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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.

Word Map on EC 6.2.1.1

Reaction

ATP
+
acetate
 +
CoA
=
AMP
 +
diphosphate
 +
acetyl-CoA

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

Inhibitors

Inhibitors on EC 6.2.1.1 - acetate-CoA ligase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
3'-Dephospho-CoASH analogues with a phosphodiester bond
-
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetyl-CoA
-
competitive to CoASH
adenylate
-
-
ADP
-
competitive to ATP
Allicin
bicarbonate
-
-
Butyrate
-
propanoate-CoA formation
cAMP
-
cyclic AMP inhibits the activity and promotes the acetylation of acetyl-CoA synthetase through competitive binding to the highly conserved ATP/AMP binding pocket and restrains SeAcs in an open conformation. 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
CO
-
CO inhibits acetyl-CoA synthesis quite strongly and in a cooperative manner
dicarbonic acid diethyl ester
-
-
diphosphate
erythrose 4-phosphate
-
-
glyceraldehyde 3-phosphate
-
weak
glycerol
glyoxylate
-
-
long-chain acyl-CoA compounds
monovalent cations
-
at 200 mM
-
NaCl
-
concentration of 5-20 mM decrease the activity 20-25%
Ni
-
the authors favor a mechanism in which methylation occurs first to Ni(p0 -) or Ni(pI -)[Fe4S4]+, followed by coordination of CO to form Ni(pII)(CO)(CH3) which breaks one of the S(Nid) bonds (forming the bis square planar Ni(II) species, as if the Ni(d)N2S2 unit were acting as a biological pseudodiphosphine, mimicking behavior common to a bidentate phosphine). The CO-insertion/CH3-migration occurs on one metal forming the trigonal planar Ni(pII)-acetyl intermediate. Finally, addition of thiolate produces the thioester. The authors disfavor the unprecedented bimetallic, CO-insertion/CH3-migration mechanism (both in its diamagnetic and paramagnetic guise) and disfavors CO, CH3+, or thiolate (CoA) binding to the distal Ni. Finally, Ni in the proximal site produces a better catalyst than does Cu
Nonidet P40
-
weak
O2
-
the enzyme is O2-sensitive
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
inhibition is reversible by either CoA or mercaptoethanol
P1,P5-di(adenosine-5)pentaphosphate
-
inhibits ADP formation
palmitoyl-CoA
propanoate
-
butyryl-CoA formation
pyridoxal 5'-phosphate
-
-
seleno-CoA
-
competitive to CoA
Short-chain CoA esters
-
-
-
sorbitol
sucrose
Tween 100
-
-
-
Xylulose 5-phosphate
-
-
additional information
-