6.2.1.1: acetate-CoA ligase

This is an abbreviated version!
For detailed information about acetate-CoA ligase, go to the full flat file.

Reaction

Synonyms

ACAS, ACD, AceCS, AceCS1, AceCS2, Acetate thiokinase, Acetate--CoA ligase, acetate:CoA ligase (AMP-forming), Acetic thiokinase, Acetyl activating enzyme, Acetyl CoA ligase, Acetyl CoA synthase, acetyl CoA synthetase, acetyl coenzyme A synthase/carbon monoxide dehydrogenase, Acetyl coenzyme A synthetase, Acetyl-CoA synthase, Acetyl-CoA synthetase, acetyl-CoA synthetase 2, acetyl-CoA synthetase short-chain family member 2, Acetyl-coenzyme A synthase, acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, acetyl-coenzyme A synthetase, ACS, ACS/CODH, ACS1, Acs1p, ACS2, Acs2p, AcsA, acsA1, AcsA2, AcsA3, ACSS2, Acyl-activating enzyme, Acyl-CoA synthetase, adenosine monophosphate-forming acetyl-CoA synthetase, ADP-forming acetyl-CoA synthetase, AF-ACS2, AMP acetyl-coenzyme A synthetase, AMP-Acs, AMP-dependent ACS, AMP-forming acetyl coenzyme A synthetase, AMP-forming acetyl-CoA synthetase, AMP-forming ACS, AMP-forming CoA ligase, carbon monoxide dehydrogenase/acety-coenzyme A synthase, carbon monoxide dehydrogenase/acetyl-CoA synthase, CODH/ACS, More, MT-ACS1, mtCODH/ACS, Mthe_1194, SeAcs, Short chain fatty acyl-CoA synthetase, Short-chain acyl-coenzyme A synthetase, Synthetase, acetyl coenzyme A

ECTree

     6 Ligases

         6.2 Forming carbon-sulfur bonds

             6.2.1 Acid-thiol ligases

                6.2.1.1 acetate-CoA ligase

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Results	in table
11	Activating Compound
37970	AA Sequence
3	Application
1	CAS Registry Number
32	Cloned(Commentary)
29	Cofactor
5	Crystallization (Commentary)
475	Disease/ Diagnostics
4	Expression
23	General Information
9	General Stability
65	Inhibitors
6	kcat/KM [mM/s]
3	Ki Value [mM]
165	KM Value [mM]
36	Localization
75	Metals/Ions
39	Molecular Weight [Da]
60	Natural Substrates/ Products (Substrates)
145	Organism
1	Oxidation Stability
27	Pathway
68	PDB ID
26	pH Optimum
11	pH Range
5	pI Value
7	Posttranslational Modification
74	Protein Variants
35	Purification (Commentary)
4	Reaction
1	Reaction Type
127	Reference
78	Source Tissue
18	Specific Activity [micromol/min/mg]
7	Storage Stability
212	Substrates and Products (Substrate)
47	Subunits
157	Synonyms
1	Systematic Name
18	Temperature Optimum [°C]
4	Temperature Range [°C]
6	Temperature Stability [°C]
73	Turnover Number [1/s]

General Information

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General Information on EC 6.2.1.1 - acetate-CoA ligase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

Moorella thermoacetica

-

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

714724

malfunction

6 entries

metabolism

3 entries

physiological function

12 entries

additional information

Salmonella enterica

-

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

716267

malfunction

Salmonella enterica

-

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

716267

malfunction

Pyrococcus furiosus

-

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)

725872

malfunction

Salmonella enterica

-

cyclic AMP inhibits the activity and promotes the acetylation of acetyl-CoA synthetase through competitive binding to the ATP/AMP pocket. cAMP directly binds to the enzyme and inhibits its activity in a substrate-competitive manner. cAMP binding increases SeAcs acetylation by simultaneously promoting Pat-dependent acetylation and inhibiting CobB-dependent deacetylation, resulting in enhanced SeAcs inhibition

745369

malfunction

Homo sapiens

Q9NR19

decreased isoform ACSS2 expression inhibits renal cell carcinoma cell migration and invasion

744665

malfunction

Mus musculus

-

in adult mice, attenuation of hippocampal isoform ACSS2 expression impairs long-term spatial memory

745887

malfunction

Salmonella enterica G2466

-

cyclic AMP inhibits the activity and promotes the acetylation of acetyl-CoA synthetase through competitive binding to the ATP/AMP pocket. cAMP directly binds to the enzyme and inhibits its activity in a substrate-competitive manner. cAMP binding increases SeAcs acetylation by simultaneously promoting Pat-dependent acetylation and inhibiting CobB-dependent deacetylation, resulting in enhanced SeAcs inhibition

-

metabolism

Moorella thermoacetica

-

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

714240

metabolism

Salmonella enterica

-

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

716267

metabolism

Homo sapiens

Q9NR19

isoform ACSS2 retains acetate to maintain histone acetylation

744656

physiological function

Saccharomyces cerevisiae

-

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

705678

physiological function

Mus musculus

-

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

703038

physiological function

Salmonella enterica

-

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

716267

physiological function

Methanothrix thermoacetophila

A0B8F1

activation of acetate in energy metabolism

726837

physiological function

Saccharomyces cerevisiae

-

acetyl-CoA synthetase 2 is a regulator of autophagy and lifespan

744651

physiological function

Saccharomyces cerevisiae

P52910

enzyme overexpression results in higher resistance to acetic acid as measured by an increased growth rate and shorter lag phase relative to a wild type strain, suggesting that enzyme-mediated consumption of acetic acid during fermentation contributes to acetic acid detoxification

744932

physiological function

Homo sapiens

Q9NR19

enzyme-mediated acetyl-CoA synthesis from acetate is necessary for human cytomegalovirus infection and can compensate for the loss of ATP-citrate lyase

746321

physiological function

Homo sapiens

Q9NR19

isoform ACSS2 is an important factor for promoting renal cell carcinoma development and is essential for cell migration and invasion

744665

physiological function

Mus musculus

-

the enzyme regulates histone acetylation and hippocampal memory

745887

physiological function

Salmonella enterica

-

the high-affinity biosynthetic pathway for converting acetate to acetyl-coenzyme A (acetyl-CoA) is catalyzed by the central metabolic enzyme acetyl-coenzyme A synthetase (Acs), which is finely regulated both at the transcriptional level via cyclic AMP (cAMP)-driven trans-activation and at the post-translational level via acetylation inhibition. The cAMP contact residues are well conserved from prokaryotes to eukaryotes, suggesting a general regulatory mechanism of cAMP on Acs. cAMP generally inhibits other acyl- or aryl-CoA synthetases

745369

physiological function

Salmonella enterica G2466

-

the high-affinity biosynthetic pathway for converting acetate to acetyl-coenzyme A (acetyl-CoA) is catalyzed by the central metabolic enzyme acetyl-coenzyme A synthetase (Acs), which is finely regulated both at the transcriptional level via cyclic AMP (cAMP)-driven trans-activation and at the post-translational level via acetylation inhibition. The cAMP contact residues are well conserved from prokaryotes to eukaryotes, suggesting a general regulatory mechanism of cAMP on Acs. cAMP generally inhibits other acyl- or aryl-CoA synthetases

-

physiological function

Methanothrix thermoacetophila DSM 6194

-

activation of acetate in energy metabolism

-