Information on EC 2.3.1.13 - glycine N-acyltransferase and Organism(s) Homo sapiens

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Homo sapiens


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.13
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RECOMMENDED NAME
GeneOntology No.
glycine N-acyltransferase
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylalanine metabolism
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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5 novel single nucleotide polymorphisms of the GlyAT gene, including a polymorphism resulting in an amino acid change of Arg131His, in Japanese individuals are identified. The allelic frequency of this polymorphism in Japanese is 0.005, and none possessed this single nucleotide polymorphism among 31 caucasian individuals. Three genetic polymorphisms, 7527 T to A, 21289G to A and 21364A to G, cause the amino acid changes
metabolism
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the enzyme activity affects mitochondrial ATP production, glycine availability, free coenzyme A availability, and the toxicity of various organic acids
physiological function
-
the enzyme plays a role in liver cancer and musculoskeletal development
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
arachidonoyl-CoA + glycine
CoA + N-arachidonoylglycine
show the reaction diagram
-
-
-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
benzoyl-CoA + L-alanine
CoA + N-benzoyl-L-alanine
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + L-asparagine
CoA + N-benzoyl-L-asparagine
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + L-glutamic acid
CoA + N-benzoyl-L-glutamic acid
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + L-glutamine
CoA + N-benzoyl-L-glutamine
show the reaction diagram
isovaleryl-CoA + glycine
CoA + N-isovalerylglycine
show the reaction diagram
-
-
-
?
octanoyl-CoA + glycine
CoA + N-octanoylglycine
show the reaction diagram
-
-
-
?
oleoyl-CoA + glycine
CoA + N-oleoyl-glycine
show the reaction diagram
-
-
-
?
salicyl-CoA + glycine
CoA + N-salicylglycine
show the reaction diagram
-
-
-
?
stearoyl-CoA + glycine
CoA + N-stearoyl-glycine
show the reaction diagram
-
-
-
?
additional information
?
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substrates are medium- and long-chain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA. Enzyme is specific for glycine as an acceptor molecule, and preferentially produces N-oleoyl glycine. No substrates: docosahexanoyl-CoA and chenodeoxycholoyl-CoA, L-alanine, l-serine
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
K3PO4
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100 mM, 68% inhibition
KCl
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100 mM, 79% inhibition
NaCl
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100 mM, 53% inhibition; 100 mM, 57% inhibition
oleoyl-CoA
slight substrate inhibition above 0.05 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
997
alanine
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acyl donor benzoyl-CoA
0.021 - 57.9
benzoyl-CoA
6.4
glycine
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acyl donor benzoyl-CoA
124
isovaleryl-CoA
-
-
198
Octanoyl-CoA
-
-
0.0044
oleoyl-CoA
pH not specified in the publication, temperature not specified in the publication
83.7
salicyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.19
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activity in liver 4 h after birth
2.51
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activity in liver of a 7 months old child
6.38
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mean activity in liver of children aged 18 months to 11 years
6.5
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activity in liver of adults aged 24 to 40 years
13.9
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4 - 8.6
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-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.44
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression in salivary gland and trachea
Manually annotated by BRENDA team
highest expression in salivary gland and trachea
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
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27000, SDS-PAGE
30000
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1 * 30000, SDS-PAGE
35100
SDS-PAGE, Western blot analysis
56000
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x * 56000, thioredoxin-His-tagged fusion protein, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 56000, thioredoxin-His-tagged fusion protein, SDS-PAGE
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, hydroxylapatite, Biogel P 100, Blue-dextran agarose, chromatofocusing
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Protino Ni-TED 2000 column chromatography and Sephadex G25 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Origami cells
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overexpression in HEK293T cells, transient expression in COS-7 cells as myc-tagged GLYATL1 fusion protein, GLYATL1 is involved in heat shock response pathway
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform Glyat expression is suppressed in all hepatocellular carcinomas, but not in other liver diseases. Glyat repression in cancerous cells in the liver is controlled at the transcriptional level
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arg131His
-
polymorphism resulting in an amino acid change of Arg131His, in Japanese individuals
E226Q
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active site mutant
E227Q
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inactive
Q61L
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the mutation has a negative effect on the enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
isoform Glyat expression is suppressed in all hepatocellular carcinomas, but not in other liver diseases. Glyat repression in cancerous cells in the liver is controlled at the transcriptional level