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6.2.1.13: acetate-CoA ligase (ADP-forming)

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

Word Map on EC 6.2.1.13

Reaction

ATP
+
acetate
 +
CoA
=
ADP
 +
phosphate
 +
acetyl-CoA

Synonyms

ACD, acetate:CoA ligase [ADP-forming], acetate:coenzyme A ligase (ADP-forming), Acetyl-CoA synthetase, Acetyl-CoA synthetase (ADP-forming), acetyl-coenzyme A synthetase, acetyl-coenzyme A synthetase (ADP-forming), ACS, ACS III, ACS1, ACS2, ADP acetyl-coenzyme A synthetase, ADP-ACS, ADP-forming acetyl-CoA synthetase, ADP-forming acetyl-CoA synthetase isoenzyme I, ADP-forming acetyl-coenzyme A synthetase, ADP-forming acyl coenzyme A synthetase, ADP-forming acyl-CoA synthetase, EhACD, PF1540, PF1787, Synthetase, acetyl coenzyme A (adenosine diphosphate-forming), TK0944/TK0943 protein

ECTree

     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.13 acetate-CoA ligase (ADP-forming)

Engineering

Engineering on EC 6.2.1.13 - acetate-CoA ligase (ADP-forming)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D674A
D674E
the variant retains about 45% activity compared to wild type enzyme
D674N
the variant retains about 1% activity compared to wild type enzyme
E213A
E213D
the variant retains about 1% activity compared to wild type enzyme
E213Q
the variant retains about 1% activity compared to wild type enzyme
E218A
site-directed mutagenesis, the mutant variant is not phosphorylated by acetyl-CoA and phosphate
H252A
H533D
the variant retains about 3% activity compared to wild type enzyme
H533E
the variant retains about 1% activity compared to wild type enzyme
H533K
the variant retains about 10% activity compared to wild type enzyme
H533N
the variant retains about 5% activity compared to wild type enzyme
H533Q
the variant retains about 5% activity compared to wild type enzyme
H533R
D212betaE
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 2-4% of the wild-type activity, phosphorylation of the mutant is reduced
E218alphaD
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 1-10% of the wild-type activity, phopshorylation of the mutant is reduced
E218alphaQ
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, phopshorylation of the mutant is reduced
E218Dalpha
1-10% of wild-type activity
H257alphaD
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is not phosphorylated at both the alpha- and beta-subunit
H257Dalpha
mutant shows no activity in either direction
H71betaA
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is impaired in phosphorylation of the beta subunit
G266S
-
the Acs mutant does not cause growth arrest in contrast to the wild-type enzyme
additional information