diphosphate + acryloyl-CoA
-
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
mutant enzymes I312A and W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
mutant enzymes I312A and W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
20% of the activity relative to acetate
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
26% of the activity with acetyl-CoA
-
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
25% of the activity with acetate
-
-
?
ATP + fluoroacetate + CoA
AMP + diphosphate + fluoroacetyl-CoA
-
-
-
-
-
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
very poor activity
-
-
-
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
30% of the activity with acetate
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
5% of the activity relative to acetate
-
-
-
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
48% of the activity relative to acetate
-
-
-
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
118% of the activity with acetate
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
-
-
-
-
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
AF-ACS2 has 2.3fold higher affinity and catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
-
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
MT-ACS1 is limited to acetate and propionate as acyl substrates. MT-ACS1 has nearly 11fold higher affinity and 14fold higher catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
-
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
55% of the activity with acetyl-CoA
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase. Acetate-CoA ligase operates at the end of the pathway
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase. Acetate-CoA ligase operates at the end of the pathway
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Acs2p is the major acetyl-CoA source for HATs in glucose
-
-
?
ATP + valerate + CoA
AMP + diphosphate + valeryl-CoA
-
mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme
-
-
?
ATP + valerate + CoA
AMP + diphosphate + valeryl-CoA
8% of the activity with acetyl-CoA
-
-
?
dATP + acetate + CoA
dAMP + diphosphate + acetyl-CoA
-
70% of the activity relative to ATP
-
-
dATP + acetate + CoA
dAMP + diphosphate + acetyl-CoA
-
30% of the activity relative to ATP
-
-
-
dATP + acetate + CoA
dAMP + diphosphate + acetyl-CoA
AceCS2 plays a role in the production of energy under ketogenic conditions, such as starvation and diabetes. Acetyl-CoAs produced by AceCS2 are utilized mainly for oxidation
-
?
additional information
?
-
-
metabolic connection between acetate utilization and cell density
-
-
-
additional information
?
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-
metabolic connection between acetate utilization and cell density
-
-
-
additional information
?
-
role of ACS in destroying fermentative intermediates
-
-
-
additional information
?
-
-
the enzyme can catalyze the activation to their CoA thioesters of some of the side-chain precursors required in Penicillium chrysogenum and Aspergillus nidulans for the production of several penicillins
-
-
-
additional information
?
-
-
the acetyltransferase enzyme, AcuA, controls the activity of the acetyl coenzyme A synthetase, AcsA, by acetylating residue Lys549, overview
-
-
-
additional information
?
-
-
enzyme catalyzes acetate-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
acetate thiokinase is not involved in autotrophic CO2 fixation
-
-
-
additional information
?
-
-
CODH/ACS is a bifunctional enzyme that is responsible for the reduction of CO2 to CO and subsequent assembly of acetyl-CoA, as part of the Wood-Ljungdahl carbon fixation pathway, the enzyme is a key player in the global carbon cycle
-
-
-
additional information
?
-
-
bifunctional Ni-Fe-S containing ACS/CODH, although alpha and beta subunits catalyze separate reactions, they interact functionally when CO2 is used as a substrate in the synthesis of acetyl-CoA
-
-
-
additional information
?
-
-
the enzyme is a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase, Moorella thermoacetica CODH/ACS contains a very long enzyme channel to allow for intermolecular CO transport, mechanism and reaction steps, overview. Structure-function analysis in comparison to monofunctional Acs, overview
-
-
-
additional information
?
-
-
3'-dephospho-CoASH analogues with a phosphodiester bond are not capable of accepting acetate
-
-
-
additional information
?
-
-
the enzyme can activate many other molecules to acyl-CoA derivatives: hexanoate, 3-hexenoate, heptanoate, octanoate, 3-octenoate, phenylacetate, 2-thiophene acetate, 3-thiophene acetate
-
-
-
additional information
?
-
-
the enzyme can catalyze the activation to their CoA thioesters of some of the side-chain precursors required in Penicillium chrysogenum and Aspergillus nidulans for the production of several penicillins
-
-
-
additional information
?
-
-
enzyme catalyzes propanoate-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
reaction mechanism of ATP-diphosphate exchange is ordered, ATP is the first substrate to react with the enzyme, and some form of diphosphate is the first product released
-
-
-
additional information
?
-
-
enzyme catalyzes acetate-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
the enzyme performs arsenolysis, the alpha-subunit alone also catalyzes arsenolysis, overview
-
-
-
additional information
?
-
-
may contribute to the adenosine 5'-tetraphosphate synthesis and adenosine 5'-pentaphosphate synthesis during yeast sporulation
-
-
-
additional information
?
-
-
the enzyme also forms a carbon-nitrogen bond, reaction of EC 6.3.1 acid-ammonia (or amide) ligase, i.e. amide synthase, and EC 6.3.2 acid-amino acid ligase, i.e. peptide synthase, comprising the amino group of the cysteine and the carboxyl group of the acid, overview
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CheY + acetyl-CoA + ATP
acetyl-CheY + CoA + AMP + diphosphate
-
CheY is the the excitatory response regulator in the chemotaxis system of Escherichia coli, acetyl-CoA synthetase-catalyzed transfer of acetyl groups from acetate to CheY and autocatalyzed transfer from AcCoA, mechanism, overview
-
-
?
dATP + acetate + CoA
dAMP + diphosphate + acetyl-CoA
Q99NB1
AceCS2 plays a role in the production of energy under ketogenic conditions, such as starvation and diabetes. Acetyl-CoAs produced by AceCS2 are utilized mainly for oxidation
-
?
ATP + acetate + CoA
?
-
enzyme plays an important role in the oxidative part of the aceticlastic reaction
-
-
-
ATP + acetate + CoA
?
-
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
-
gene acs encoding the enzyme is regulated by quorum sensing, and acs regulation plays a role in symbiosis, overview
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
gene acs encoding the enzyme is regulated by quorum sensing, and acs regulation plays a role in symbiosis, overview
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
no relationship between the enzyme level and the capacity of the plants to incorporate CO2 into labeled fatty acids. Very limited role of the enzyme in the biosynthesis of lipids
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
acetate-CoA ligase is a key enzyme for conversion of acetate to acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
enzyme is involved in pathway of acetate activation. Cells induce acs transcription, and thus the ability to assimilate acetate, in response to rising cAMP levels, falling oxygen partial pressure, and the flux of carbon through pathways associated with acetate metabolism
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
Q9NR19
the enzyme activates acetate so that it can be used for lipid synthesis or for energy generation. The acetyl-CoA synthetase mRNA, and hence the ability of cells to activate acetate, is regulated by sterol regulatory element-binding proteins in parallel with fatty acid synthesis in animal cells
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
Q9NUB1
AceCS2 is reversibly acetylated at Lys642 in the active site of the enzyme. A mammalian sirtuin directly controls the activity of a metabolic enzyme by means of reversible lysine acetylation
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
Q2XNL6
acetate-CoA ligase is a key enzyme for conversion of acetate to acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
A0B8F1
activation of acetate in energy metabolism
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
A0B8F1
activation of acetate in energy metabolism
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase is a key enzyme in the Wood-Ljungdahl pathway of carbon fixation
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
reaction of acetylated ACS with CoA and Fd-II, a step of the catalytic cycle in which the acetylated ACS reacts with CoA to form acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
lipogenic enzyme, gene is highly induced by SREBP-1a, SREBP-1c and SREBP-2. The enzyme might also play an important role in basic cellular energy metabolism
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
Q6EMJ3
acetyl-CoA synthetase from Pseudomonas putida U is the only acyl-CoA activating enzyme induced by acetate in this bacterium
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase. Acetate-CoA ligase operates at the end of the pathway
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase. Acetate-CoA ligase operates at the end of the pathway
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
-
nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Acs2p is the major acetyl-CoA source for HATs in glucose
-
-
?
additional information
?
-
-
metabolic connection between acetate utilization and cell density
-
-
-
additional information
?
-
-
metabolic connection between acetate utilization and cell density
-
-
-
additional information
?
-
B9DGD6
role of ACS in destroying fermentative intermediates
-
-
-
additional information
?
-
-
the enzyme can catalyze the activation to their CoA thioesters of some of the side-chain precursors required in Penicillium chrysogenum and Aspergillus nidulans for the production of several penicillins
-
-
-
additional information
?
-
-
the acetyltransferase enzyme, AcuA, controls the activity of the acetyl coenzyme A synthetase, AcsA, by acetylating residue Lys549, overview
-
-
-
additional information
?
-
-
acetate thiokinase is not involved in autotrophic CO2 fixation
-
-
-
additional information
?
-
-
CODH/ACS is a bifunctional enzyme that is responsible for the reduction of CO2 to CO and subsequent assembly of acetyl-CoA, as part of the Wood-Ljungdahl carbon fixation pathway, the enzyme is a key player in the global carbon cycle
-
-
-
additional information
?
-
-
the enzyme can catalyze the activation to their CoA thioesters of some of the side-chain precursors required in Penicillium chrysogenum and Aspergillus nidulans for the production of several penicillins
-
-
-
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
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
-
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Co2+
Cu2+
-
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Fe2+
K+
Li+
-
activation at 5-8 mM, absolute requirement for certain monovalent cations, inhibition above 10 mM
Mg2+
Mn2+
Na+
NH4+
Ni
-
nickel-containing bimetallic site, the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase
Ni2+
Rb+
-
activates, absolute requirement for certain monovalent cations, no inhibition at high concentrations
Tris
-
activates, absolute requirement for certain monovalent cations, no inhibition at high concentrations
additional information
-
the enzyme uses seven metalloclusters in four reaction steps, overview
Ca2+
-
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Ca2+
-
can replace Mg2+ in activation, with 50% of the efficiency relative to MgCl2; Km for CaCl2 is 1.2 mM
Ca2+
about 30% of the activation with Mg2+ or Mn2+
Ca2+
-
10 mM, can replace Mg2+ in activation, with 30% of the efficiency relative to Mg2+
Co2+
-
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Co2+
-
can replace Mg2+ in activation, 50% as effective as MgCl2, Km for CoCl2 is 0.2 mM
Co2+
about 80% of the activation with Mg2+ or Mn2+
Fe2+
-
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Fe2+
-
CODH/ACS uses a Ni-Fe-S center called the C-cluster to reduce carbon dioxide to carbon monoxide and uses a second Ni-Fe-S center, called the A-cluster, to assemble acetyl-CoA from a methyl group, coenzyme A, and C-cluster-generated CO
Fe2+
-
the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH
Fe2+
-
the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, exchange coupling pathway between the Sc = 1/2 [Fe4S4]1+ cluster and the SNi = 1/2 Nip 1+ involves the cysteinate that links one cluster site, previously labeled FeD, to the Ni1+, structure and spectral analysis, overview
Fe2+
-
the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA
K+
-
absolute requirement for a monovalent cation, stimulates, Km: 14.3 mM, inhibition above 0.1 M
K+
-
activates, absolute requirement for certain monovalent cations, no inhibition at high concentrations
K+
-
KCl increases the activity of the enzyme about 60% at 5 mM and 80% at 20 mM
Mg2+
-
AF-ACS2 shows strong preference for Mg2+ and Mn2+ as the divalent metal
Mg2+
-
required; two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Mg2+
-
inhibition at high concentrations where the metal is present as the free ion; Km for MgCl2 is 0.3 mM; required
Mg2+
strong preference for Mg2+ and Mn2+ as the divalent metal
Mn2+
-
AF-ACS2 shows strong preference for Mg2+ and Mn2+ as the divalent metal
Mn2+
-
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Mn2+
strong preference for Mg2+ and Mn2+ as the divalent metal
Mn2+
-
64% of the activation relative to Mg2+; can replace Mg2+ in activation
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
Na+
-
absolute requirement for a monovalent cation, poor activator, Km: 33 mM, no inhibition at higher concentrations
Na+
-
activation at 5-8 mM, absolute requirement for certain monovalent cations, inhibition above 10 mM
NH4+
-
absolute requirement for a monovalent cation, stimulates, Km: 14.3 mM, inhibition above 0.1 M
NH4+
-
activates, absolute requirement for certain monovalent cations, no inhibition at high concentrations
Ni2+
-
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding
Ni2+
about 25% of the activation with Mg2+ or Mn2+
Ni2+
-
Mössbauer and EPR spectroscopies of alpha-subunit activated with Ni2+
Ni2+
-
activates, the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH. Upon incubation in NiCl2, the complete A-cluster assembles, and the isolated a subunit develops approximately 10% of the maximal catalytic activity relative to that of the alpha2beta2 tetramer
Ni2+
-
the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, exchange coupling pathway between the Sc = 1/2 [Fe4S4]1+ cluster and the SNi = 1/2 Nip 1+ involves the cysteinate that links one cluster site, previously labeled FeD, to the Ni1+, structure and spectral analysis, overview
Ni2+
-
the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA
Ni2+
-
the active site of ACS, denoted as the A-cluster, is composed of a redox-active [Fe4-S4] cluster and a dinuclear Ni(II)d-Ni(II)p unit. Synthesis of the dinuclear Ni(II)-Ni(I) complex NiII(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate)NiI(S-2,6-dimesitylphenyl)-(triphenylphosphine) as a Ni(II)d-Ni(I)p model of the A-cluster in acetyl CoA synthase
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CO
-
CO inhibits acetyl-CoA synthesis quite strongly and in a cooperative manner
Ni
-
the authors favor a mechanism in which methylation occurs first to Ni(p0 -) or Ni(pI -)[Fe4S4]+, followed by coordination of CO to form Ni(pII)(CO)(CH3) which breaks one of the S(Nid) bonds (forming the bis square planar Ni(II) species, as if the Ni(d)N2S2 unit were acting as a biological pseudodiphosphine, mimicking behavior common to a bidentate phosphine). The CO-insertion/CH3-migration occurs on one metal forming the trigonal planar Ni(pII)-acetyl intermediate. Finally, addition of thiolate produces the thioester. The authors disfavor the unprecedented bimetallic, CO-insertion/CH3-migration mechanism (both in its diamagnetic and paramagnetic guise) and disfavors CO, CH3+, or thiolate (CoA) binding to the distal Ni. Finally, Ni in the proximal site produces a better catalyst than does Cu
P1,P5-di(adenosine-5)pentaphosphate
-
inhibits ADP formation
Allicin
-
reversible noncovalent specific inhibitor of acetyl-CoA synthetase
diphosphate
addition of 0.25 mM diphosphate results in 50% reduction of the reaction rate
long-chain acyl-CoA compounds
-
e.g. palmitoyl-CoA, stearoyl-CoA and oleoyl-CoA are potent inhibitors of aerobic enzyme form but not from nonaerobic enzyme form
palmitoyl-CoA
-
noncompetitive with respect to both acetate and CoA , inhibits adenosine 5´-tetraphosphate synthesis
additional information
no inhibition by AMP, ADP, ATP or phosphate
-
additional information
-
antiserum prepared against the aerobic isoenzyme inhibits the homologous enzyme activity but shows no effect on nonaerobic acetyl-CoA synthetase activity
-
additional information
-
aerobic and non-aerobic enzyme form: antibody directed towards one protein precipitated and inhibits the activity of the homologous, but not of the heterologous enzyme
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CobB Sir2 protein
-
activation of the acetylated enzyme requires the nicotinamide adenine dinucleotide-dependent protein deacetylase activity of the CobB Sir2 protein
-
SIR2 protein
-
short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function
-
SIRT1
-
AceCS1 is completely inactivated upon acetylation and is rapidly reactivated by SIRT3 deacetylation
-
SIRT3
-
AceCS2 is completely inactivated upon acetylation and is rapidly reactivated by SIRT3 deacetylation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4 - 10
acetate
-
mutant L641P, pH not specified in the publication, temperature not specified in the publication
41
acetate
-
wild-type Acs, pH not specified in the publication, temperature not specified in the publication
11000
acetate
-
mutant G266S, pH not specified in the publication, temperature not specified in the publication
1.7
ATP
pH 7.0, 65°C, mutant enzyme G501A; pH 7.0, 65°C, mutant enzyme T499A; pH 7.0, 65°C, mutant enzyme Y498A
0.18
CoA
-
65°C, mutant enzyme I312A; 65°C, mutant enzyme V388G
additional information
additional information
-
kinetics and extent of reduction of the Fe4S4 cubane in the apo-alpha subunit and the Ni-activated a subunit upon exposure to titanium(III) citrate, detailed overview
-
additional information
additional information
-
kinetic parameters of wild type and mutant enzymes at 55°C, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1500
acetate
-
mutant L641P, pH not specified in the publication, temperature not specified in the publication
3200
acetate
-
mutant G266S, pH not specified in the publication, temperature not specified in the publication
9400
acetate
-
wild-type Acs, pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
acetate
-
mutant G266S, pH not specified in the publication, temperature not specified in the publication
3.6
acetate
-
mutant L641P, pH not specified in the publication, temperature not specified in the publication
229
acetate
-
wild-type Acs, pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.6
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
pH 5.5: about 60% of maximal activity, pH 8.5: about 50% of maximal activity
6 - 10.5
-
6: about 50% of maximal activity, 10.5: about 60% of activity maximum
6 - 9.7
-
6.0: about 45% of maximal activity, 9.7: about 70% of maximal activity
7.5 - 10
-
7.5: about 50% of maximal activity, 10.0: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
65 - 70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: about 45% of maximal activity, 50°C: about 30% of maximal activity
45 - 85
-
45°C: about 55% of maximal activity, 85°C: about 60% of maximal activity, AF-ACS2
45 - 75
45°C: about 55% of maximal activity, 75°C: about 50% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
marked induction of AceCS1 mRNA and protein during differentiation of 3T3-L1 cells, neither AceCS2 mRNA nor protein is detected in undifferentiated or differentiated 3T3-L1 cells
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
-
from Glycine max L. cv. Williams inoculated with Bradyrhizobium japonicum
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
additional information
no AceCS2 activity is detected in liver. Marked induction of AceCS1 mRNA and protein during differentiation of 3T3-L1 cells, neither AceCS2 mRNA nor protein is detected in undifferentiated or differentiated 3T3-L1 cells
-
1.5fold-2fold higher activity of the enzyme in the periportal zone of the male rat liver compared with the perivenous zone in the fed state, but not in the fasted/refed state
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform ACS2 is localized primarily to the nucleus, with a minor amount in the cytosol
-
isoform ACS2 is localized primarily to the nucleus, with a minor amount in the cytosol
-
constitutive membrane-associated (but not an integral) protein complex, localized at the outermost membrane; outermost membrane
-
constitutive membrane-associated (but not an integral) protein complex, localized at the outermost membrane; outermost membrane
-
-
constitutive membrane-associated (but not an integral) protein complex, localized at the outermost membrane; outermost membrane
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
72000
75000
77000
78000
261800
-
ultracentrifugal studies, sedimentation equilibrium absorption optics
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homooligomer
monomer
tetramer
trimer
additional information
?
x * 71000, AceCS2, SDS-PAGE; x * 74662, AceCS2, calculation from nucleotide sequence; x * 78000, AceCS1, SDS-PAGE
tetramer
-
acetyl-coenzyme A synthase/carbon monoxide dehydrogenase is an alpha2beta2 tetramer, alpha-subunit structure, overview
tetramer
-
acetyl-coenzyme A synthase/carbon monoxide dehydrogenase is an alpha2beta2 tetramer, structure analysis, overview
additional information
-
Moorella thermoacetica CODH/ACS contains a very long enzyme channel to allow for intermolecular CO transport, overview
additional information
-
the beta2 subunits are solely responsible for catalyzing the CODH reaction
additional information
-
the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA. The ACS/CODH from Moorella thermoacetica is an alpha2beta2 tetramer containing seven metal clusters connected by a molecular tunnel network, overview
additional information
-
structural analysis by circular dichroism spectroscopy and structure modelling, comparison of domain organization of subunits to succinyl-CoA synthetases, EC 6.2.1.5, overview
additional information
-
the active site of ACS, denoted as the A-cluster, is composed of a redox-active [Fe4-S4] cluster and a dinuclear Ni(II)d–Ni(II)p unit. Synthesis of the dinuclear Ni(II)-Ni(I) complex NiII(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate)NiI(S-2,6-dimesitylphenyl)-(triphenylphosphine) as a Ni(II)d-Ni(I)p model of the A-cluster in acetyl CoA synthase
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
proteolytic modification
the putative mitochondrial targeting signal is cleaved during the transportation of the enzyme into the mitochondria matrix
side-chain modification
-
the acetyltransferase enzyme, AcuA, controls the activity of the acetyl coenzyme A synthetase, AcsA, by acetylating residue Lys549, overview
acetylation
-
posttranslational regulation by acetylation of Lys609. Acetylation blocks synthesis of the adenylate intermediate but does not affect the thioester-forming activity of the enzyme
acetylation
-
the enzyme is regulated by a Sir2-dependent protein acetylation/deacetylation system. Leu641 is critical for the acetylation of the enzyme by protein acetyltransferase.Mutation at Leu641 prevents the acetylation of Acs by protein acetyltransferase and maintains the acetyl-coenzyme A synthetase in its active state
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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
vapor diffusion method, crystallographic structures of wild-type enzyme and mutant enzymes R194A, R584A, R584E, K609A, and V386A
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
half-life: 8 min. Addition of 1 M (NH4)2SO4 stabilizes the enzyme to a half-life of 24 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
-
-20°C, cannot be stored for more than 3 days without a considerable loss of activity
-
0-4°C, 20 mM Tris/Hcl, pH 8.0, 10 mM ATP, 5 mM MgCl2, 1 mM DTT or 5 mM 2-mercaptoethanol, 20% glycerol, stable for at least 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant alpha and beta subunits from Escherichia coli strain BL21(DE3) by heat tteatment at 90°C for 30 min, hydrophobic interaction chromatography, and gel filtration
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recombinant C-terminally His-tagged ACS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography under anaerobic conditions
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10-deacetylbaccatin III 10beta-O-acetyltransferase (DBAT) from Taxus can catalyze the transfer of acetyl, propionyl or n-butyryl from CoA to the C10-hydroxyl of 10-deacetylbaccatin III. Escherichia coli JM109 are transformed to recombinantly express dbat, and this enzyme function is coupled to that of acetyl-CoA synthase expressed from and regulated by genes encoded on the bacterial chromosome
Taxus sp.
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acetyl-CoA synthetase overexpression in Escherichia coli demonstrates more efficient acetate assimilation and lower acetate accumulation
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expression in Escherichia coli
expression of C-terminally His-tagged ACS in Escherichia coli strain BL21(DE3)
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genes acdIa and acdIb encoding the alpha and beta subunits, expression in Escherichia coli strain BL21(DE3)
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overexpression in Escherichia coli
residues 72-713 of ACS are subcloned into expression vector pET28a and expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of CO dehydrogenase/acetyl coenzyme A synthase in Methanosarcina spp. is coordinately regulated in response to substrate by differential transcription initiation and early elongation termination near the 3' end of a 371-bp leader sequence
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A498A
alteration does not significantly affect the Km for any substrate but reduces the turnover rate kcat 41fold
G501A
two- to threefold reduced Km values for acetate, ATP and CoA. The turnover rate is over 200fold reduced
I312A
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kcat/Km for acetate is 15fold lower than wild-type value, kcat/Km for propionate is 5.2fold lower than wild-type value. Mutant enzyme shows activity with butyrate
T313K
-
Km for acetate is 170fold higher than wild-type value, kcat for acetate is 34fold lower than wild-type value
T313V
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kcat/Km for acetate is 2.5fold lower than wild-type value, kcat/Km for propionate is identical to wild-type value
V388A
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kcat/Km for acetate is 6.9fold lower than wild-type value, kcat/Km for propionate is 2.5fold higher than wild-type value, mutant enzyme shows activity with wild-type enzyme
V388G
-
kcat/Km for acetate is 93fold lower than wild-type value, kcat/Km for propionate is 26fold lower than wild-type value
W416G
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kcat/Km for acetate is 71.5fold lower than wild-type value, kcat/Km for propionate is 13fold lower than wild-type value, mutant enzyme shows activity with: butyrate, valerate, hexanoate, heptanoate, octanoate, 4-methylvalerate and 3-methylvalerate
I312A
-
kcat/Km for acetate is 15fold lower than wild-type value, kcat/Km for propionate is 5.2fold lower than wild-type value. Mutant enzyme shows activity with butyrate
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T313K
-
Km for acetate is 170fold higher than wild-type value, kcat for acetate is 34fold lower than wild-type value
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T313V
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kcat/Km for acetate is 2.5fold lower than wild-type value, kcat/Km for propionate is identical to wild-type value
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V388A
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kcat/Km for acetate is 6.9fold lower than wild-type value, kcat/Km for propionate is 2.5fold higher than wild-type value, mutant enzyme shows activity with wild-type enzyme
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V388G
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kcat/Km for acetate is 93fold lower than wild-type value, kcat/Km for propionate is 26fold lower than wild-type value
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A110C
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site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme
A222L
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site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme
A265M
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site-directed mutagenesis, alpha-subunit mutant, the recombinantly expressed mutant enzymes cannot be purified
C509A
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site-directe mutagenesis, mutant C509A shows a significantly diminished methyl transfer activity compared to the wild-type enzyme
C509H
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site-directed mutagenesis, mutant C509H can accept a methyl group from CH3-Co3+FeSP at over 70% extent. The near-wild-type-level of methyl group transfer activity for C509H indicates that the di-nickel site is assembled well in this mutant, and strongly suggests that an imidazole group can bridge the di-nickel site to the cubane of the A-cluster. Histidine that replaces the bridging cysteine 509 might function as a bridge, with one nitrogen of the imidazole ring coordinating to a cubane Fe and the other nitrogen coordinating to Nip
C509S
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site-directed mutagenesis, mutant C509S, in which the cysteinate bridge C509 might be replaced by a serine oxide, exhibits no detectable methyl transfer activity. Oxygen is a harder donor than sulfide, and the electronic coupling between the cubane and the di-nickel site may differ relative to sulfide. Absence of methyl transfer activity in C509S indicates that an O bridge is not sufficient for this communication
C509V
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site-directed mutagenesis, mutant C509V exhibits no detectable methyl group transfer activity due to it lacking a bridging coordinating atom, Val is more bulky and has greater steric hindrance
D212Ebeta