Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.2.1.1 extracted from

  • Chan, C.; Garrity, J.; Crosby, H.; Escalante-Semerena, J.
    In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate (2011), Mol. Microbiol., 80, 168-183.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
G266S random mutagenesis, mutant Km for acetate is 268fold higher than that of the AcsWT enzyme, while kcat is 3fold reduced Salmonella enterica
G266S the Acs mutant does not cause growth arrest in contrast to the wild-type enzyme Salmonella enterica
K609A random mutagenesis Salmonella enterica
L641P random mutagenesis, mutant Km for acetate is higher than that of the AcsWT enzyme, while kcat is reduced Salmonella enterica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4 10 acetate mutant L641P, pH not specified in the publication, temperature not specified in the publication Salmonella enterica
41
-
acetate wild-type Acs, pH not specified in the publication, temperature not specified in the publication Salmonella enterica
11000
-
acetate mutant G266S, pH not specified in the publication, temperature not specified in the publication Salmonella enterica

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Salmonella enterica 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + acetate + CoA Salmonella enterica
-
AMP + diphosphate + acetyl-CoA
-
?

Organism

Organism UniProt Comment Textmining
Salmonella enterica
-
gene acs, different strains
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate + CoA
-
Salmonella enterica AMP + diphosphate + acetyl-CoA
-
?

Synonyms

Synonyms Comment Organism
acetyl-coenzyme A synthetase
-
Salmonella enterica
ACS
-
Salmonella enterica
More Acs is a member of the broadly distributed AMP-forming acyl-CoA synthetase family of enzymes Salmonella enterica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1500
-
acetate mutant L641P, pH not specified in the publication, temperature not specified in the publication Salmonella enterica
3200
-
acetate mutant G266S, pH not specified in the publication, temperature not specified in the publication Salmonella enterica
9400
-
acetate wild-type Acs, pH not specified in the publication, temperature not specified in the publication Salmonella enterica

Cofactor

Cofactor Comment Organism Structure
ATP
-
Salmonella enterica

General Information

General Information Comment Organism
malfunction growth on 10 mM acetate causes an acs+ induction in a Salmonella enterica strain, that cannot acetylate, i.e. inactivate Acs, leads to growth arrest, a condition that correlates with a drop in energy charge in the acetylation-deficient strain, relative to the energy charge in the acetylation-proficient strain. Acs-dependent depletion of ATP, coupled with the rise in AMP levels, prevents the synthesis of ADP needed to replenish the pool of ATP Salmonella enterica
metabolism activation of weak organic acids by acyl-CoA synthetases is costly to cells, since it requires 2 mol of ATP per mol of substrate; 1 mol of ATP is consumed to activate the organic acid, while the second mol of ATP is needed to convert AMP to ADP, the immediate precursor of ATP. Further loss of energy resources during the course of the Acs reaction is caused by the hydrolysis of diphosphate to monophosphate through pyrophosphate phosphohydrolase, EC 3.6.1.1 Salmonella enterica
additional information growth arrest is caused by elevated Acs activity, while overproduction of ADP-forming Ac-CoA synthesizing systems, EC 6.2.1.13, do not affect the growth behaviour of acetylation-deficient or acetylation-proficient strains, effects of Acs on growth of different strains, also sirtuin-dependent protein acylation/deacylation system-defective strains, overview. Increased CoA biosynthesis partially alleviates the negative effect caused by high Acs activity, regulation, overview Salmonella enterica
physiological function 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 Salmonella enterica

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.29
-
acetate mutant G266S, pH not specified in the publication, temperature not specified in the publication Salmonella enterica
3.6
-
acetate mutant L641P, pH not specified in the publication, temperature not specified in the publication Salmonella enterica
229
-
acetate wild-type Acs, pH not specified in the publication, temperature not specified in the publication Salmonella enterica