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Literature summary extracted from

  • Thao, S.; Escalante-Semerena, J.C.
    Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N-lysine acetyltransferase involved in carbon and energy metabolism (2011), mBio, 2, e00216-11.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.32 expressed as a His-tagged fusion protein Salmonella enterica

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.32 0.01
-
acetyl-CoA K0.5, pH 7.0, 37°C Salmonella enterica
2.3.1.32 0.132
-
Acs (AMP forming) pH 7.0, 37°C Salmonella enterica

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.32 acetyl-CoA + L-Lys
-
Salmonella enterica ?
-
?
2.3.1.32 Acs (AMP forming) + L-Lys
-
Salmonella enterica ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.32 GCN5-related N-acetyltransferase
-
Salmonella enterica
2.3.1.32 GNAT
-
Salmonella enterica
2.3.1.32 SePat
-
Salmonella enterica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.32 37
-
assay at Salmonella enterica

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.32 4.3
-
acetyl-CoA K0.5, pH 7.0, 37°C Salmonella enterica
2.3.1.32 8
-
Acs (AMP forming) pH 7.0, 37°C Salmonella enterica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.32 7.5
-
assay at Salmonella enterica

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.32 60
-
Acs (AMP forming) pH 7.0, 37°C Salmonella enterica