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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

Engineering

Engineering on EC 6.2.1.1 - acetate-CoA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A498A
alteration does not significantly affect the Km for any substrate but reduces the turnover rate kcat 41fold
A500T
kcat value decreases 44fold
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
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
G266S
G524L
G524S
-
kcat/Km for ATP is 1.6fold lower than wild-type value, kcat/Km for CoA is 19fold lower than wild-type value
K609A
L641P
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
additional information