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Literature summary extracted from

  • Reger, A.S.; Carney, J.M.; Gulick, A.M.
    Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase (2007), Biochemistry, 46, 6536-6546.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.2.1.1 vapor diffusion method, crystallographic structures of wild-type enzyme and mutant enzymes R194A, R584A, R584E, K609A, and V386A Salmonella enterica

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.1 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 Salmonella enterica
6.2.1.1 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 Salmonella enterica
6.2.1.1 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 Salmonella enterica
6.2.1.1 G524L inactive mutant enzyme Salmonella enterica
6.2.1.1 G524L mutant enzyme is unable to catalyze the complete reaction yet catalyzes the adenylation half-reaction with activity comparable to the wild-type enzyme Salmonella enterica
6.2.1.1 G524S kcat/Km for ATP is 1.6fold lower than wild-type value, kcat/Km for CoA is 19fold lower than wild-type value Salmonella enterica
6.2.1.1 K609A inactive mutant enzyme Salmonella enterica
6.2.1.1 K609A mutation results in an enzyme that is unable to catalyze the adenylate reaction Salmonella enterica
6.2.1.1 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 Salmonella enterica
6.2.1.1 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 Salmonella enterica
6.2.1.1 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 Salmonella enterica
6.2.1.1 R584A kcat/Km for ATP is 1.2 fold than wild-type value, kcat/Km for CoA is 19fold lower than wild-type value Salmonella enterica
6.2.1.1 R584E kcat/Km for ATP is 1.1fold higher than wild-type value, kcat/Km for CoA is 21fold lower than wild-type value Salmonella enterica

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.1 0.0224
-
 ATP pH 7.5, mutant enzyme R526A Salmonella enterica
6.2.1.1 0.0238
-
 ATP pH 7.5, mutant enzyme A357V Salmonella enterica
6.2.1.1 0.0265
-
 ATP pH 7.5, mutant enzyme R584E Salmonella enterica
6.2.1.1 0.0287
-
 ATP pH 7.5, mutant enzyme R194A Salmonella enterica
6.2.1.1 0.0373
-
 ATP pH 7.5, mutant enzyme R194E Salmonella enterica
6.2.1.1 0.0381
-
 ATP pH 7.5, mutant enzyme R584A Salmonella enterica
6.2.1.1 0.044
-
 ATP pH 7.5, mutant enzyme D517P Salmonella enterica
6.2.1.1 0.05
-
 CoA pH 7.5, wild-type enzyme Salmonella enterica
6.2.1.1 0.0638
-
 ATP pH 7.5, mutant enzyme G524S Salmonella enterica
6.2.1.1 0.0771
-
 ATP pH 7.5, wild-type enzyme Salmonella enterica
6.2.1.1 0.1072
-
 CoA pH 7.5, mutant enzyme R194E Salmonella enterica
6.2.1.1 0.133
-
 CoA pH 7.5, mutant enzyme A357V Salmonella enterica
6.2.1.1 0.1417
-
 CoA pH 7.5, mutant enzyme R194A Salmonella enterica
6.2.1.1 0.205
-
 CoA pH 7.5, mutant enzyme R526A Salmonella enterica
6.2.1.1 0.228
-
 CoA pH 7.5, mutant enzyme D517G Salmonella enterica
6.2.1.1 0.243
-
 ATP pH 7.5, mutant enzyme D517G Salmonella enterica
6.2.1.1 0.3583
-
 CoA pH 7.5, mutant enzyme R584A Salmonella enterica
6.2.1.1 0.426
-
 CoA pH 7.5, mutant enzyme R584E Salmonella enterica
6.2.1.1 0.448
-
 CoA pH 7.5, mutant enzyme G524S Salmonella enterica
6.2.1.1 0.527
-
 CoA pH 7.5, mutant enzyme D517P Salmonella enterica

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.1 Salmonella enterica
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.1
-
 Salmonella enterica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.1 ATP + acetate + CoA
-
 Salmonella enterica AMP + diphosphate + acetyl-CoA
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.2.1.1 1.7
-
 ATP pH 7.5, wild-type enzyme Salmonella enterica
6.2.1.1 3.2
-
 CoA pH 7.5, wild-type enzyme Salmonella enterica
6.2.1.1 35
-
 CoA pH 7.5, mutant enzyme A357V Salmonella enterica
6.2.1.1 36.4
-
 ATP pH 7.5, mutant enzyme R584E Salmonella enterica
6.2.1.1 37.4
-
 ATP pH 7.5, mutant enzyme R526A Salmonella enterica
6.2.1.1 38.9
-
 ATP pH 7.5, mutant enzyme A357V Salmonella enterica
6.2.1.1 39.9
-
 ATP pH 7.5, mutant enzyme R194A Salmonella enterica
6.2.1.1 40
-
 CoA pH 7.5, mutant enzyme R194E Salmonella enterica
6.2.1.1 40.5
-
 CoA pH 7.5, mutant enzyme R526A Salmonella enterica
6.2.1.1 40.8
-
 CoA pH 7.5, mutant enzyme R584E Salmonella enterica
6.2.1.1 40.9
-
 ATP pH 7.5, mutant enzyme D517P Salmonella enterica
6.2.1.1 41.1
-
 CoA pH 7.5, mutant enzyme R194A Salmonella enterica
6.2.1.1 41.5
-
 CoA pH 7.5, mutant enzyme R584A Salmonella enterica
6.2.1.1 41.7
-
 ATP pH 7.5, mutant enzyme R194E Salmonella enterica
6.2.1.1 42.4
-
 CoA pH 7.5, mutant enzyme D517G Salmonella enterica
6.2.1.1 42.8
-
 ATP pH 7.5, mutant enzyme D517G Salmonella enterica
6.2.1.1 43.1
-
 CoA pH 7.5, mutant enzyme G524S Salmonella enterica
6.2.1.1 43.8
-
 CoA pH 7.5, mutant enzyme D517P Salmonella enterica
6.2.1.1 46.7
-
 ATP pH 7.5, mutant enzyme R584A Salmonella enterica
6.2.1.1 49.8
-
 ATP pH 7.5, mutant enzyme G524S Salmonella enterica
6.2.1.1 95.1
-
 CoA pH 7.5, wild-type enzyme Salmonella enterica
6.2.1.1 100.6
-
 ATP pH 7.5, wild-type enzyme Salmonella enterica