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Literature summary extracted from

  • Lawrence, S.H.; Luther, K.B.; Schindelin, H.; Ferry, J.G.
    Structural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila (2006), J. Bacteriol., 188, 1143-1154.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.8 expression in Escherichia coli Methanosarcina thermophila

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.8 hanging drop vapor diffusion method. Crystal structures of phosphotransacetylase in complex with the substrate CoA reveals one CoA (CoA(1)) bound in the proposed active site cleft and an additional CoA (CoA(2)) bound at the periphery of the cleft. The crystal structures indicat that binding of CoA(1) is mediated by a series of hydrogen bonds and extensive van der Waals interactions with the enzyme and that there are fewer of these interactions between CoA(2) and the enzyme Methanosarcina thermophila

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.8 D316E kcat for the reaction of acetyl phosphate and CoA is 2.4fold lower than wild-type value, Km for CoA is 1.1fold higher than wild-type value, Km for acetyl phosphate is 1.4fold lower than wild-type value Methanosarcina thermophila
2.3.1.8 R310A kcat for the reaction of acetyl phosphate and CoA is 22.6fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 122fold higher than wild-type value Methanosarcina thermophila
2.3.1.8 R310K kcat for the reaction of acetyl phosphate and CoA is 472fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 2.9fold higher than wild-type value Methanosarcina thermophila
2.3.1.8 R310Q kcat for the reaction of acetyl phosphate and CoA is 75.2fold lower than wild-type value, Km for CoA is 2.8fold higher than wild-type value, Km for acetyl phosphate is 4.2fold higher than wild-type value Methanosarcina thermophila
2.3.1.8 S309A kcat for the reaction of acetyl phosphate and CoA is 358fold lower than wild-type value, Km for CoA is nearly identical to wild-type value, Km for acetyl phosphate is 1.96fold lower than wild-type value Methanosarcina thermophila
2.3.1.8 S309C kcat for the reaction of acetyl phosphate and CoA is 851fold lower than wild-type value, Km for CoA is1.4 fold higher than wild-type value, Km for acetyl phosphate is 1.4fold higher than wild-type value Methanosarcina thermophila
2.3.1.8 S309T kcat for the reaction of acetyl phosphate and CoA is 337fold lower than wild-type value, Km for CoA is 1.8fold lower than wild-type value, Km for acetyl phosphate is nearly identical to wild-type value Methanosarcina thermophila

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.8 0.037
-
 CoA 23°C, pH 7.2, mutant enzyme S309T Methanosarcina thermophila
2.3.1.8 0.065
-
 CoA 23°C, pH 7.2, wild-type enzyme Methanosarcina thermophila
2.3.1.8 0.067
-
 CoA 23°C, pH 7.2, mutant enzyme S309A Methanosarcina thermophila
2.3.1.8 0.074
-
 CoA 23°C, pH 7.2, mutant enzyme D316E Methanosarcina thermophila
2.3.1.8 0.094
-
 acetyl phosphate 23°C, pH 7.2, mutant enzyme S309A Methanosarcina thermophila
2.3.1.8 0.094
-
 CoA 23°C, pH 7.2, mutant enzyme S309C Methanosarcina thermophila
2.3.1.8 0.116
-
 CoA 23°C, pH 7.2, mutant enzyme R310K Methanosarcina thermophila
2.3.1.8 0.12
-
 CoA 23°C, pH 7.2, mutant enzyme R310A Methanosarcina thermophila
2.3.1.8 0.143
-
 acetyl phosphate 23°C, pH 7.2, mutant enzyme D316E Methanosarcina thermophila
2.3.1.8 0.175
-
 acetyl phosphate 23°C, pH 7.2, mutant enzyme S309T Methanosarcina thermophila
2.3.1.8 0.185
-
 CoA 23°C, pH 7.2, mutant enzyme R310Q Methanosarcina thermophila
2.3.1.8 0.185
-
 acetyl phosphate 23°C, pH 7.2, wild-type enzyme Methanosarcina thermophila
2.3.1.8 0.255
-
 acetyl phosphate 23°C, pH 7.2, mutant enzyme S309C Methanosarcina thermophila
2.3.1.8 0.531
-
 acetyl phosphate 23°C, pH 7.2, mutant enzyme R310K Methanosarcina thermophila
2.3.1.8 0.775
-
 acetyl phosphate 23°C, pH 7.2, mutant enzyme R310Q Methanosarcina thermophila
2.3.1.8 22.5
-
 acetyl phosphate 23°C, pH 7.2, mutant enzyme R310A Methanosarcina thermophila

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.8 Methanosarcina thermophila P38503
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.8
-
 Methanosarcina thermophila

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.8 acetyl-phosphate + CoA
-
 Methanosarcina thermophila acetyl-CoA + phosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.8 6.1
-
 CoA 23°C, pH 7.2, mutant enzyme S309C Methanosarcina thermophila
2.3.1.8 11
-
 CoA 23°C, pH 7.2, mutant enzyme R310K Methanosarcina thermophila
2.3.1.8 14.5
-
 CoA 23°C, pH 7.2, mutant enzyme S309A Methanosarcina thermophila
2.3.1.8 15.4
-
 CoA 23°C, pH 7.2, mutant enzyme S309T Methanosarcina thermophila
2.3.1.8 69
-
 CoA 23°C, pH 7.2, mutant enzyme R310Q Methanosarcina thermophila
2.3.1.8 230
-
 CoA 23°C, pH 7.2, mutant enzyme R310A Methanosarcina thermophila
2.3.1.8 2150
-
 CoA 23°C, pH 7.2, mutant enzyme D316E Methanosarcina thermophila
2.3.1.8 5190
-
 CoA 23°C, pH 7.2, wild-type enzyme Methanosarcina thermophila