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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
-
-
-
-
?
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
-
-
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
-
-
-
-
?
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 + 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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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+
-
10 mM, can replace Mg2+ in activation, with 30% of the efficiency relative to Mg2+
Ca2+
about 30% of the activation with Mg2+ or Mn2+
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+
-
10 mM, 90% of the activation relative to Mg2+
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, 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+
-
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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A498A
alteration does not significantly affect the Km for any substrate but reduces the turnover rate kcat 41fold
A500T
kcat value decreases 44fold
D502A
inactive mutant enzyme
D502E
inactive mutant enzyme
D502N
inactive mutant enzyme
G501A
two- to threefold reduced Km values for acetate, ATP and CoA. The turnover rate is over 200fold reduced
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
T313K
-
Km for acetate is 170fold higher than wild-type value, kcat for acetate is 34fold lower than wild-type value
T313V
-
kcat/Km for acetate is 2.5fold lower than wild-type value, kcat/Km for propionate is identical to wild-type value
T499A
kcat value decreases 83fold
V388A
-
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
-
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
Y498F
inactive mutant enzyme
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
-
T313K
-
Km for acetate is 170fold higher than wild-type value, kcat for acetate is 34fold lower than wild-type value
-
T313V
-
kcat/Km for acetate is 2.5fold lower than wild-type value, kcat/Km for propionate is identical to wild-type value
-
V388A
-
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
-
A110C
-
site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme
A222L
-
site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme
A265M
-
site-directed mutagenesis, alpha-subunit mutant, the recombinantly expressed mutant enzymes cannot be purified
C509A
-
site-directe mutagenesis, mutant C509A shows a significantly diminished methyl transfer activity compared to the wild-type enzyme
C509H
-
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
-
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
-
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
-
site-directed mutagenesis, the mutant shows 2-4% of wild-type activity, slightly impaired in arsenolysis
D212Nbeta
-
site-directed mutagenesis, the mutant shows highly reduced phosphorylation/phosphorolysis activity, but only slightly impaired in arsenolysis
E218Qalpha
-
site-directed mutagenesis, inactive mutant
H257Dalpha
-
site-directed mutagenesis, inactive mutant
H71Abeta
-
site-directed mutagenesis, inactive mutant concerning phosphorylation/phosphorolysis, slightly impaired in arsenolysis
K615Q
-
the mutant of isoform Acs3 retains 10% of wild type activity
K615R
-
the mutant of isoform Acs3 retains 10% of wild type activity
K620Q
-
the mutant of isoform Acs1 retains 10% of wild type activity
K620R
-
the mutant of isoform Acs1 retains 10% of wild type activity
K615Q
-
the mutant of isoform Acs3 retains 10% of wild type activity
-
K615R
-
the mutant of isoform Acs3 retains 10% of wild type activity
-
K620Q
-
the mutant of isoform Acs1 retains 10% of wild type activity
-
K620R
-
the mutant of isoform Acs1 retains 10% of wild type activity
-
A357V
-
kcat/Km for ATP is 1.2fold higher than wild-type value, kcat/Km for CoA is 3.2fold lower than wild-type value
D411A
-
site-directed mutagenesis, the mutant SeAcs variant shows a nearly 10fold increased dissociation constant compared to the wild-type enzyme
D500A
-
site-directed mutagenesis, the mutant SeAcs variant is defective in cAMP binding
D517G
-
kcat/Km for ATP is 6.5fold lower than wild-type value, kcat/Km for CoA is 9.5fold lower than wild-type value
D517P
-
kcat/Km for ATP is 1.4fold lower than wild-type value, kcat/Km for CoA is 23.7fold lower than wild-type value
G524S
-
kcat/Km for ATP is 1.6fold lower than wild-type value, kcat/Km for CoA is 19fold lower than wild-type value
N521A
-
site-directed mutagenesis, the mutant SeAcs variant shows a higher dissociation constant compared to the wild-type enzyme
Q415A
-
site-directed mutagenesis, the mutant SeAcs variant is defective in cAMP binding
R194A
-
kcat/Km for ATP is 1.1fold higher than wild-type value, kcat/Km for CoA is 6.3fold lower than wild-type value
R194E
-
kcat/Km for ATP is 1.2fold lower than wild-type value, kcat/Km for CoA is 4.75fold lower than wild-type value
R515A
-
site-directed mutagenesis, the mutant SeAcs variant shows a nearly 10fold increased dissociation constant compared to the wild-type enzyme
R526A
-
kcat/Km for ATP is 1.2fold higher than wild-type value, kcat/Km for CoA is 9.5fold lower than wild-type value
R584A
-
kcat/Km for ATP is 1.2 fold than wild-type value, kcat/Km for CoA is 19fold lower than wild-type value
R584E
-
kcat/Km for ATP is 1.1fold higher than wild-type value, kcat/Km for CoA is 21fold lower than wild-type value
T416A
-
site-directed mutagenesis, the mutant SeAcs variant shows a higher dissociation constant compared to the wild-type enzyme
W413A
-
site-directed mutagenesis, the mutant SeAcs variant is defective in cAMP binding
D411A
-
site-directed mutagenesis, the mutant SeAcs variant shows a nearly 10fold increased dissociation constant compared to the wild-type enzyme
-
D500A
-
site-directed mutagenesis, the mutant SeAcs variant is defective in cAMP binding
-
T416A
-
site-directed mutagenesis, the mutant SeAcs variant shows a higher dissociation constant compared to the wild-type enzyme
-
W413A
-
site-directed mutagenesis, the mutant SeAcs variant is defective in cAMP binding
-
S608T
-
when mutant enzyme S608T is acetylated, it loses about 80% activity compared to the wild type
G266S
-
random mutagenesis, mutant Km for acetate is 268fold higher than that of the AcsWT enzyme, while kcat is 3fold reduced
G266S
-
the Acs mutant does not cause growth arrest in contrast to the wild-type enzyme
G524L
-
inactive mutant enzyme
G524L
-
mutant enzyme is unable to catalyze the complete reaction yet catalyzes the adenylation half-reaction with activity comparable to the wild-type enzyme
K609A
-
random mutagenesis
K609A
-
inactive mutant enzyme
K609A
-
mutation results in an enzyme that is unable to catalyze the adenylate reaction
L641P
-
mutation at Leu641 prevents the acetylation of Acs by protein acetyltransferase and maintains the acetyl-coenzyme A synthetase in its active state
L641P
-
random mutagenesis, mutant Km for acetate is higher than that of the AcsWT enzyme, while kcat is reduced
additional information
-
the acs mutant of Vibrio fischeri is unable to utilize acetate and has a competitive defect when colonizing the squid, indicating the importance of proper control of acetate metabolism in the light of organ symbiosis, acs mutants are not hypermotile
additional information
a constructed acs1 knockout mutant has a disruption in the plastidic acetyl-CoA synthetase gene leading to 90% decreased ACS activity and largely blocked incorporation of exogenous 14C-acetate and 14C-ethanol into fatty acids. Whereas the disruption has no significant effect on the synthesis of bulk seed triacylglycerols, the acs1 plants are smaller and flowered later. The acs1 mutant shows increased sensitivity to exogenous acetate, ethanol, and acetaldehyde compared to wild-type plants, phenotype, overview
additional information
-
all mutations in the alpha-subunit have dramatic effects on arsenolysis activity, while mutations in the beta-subunit cause only moderate loss of activity
additional information
-
cAMP has no effect on acetylation promotion of the mutant SeAcs enzymes
additional information
-
cAMP has no effect on acetylation promotion of the mutant SeAcs enzymes
-
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Patel, S.S.; Walt, D.R.
Substrate specificity of acetyl coenzyme A synthetase
J. Biol. Chem.
262
7132-7134
1987
Saccharomyces cerevisiae
brenda
Connerton, I.F.; Fincham, J.R.; Sandeman, R.A.; Hynes, U.K.
Comparison and cross-species expression of the acetyl-CoA synthetase genes of the Ascomycete fungi, Aspergillus nidulans and Neurospora crassa
Mol. Microbiol.
4
451-460
1990
Aspergillus nidulans, Neurospora crassa
brenda
Kohler, H.P.; Zehnder, A.J.B.
Carbon monoxide dehydrogenase and acetate thiokinase in Methanothrix soehngenii
FEMS Microbiol. Lett.
21
287-292
1984
Methanothrix soehngenii
-
brenda
Maruyama, K.
Short-chain acyl-coenzyme A synthetase in Rhodopseudomonas sphaeroides
J. Biochem.
91
725-730
1982
Cereibacter sphaeroides
brenda
Frenkel, E.P.; Kitchens, R.L.
Acetyl-CoA synthetase from bakers yeast (Saccharomyces cerevisiae)
Methods Enzymol.
71
317-324
1981
Saccharomyces cerevisiae
brenda
Oberlies, G.; Fuchs, G.; Thauer, R.K.
Acetate thiokinase and the assimilation of acetate in Methanobacterium thermoautotrophicum
Arch. Microbiol.
128
248-252
1980
Methanothermobacter thermautotrophicus
brenda
Satyanarayana, T.; Chervenka, C.H.; Klein, H.P.
Subunit specificity of the two acetyl-CoA synthetases of yeast as revealed by an immunological approach
Biochim. Biophys. Acta
614
601-606
1980
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
brenda
Scaife, J.R.; Tichivangana, J.Z.
Short chain acyl-CoA synthetase in ovine rumen epithelium
Biochim. Biophys. Acta
619
445-450
1980
Ovis aries
brenda
Woodnutt, G.; Parker, D.S.
Rabbit liver acetyl-CoA synthetase
Biochem. J.
175
757-759
1978
Oryctolagus cuniculus
brenda
Frenkel, E.P.; Kitchens, R.L.
Purification and properties of acetyl coenzyme A synthetase from bakers yeast
J. Biol. Chem.
252
504-507
1977
Saccharomyces cerevisiae
brenda
O'Sullivan, J.; Ettlinger, L.
Characterization of the acetyl-CoA synthetase of Acetobacter aceti
Biochim. Biophys. Acta
450
410-417
1976
Acetobacter aceti
brenda
Satyanarayana, T.; Klein, H.P.
Studies on the aerobic acetyl-coenzyme A synthetase of Saccharomyces cerevisiae: purification, crystallization, and physical properties of the enzyme
Arch. Biochem. Biophys.
174
480-490
1976
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
brenda
Reijnierse, G.L.A.; Veldstra, H.; Van den Berg, C.J.
Short-chain fatty acid synthesis in brain. Subcellular localization and changes during development
Biochem. J.
152
477-484
1975
Rattus norvegicus
brenda
Londesborough, J.C.; Webster, L.T.
Fatty acyl-CoA synthetases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
10
469-488
1974
Aspergillus niger, Bos taurus, Euglena gracilis, Oryctolagus cuniculus, Rattus norvegicus
-
brenda
Satyanarayana, T.; Mandel, A.D.; Klein, H.P.
Evidence for two immunologically distinct acetyl-coenzyme A synthetases in yeast
Biochim. Biophys. Acta
341
396-401
1974
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
brenda
Young, O.A.; Anderson, J.W.
The enzymology of short-chain fatty acyl-coenzyme A synthetase from seed of Pinus radiata
Biochem. J.
137
435-442
1974
Pinus radiata
brenda
Satyanarayana, T.; Klein, H.P.
Studies on acetyl-coenzyme A synthetase of yeast: inhibition by long-chain acyl-coenzyme A esters
J. Bacteriol.
115
600-606
1973
Saccharomyces cerevisiae, Saccharomyces cerevisiae LK2G12
brenda
Londesborough, J.L.; Yuan, S.L.; Webster, L.T.
The molecular weight and thiol residues of acetyl-coenzyme A synthetase from ox heart mitochondria
Biochem. J.
133
23-36
1973
Bos taurus
brenda
Preston, G.G.; Wall, J.D.; Emerich, D.W.
Purification and properties of acetyl-CoA synthetase from Bradyrhizobium japonicum bacteroids
Biochem. J.
267
179-183
1990
Bradyrhizobium japonicum
brenda
Jetten, M.S.M.; Stams, A.J.M.; Zehnder, A.J.B.
Isolation and characterization of acetyl-coenzyme A synthetase from Methanothrix soehngenii
J. Bacteriol.
171
5430-5435
1989
Methanothrix soehngenii
brenda
Focke, M.; Feld, A.; Lichtenthaler, H.K.
Allicin, a naturally occuring antibiotic from garlic, specifically inhibits acetyl-CoA synthetase
FEBS Lett.
261
106-108
1990
Bos taurus, Saccharomyces cerevisiae, Hordeum vulgare
brenda
Khramtsov, N.V.; Blunt, D.S.; Montelone, B.A.; Upton, S.J.
The putative acetyl-CoA synthetase gene of Cryptosporidium parvum and a new conserved protein motif in acetyl-CoA synthetases
J. Parasitol.
82
423-427
1996
Cryptosporidium parvum
brenda
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