Any feedback?
Information on EC 2.3.1.13 - glycine N-acyltransferase and Organism(s) Bos taurus and UniProt Accession Q2KIR7
for references in articles please use BRENDA:EC2.3.1.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.13 glycine N-acyltransferaseIUBMB Comments
The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor. Not identical with EC 2.3.1.68 glutamine N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase.
Specify your search results
Word Map
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glyat, glyatl1, glycine n-acyltransferase, glycine-n-acylase, glycine-n-acyltransferase, acyl-coa:glycine n-acyltransferase, glycine acyltransferase, glyatl3, glycine-n-acyltransferase like 1, glyatl2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, glycine
-
-
-
-
glycine acyltransferase
-
-
-
-
glycine-N-acylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + glycine = CoA + N-acylglycine
residue Glu226 functions to deprotonate glycine, facilitating nucleophilic attack on the acyl-CoA substrate
acyl-CoA + glycine = CoA + N-acylglycine
sequential reaction mechanism, acyl-CoA substrate adds to the enzyme first, glycine adds before CoA leaves and the peptide product dissociates last
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:glycine N-acyltransferase
The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor. Not identical with EC 2.3.1.68 glutamine N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
butyryl-CoA + glycine
CoA + N-butyrylglycine
-
19% of activity with benzoyl-coA
-
?
heptanoyl-CoA + glycine
CoA + N-heptanoylglycine
-
3.9% of activity with benzoyl-coA
-
?
isovaleryl-CoA + glycine
CoA + N-isovalerylglycine
-
8.4% of activity with benzoyl-coA
-
?
salicyl-CoA + glycine
CoA + salicyluric acid
-
15% of activity with benzoyl-coA
-
?
acyl-CoA + glycine
CoA + N-acylglycine
-
phenylacetyl-CoA or indoleacetyl-CoA can not act as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
-
phenylacetyl-CoA or indoleacetyl-CoA can not act as acyl donor
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
1 mM, 90% inhibition after 40 min, 20% activity can be recovered by adding 20fold excess of dithiothreitol, benzoyl-CoA protects
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLYAT_BOVIN
295
0
33907
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme fractions from hydroxylapatite column are inactivated by dialysis or concentration by ultracentrifugation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nandi, D.L.; Lucas, S.V.; Webster, L.T.
Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization
J. Biol. Chem.
254
7230-7237
1979
Bos taurus
Webster, L.T.
Benzoyl-CoA: amino acid and phenylacetyl-CoA: amino acid N-acyltransferases
Methods Enzymol.
77
301-308
1981
Bos taurus
Kelley, M.; Vessey, D.A.
Isolation and characterization of mitochondrial acyl-CoA: glycine N-acyltransferase from kidney
J. Biochem. Toxicol.
8
65-69
1993
Bos taurus
-
Van der Westhuizen, F.H.; Pretorius, P.J.; Erasmus, E.
The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase
J. Biochem. Mol. Toxicol.
14
102-109
2000
Bos taurus, Homo sapiens
EXTERNAL LINKS (specific for EC-Number 2.3.1.13)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
