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Literature summary for 2.3.1.13 extracted from

  • Badenhorst, C.P.; Jooste, M.; van Dijk, A.A.
    Enzymatic characterization and elucidation of the catalytic mechanism of a recombinant bovine glycine N-acyltransferase (2012), Drug Metab. Dispos., 40, 346-352.
    View publication on PubMed
Search for more literature for 2.3.1.13

Cloned(Commentary)

Cloned (Comment) Organism
-
 Bos taurus

Protein Variants

Protein Variants Comment Organism
E226Q about 3fold increase in Km value for lgycine Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0016
-
 glycine wild-type, pH 8.0, 30°C Bos taurus
0.002
-
 glycine recombinant wild-type, pH 8.0, 30°C Bos taurus
0.007
-
 glycine mutant E226Q, pH 8.0, 30°C Bos taurus
0.016
-
 benzoyl-CoA wild-type, pH 8.0, 30°C Bos taurus
0.016
-
 benzoyl-CoA recombinant wild-type, pH 8.0, 30°C Bos taurus
0.018
-
 benzoyl-CoA mutant E226Q, pH 8.0, 30°C Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Bos taurus 5739
-

Organism

Organism UniProt Comment Textmining
Bos taurus Q2KIR7
-
-

Reaction

Reaction Comment Organism Reaction ID
acyl-CoA + glycine = CoA + N-acylglycine residue Glu226 functions to deprotonate glycine, facilitating nucleophilic attack on the acyl-CoA substrate Bos taurus
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-CoA + glycine
-
 Bos taurus CoA + N-benzoylglycine
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 for mutant E226Q, activity increases significantly when raising the pH above 8.0, while for wild-type, activity remains more or less stable up to pH 9.0 Bos taurus
7.5 8.5 wild-type Bos taurus