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
-
6.2.1.13
-
archaea
-
saethre-chotzen
-
amitochondriate
-
hyperthermophilic
-
cranial
-
protist
-
entamoeba
-
giardia
-
histolytica
-
acrocephalosyndactyly
-
amp-forming
-
pyrococcus
-
furiosus
-
succinyl-coa
-
skull
-
propionyl-coa
-
lamblia
-
pyruvate:ferredoxin
-
sutures
-
archaeoglobus
-
archaebacteria
-
phosphotransacetylase
-
acetate-forming
-
ppi-dependent
-
syndactyly
-
embden-meyerhof
- 6.2.1.13
- archaea
-
saethre-chotzen
-
amitochondriate
-
hyperthermophilic
-
cranial
-
protist
-
entamoeba
- giardia
- histolytica
-
acrocephalosyndactyly
-
amp-forming
- pyrococcus
- furiosus
- succinyl-coa
-
skull
- propionyl-coa
- lamblia
-
pyruvate:ferredoxin
-
sutures
- archaeoglobus
- archaebacteria
- phosphotransacetylase
-
acetate-forming
-
ppi-dependent
-
syndactyly
-
embden-meyerhof
Reaction
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
Advanced search results
KCat KM Value
KCat KM Value on EC 6.2.1.13 - acetate-CoA ligase (ADP-forming)
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0.59
mutant enzyme H533D, pH and temperature not specified in the publication
0.67
acetate
mutant enzyme H533E, pH and temperature not specified in the publication
1.9
acetate
mutant enzyme H533N, pH and temperature not specified in the publication
2.2
acetate
mutant enzyme H533Q, pH and temperature not specified in the publication
3.3
acetate
mutant enzyme H533R, pH and temperature not specified in the publication
4.1
acetate
mutant enzyme H533K, pH and temperature not specified in the publication
4.8
acetate
mutant enzyme H533A, pH and temperature not specified in the publication
16
acetate
wild type enzyme, pH and temperature not specified in the publication
0.06
mutant enzyme H533D, pH and temperature not specified in the publication
0.09
acetyl-CoA
mutant enzyme H533Q, pH and temperature not specified in the publication
10
acetyl-CoA
mutant enzyme H533E, pH and temperature not specified in the publication
79
acetyl-CoA
mutant enzyme H533K, pH and temperature not specified in the publication
92
acetyl-CoA
mutant enzyme H533N, pH and temperature not specified in the publication
266
acetyl-CoA
mutant enzyme H533A, pH and temperature not specified in the publication
1115
acetyl-CoA
mutant enzyme H533R, pH and temperature not specified in the publication
2600
acetyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.2
mutant enzyme H533E, pH and temperature not specified in the publication
1.9
ADP
mutant enzyme H533Q, pH and temperature not specified in the publication
2.5
ADP
mutant enzyme H533N, pH and temperature not specified in the publication
2.9
ADP
mutant enzyme H533D, pH and temperature not specified in the publication
3.4
ADP
mutant enzyme H533K, pH and temperature not specified in the publication
6.9
ADP
mutant enzyme H533A, pH and temperature not specified in the publication
32
ADP
mutant enzyme H533R, pH and temperature not specified in the publication
89
ADP
wild type enzyme, pH and temperature not specified in the publication
0.07
mutant enzyme H533E, pH and temperature not specified in the publication
0.21
ATP
mutant enzyme H533D, pH and temperature not specified in the publication
0.26
ATP
mutant enzyme H533N, pH and temperature not specified in the publication
1.6
ATP
mutant enzyme H533A, pH and temperature not specified in the publication
2.4
ATP
mutant enzyme H533K, pH and temperature not specified in the publication
2.7
ATP
mutant enzyme H533R, pH and temperature not specified in the publication
27
ATP
wild type enzyme, pH and temperature not specified in the publication
116
ATP
mutant enzyme H533Q, pH and temperature not specified in the publication
0.57
mutant enzyme H533Q, pH and temperature not specified in the publication
1.1
CoA
mutant enzyme H533E, pH and temperature not specified in the publication
23
CoA
mutant enzyme H533D, pH and temperature not specified in the publication
26
CoA
mutant enzyme H533N, pH and temperature not specified in the publication
60
CoA
mutant enzyme H533A, pH and temperature not specified in the publication
70
CoA
mutant enzyme H533R, pH and temperature not specified in the publication
287
CoA
mutant enzyme H533K, pH and temperature not specified in the publication
1100
CoA
wild type enzyme, pH and temperature not specified in the publication
0.97
mutant enzyme H533K, pH and temperature not specified in the publication
1.3
phosphate
mutant enzyme H533E, pH and temperature not specified in the publication
1.7
phosphate
mutant enzyme H533N, pH and temperature not specified in the publication
2.1
phosphate
mutant enzyme H533Q, pH and temperature not specified in the publication
3.1
phosphate
mutant enzyme H533A, pH and temperature not specified in the publication
7.3
phosphate
mutant enzyme H533D, pH and temperature not specified in the publication
12
phosphate
with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C
65
phosphate
wild type enzyme, pH and temperature not specified in the publication
95
phosphate
mutant enzyme H533R, pH and temperature not specified in the publication