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ADP + acetate + CoA
AMP + diphosphate + acetyl-CoA
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
-
-
?
ATP + 2-methylvalerate + CoA
AMP + diphosphate + 2-methylvaleryl-CoA
-
-
-
?
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 + acetate + CoA
AMP + diphosphate + acetyl-CoA
ATP + acetate + seleno-CoA
AMP + diphosphate + acetyl-seleno-CoA
-
-
-
?
ATP + acrylate + CoA
AMP + diphosphate + acryloyl-CoA
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
ATP + fluoroacetate + CoA
AMP + diphosphate + fluoroacetyl-CoA
ATP + formate + CoA
AMP + diphosphate + formyl-CoA
-
27% of the activity with acetate
-
?
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
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
-
?
ATP + potassium acetate + CoA
AMP + acetyl-CoA + potassium diphosphate
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
ATP + sodium acetate + CoA
AMP + acetyl-CoA + sodium diphosphate
ATP + tetrapolyphosphate
adenosine 5'-pentaphosphate
-
-
-
?
ATP + tripolyphosphate
adenosine 5'-tetraphosphate
-
-
-
?
ATP + valerate + CoA
AMP + diphosphate + valeryl-CoA
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
-
?
CTP + acetate + CoA
CMP + diphosphate + acetyl-CoA
-
-
-
?
dATP + acetate + CoA
dAMP + diphosphate + acetyl-CoA
GTP + acetate + CoA
GMP + diphosphate + acetyl-CoA
-
-
-
?
UTP + acetate + CoA
UMP + diphosphate + acetyl-CoA
-
-
-
?
additional information
?
-
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

?
-
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
-
highly specific for ATP
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + 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
Amaranthus sp.
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
?
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
-
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 + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
neither glutathione nor pantetheine can substitute for CoA as acyl acceptor
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + 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
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
r
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
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
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
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
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
ATP in form of MgATP2-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
ATP in form of MgATP2-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
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
-
?
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
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
proposed mechanism of the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
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
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + 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
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
specific for acetate, no activity with other short-chain fatty acids
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
?
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
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
r
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
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
-
ir
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
554, 556, 559, 561, 564, 566, 570, 573, 577, 582, 693035, 744651 -
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acrylate + CoA

AMP + diphosphate + acryloyl-CoA
-
-
-
?
ATP + acrylate + CoA
AMP + diphosphate + acryloyl-CoA
-
-
-
?
ATP + acrylate + CoA
AMP + diphosphate + acryloyl-CoA
-
-
-
?
ATP + acrylate + CoA
AMP + diphosphate + acryloyl-CoA
-
-
-
?
ATP + butyrate + CoA

AMP + diphosphate + butyryl-CoA
-
no activity
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
AF-ACS2
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
isobutyrate
-
?
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
-
-
-
?
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 + fluoroacetate + CoA
AMP + diphosphate + fluoroacetyl-CoA
-
-
-
?
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
-
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
-
-
?
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
-
-
-
?
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 + 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
-
-
-
?
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 + sodium acetate + CoA

AMP + acetyl-CoA + sodium diphosphate
-
-
?
ATP + sodium acetate + CoA
AMP + acetyl-CoA + sodium diphosphate
-
-
-
?
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
-
-
?
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
?
-
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
?
-
-
-
-
?
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
-
?
additional information
?
-
-
activity determination in a coupled assay with myokinase, pyruvate kinase, and lactate dehydrogenase: SeAcs first converts acetate, CoA, and ATP to acetyl-CoA and AMP. Then, myokinase converts AMP to ADP. Pyruvate kinase converts ADP and phosphoenolpyruvate to pyruvate and ATP. Finally, lactate dehydrogenase reduces pyruvate and oxidizes NADH to NAD+
-
?
additional information
?
-
-
activity determination in a coupled assay with myokinase, pyruvate kinase, and lactate dehydrogenase: SeAcs first converts acetate, CoA, and ATP to acetyl-CoA and AMP. Then, myokinase converts AMP to ADP. Pyruvate kinase converts ADP and phosphoenolpyruvate to pyruvate and ATP. Finally, lactate dehydrogenase reduces pyruvate and oxidizes NADH to NAD+
-
?
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ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
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
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
?
-
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
-
-
-
?
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
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + 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
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
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
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
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
activation of acetate in energy metabolism
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
activation of acetate in energy metabolism
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
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
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + 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
-
-
?
additional information

?
-
-
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
?
-
-
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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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
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
KCl
-
optimal activity at 1-1.5 M
Li+
-
activation at 5-8 mM, absolute requirement for certain monovalent cations, inhibition above 10 mM
Ni
-
nickel-containing bimetallic site, the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase
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+

-
about 70% of the activation with Mg2+ or Mn2+, AF-ACS2
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+
-
Km for CaCl2 is 1.2 mM
Ca2+
-
can replace Mg2+ in activation, with 50% of the efficiency relative to MgCl2
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+

-
about 70% of the activation with Mg2+ or Mn2+, AF-ACS2
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+

-
required
Mg2+
-
inhibition above 7 mM
Mg2+
-
AF-ACS2 shows strong preference for Mg2+ and Mn2+ as the divalent metal
Mg2+
-
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
Mg2+
-
Km for MgCl2 is 0.3 mM
Mg2+
-
optimal concentration: 5 mM in presence of 1.25 mM NaCl
Mg2+
strong preference for Mg2+ and Mn2+ as the divalent metal
Mg2+
-
MgATP2- is the actual substrate
Mn2+

-
5 mM, 94% of the activation relative to Mg2+
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+
-
can replace Mg2+ in activation
Mn2+
-
Km for MnCl2 is 0.5 mM
Mn2+
strong preference for Mg2+ and Mn2+ as the divalent metal
Mn2+
-
can replace Mg2+ in activation
Mn2+
-
64% of the activation relative to Mg2+
Mn2+
-
10 mM, 90% of the activation relative to Mg2+
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
NH4+
-
increases the activity by 30% at 5 mM and 70% at 20 mM
Ni2+

-
about 35% of the activation with Mg2+ or Mn2+, AF-ACS2
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+
-
Mƶssbauer 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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29.2
2-methylvalerate
-
65°C, mutant enzyme W416G
7.6
4-methylvalerate
-
65°C, mutant enzyme W416G
10.2
Heptanoate
-
65°C, mutant enzyme W416G
6.1
hexanoate
-
65°C, mutant enzyme W416G
18.1
Octanoate
-
65°C, mutant enzyme W416G
3.59
potassium acetate
at pH 8.0 and 37°C
0.25 - 4.66
Sodium acetate
4.7
tripolyphosphate
-
synthesis of adenosine 5Ā“-tetraphosphate
11.1
valerate
-
65°C, mutant enzyme W416G
additional information
additional information
-
0.04
acetate

-
-
0.14
acetate
-
pH 6.7, 200 mM K+
0.22
acetate
-
CoA, in Tris buffer, pH 8.3, 200 mM K+
0.4
acetate
pH 7.5, 55°C
0.625
acetate
-
pH 7.5, 55°C, wild-type enzyme
1.4
acetate
pH 7.0, 65°C, mutant enzyme G501A
2.1
acetate
pH 7.0, 65°C, mutant enzyme A500T
2.9
acetate
-
isoform Acs3, at pH 7.7 and 37°C
3
acetate
pH 7.0, 65°C, mutant enzyme T499A
3.3
acetate
-
isoform Acs2, at pH 7.7 and 37°C
3.5
acetate
-
65°C, wild-type enzyme
3.5
acetate
pH 7.0, 65°C, wild-type enzyme
4 - 10
acetate
-
mutant L641P, pH not specified in the publication, temperature not specified in the publication
4.5
acetate
-
isoform Acs1, at pH 7.7 and 37°C
7.5
acetate
pH 7.0, 65°C, mutant enzyme Y498A
13.2
acetate
-
65°C, mutant enzyme V388A
24.6
acetate
-
65°C, mutant enzyme I312A
41
acetate
-
wild-type Acs, pH not specified in the publication, temperature not specified in the publication
132.1
acetate
-
65°C, mutant enzyme W416G
164.4
acetate
-
65°C, mutant enzyme V388G
596
acetate
-
65°C, mutant enzyme T313K
11000
acetate
-
mutant G266S, pH not specified in the publication, temperature not specified in the publication
0.0037
acetyl-CoA

-
pH 7.5, 80°C, wild-type alpha-subunit
0.0039
acetyl-CoA
-
pH 7.5, 55°C, wild-type enzyme
0.0042
acetyl-CoA
-
pH 7.5, 80°C, wild-type enzyme
0.026
acetyl-CoA
-
pH 8.0
5.26
Acrylate

-
-
0.093
ADP

-
pH 7.5, 55°C, wild-type enzyme
0.017
ATP

-
in Tris buffer, pH 6.7, 200 mM K+
0.0224
ATP
-
pH 7.5, mutant enzyme R526A
0.0238
ATP
-
pH 7.5, mutant enzyme A357V
0.0265
ATP
-
pH 7.5, mutant enzyme R584E
0.0287
ATP
-
pH 7.5, mutant enzyme R194A
0.0373
ATP
-
pH 7.5, mutant enzyme R194E
0.0381
ATP
-
pH 7.5, mutant enzyme R584A
0.044
ATP
-
pH 7.5, mutant enzyme D517P
0.0638
ATP
-
pH 7.5, mutant enzyme G524S
0.0771
ATP
-
pH 7.5, wild-type enzyme
0.1
ATP
-
in Pipes buffer, pH 6.7, 200 mM K+
0.16
ATP
-
synthesis of adenosine 5Ā“-tetraphosphate
0.221
ATP
-
pH 7.5, 55°C, wild-type enzyme
0.243
ATP
-
pH 7.5, mutant enzyme D517G
0.35
ATP
-
Tris buffer, pH 8.3, 200 mM K+
0.65
ATP
-
65°C, mutant enzyme T313V
1.7
ATP
pH 7.0, 65°C, mutant enzyme G501A
1.7
ATP
pH 7.0, 65°C, mutant enzyme T499A
1.7
ATP
pH 7.0, 65°C, mutant enzyme Y498A
2.3
ATP
-
65°C, mutant enzyme W416G
2.6
ATP
-
65°C, mutant enzyme V388A
3.3
ATP
-
65°C, wild-type enzyme
3.3
ATP
pH 7.0, 65°C, wild-type enzyme
3.4
ATP
-
65°C, mutant enzyme T313K
3.6
ATP
pH 7.0, 65°C, mutant enzyme A500T
4
ATP
-
65°C, mutant enzyme V388G
6.6
ATP
-
65°C, mutant enzyme I312A
0.46
Butyrate

-
65°C, mutant enzyme T313V
39.2
Butyrate
-
65°C, mutant enzyme W416G
151.9
Butyrate
-
65°C, mutant enzyme V388A
0.011
CoA

-
0.0139
CoA
-
pH 7.5, 55°C, wild-type enzyme
0.05
CoA
-
value above 0.05 mM
0.05
CoA
-
pH 7.5, wild-type enzyme
0.08
CoA
pH 7.0, 65°C, mutant enzyme G501A
0.1
CoA
pH 7.0, 65°C, mutant enzyme Y498A
0.1072
CoA
-
pH 7.5, mutant enzyme R194E
0.133
CoA
-
pH 7.5, mutant enzyme A357V
0.1417
CoA
-
pH 7.5, mutant enzyme R194A
0.18
CoA
-
65°C, mutant enzyme I312A
0.18
CoA
-
65°C, mutant enzyme V388G
0.19
CoA
-
65°C, wild-type enzyme
0.19
CoA
pH 7.0, 65°C, wild-type enzyme
0.205
CoA
-
pH 7.5, mutant enzyme R526A
0.228
CoA
-
pH 7.5, mutant enzyme D517G
0.24
CoA
pH 7.0, 65°C, mutant enzyme T499A
0.28
CoA
-
in Tris buffer, pH 6.7, 200 mM K+
0.35
CoA
-
65°C, mutant enzyme V388A
0.3583
CoA
-
pH 7.5, mutant enzyme R584A
0.426
CoA
-
pH 7.5, mutant enzyme R584E
0.43
CoA
-
65°C, mutant enzyme W416G
0.448
CoA
-
pH 7.5, mutant enzyme G524S
0.5 - 1
CoA
pH 7.0, 65°C, mutant enzyme A500T
0.527
CoA
-
pH 7.5, mutant enzyme D517P
0.7
CoA
-
65°C, mutant enzyme T313V
1.2
CoA
-
in Pipes buffer, pH 6.7, 200 mM K+
0.23
phosphate

-
pH 7.5, 80°C, wild-type enzyme
0.272
phosphate
-
pH 7.5, 55°C, wild-type enzyme
3.1
propanoate

-
-
3.9
propionate

-
AF-ACS2
4.1
propionate
-
65°C, mutant enzyme V388A
4.5
propionate
-
65°C, mutant enzyme T313V
36.5
propionate
-
65°C, wild-type enzyme
128.6
propionate
-
65°C, mutant enzyme V388G
188.8
propionate
-
65°C, mutant enzyme W416G
0.25
Sodium acetate

-
isoform ACS1, at pH 7.8 and 25°C
0.72
Sodium acetate
-
isoform ACS2, at pH 7.8 and 25°C
4.66
Sodium acetate
at pH 8.0 and 37°C
additional information
additional information

-
-
-
additional information
additional information
-
kinetic parameters of wild type and mutant enzymes at 55°C, overview
-
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
-
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