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
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6.2.1.1
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synthetases
-
peroxisomal
-
palmitate
-
acyltransferase
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cholesterol
-
phospholipid
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triglyceride
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beta-oxidation
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citrate
-
arachidonic
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carnitine
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medium-chain
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triacylglycerols
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triacsin
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palmitoyl-coa
-
oleic
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lipogenesis
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glyoxylate
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6.2.1.3
-
oleate
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acsls
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hypolipidemic
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codhs
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acetogenic
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propionyl-coa
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fadd
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phosphotransacetylase
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wood-ljungdahl
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atp-citrate
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oleoyl-coa
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glucose-limited
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arachnoid
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sn-glycerol-3-phosphate
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coash
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moorella
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1-14cacetate
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corrinoid
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fatps
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thermoaceticum
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arachidonoyl-coa
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acetoacetyl-coa
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very-long-chain
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adrenoleukodystrophy
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reacylation
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vlcfas
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extradural
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butyryl-coa
-
alpha2beta2
-
myristoyl-coa
-
acaca
-
medicine
-
analysis
- 6.2.1.1
- synthetases
- peroxisomal
- palmitate
- acyltransferase
- cholesterol
- phospholipid
- triglyceride
-
beta-oxidation
- citrate
-
arachidonic
- carnitine
-
medium-chain
- triacylglycerols
- triacsin
- palmitoyl-coa
-
oleic
-
lipogenesis
- glyoxylate
-
6.2.1.3
- oleate
-
acsls
-
hypolipidemic
-
codhs
-
acetogenic
- propionyl-coa
- fadd
- phosphotransacetylase
-
wood-ljungdahl
-
atp-citrate
- oleoyl-coa
-
glucose-limited
-
arachnoid
- sn-glycerol-3-phosphate
- coash
-
moorella
-
1-14cacetate
- corrinoid
-
fatps
- thermoaceticum
- arachidonoyl-coa
- acetoacetyl-coa
-
very-long-chain
- adrenoleukodystrophy
-
reacylation
-
vlcfas
-
extradural
- butyryl-coa
-
alpha2beta2
- myristoyl-coa
- acaca
- medicine
- analysis
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
6.2.1.1 acetate-CoA ligaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 6.2.1.1 - acetate-CoA ligase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
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
Co2+
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
Fe2+
K+
Li+
-
activation at 5-8 mM, absolute requirement for certain monovalent cations, inhibition above 10 mM
Mg2+
Mn2+
Na+
NH4+
Ni
-
nickel-containing bimetallic site, the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase
Ni2+
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+
-
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+
-
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+
-
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+
-
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+
strong preference for Mg2+ and Mn2+ as the divalent metal
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+
strong preference for Mg2+ and Mn2+ as the divalent metal
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
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
