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Information on EC 2.3.1.13 - glycine N-acyltransferase and Organism(s) Homo sapiens and UniProt Accession Q6IB77
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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.
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The taxonomic range for the selected organisms is: Homo sapiens
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, glyatl2, glycine-n-acyltransferase like 1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, glycine
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GLYATL1
glycine acyltransferase
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glycine-N-acylase
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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.
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
benzoyl-CoA + L-glutamine
CoA + N-benzoyl-L-glutamine
24% of the rate with glycine and benzoyl-CoA
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-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
best substrates are benzoyl-CoA as an acyl donor and glycine as acyl acceptor
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?
acyl-CoA + glycine
CoA + N-acylglycine
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the CoA derivatives of a number of aliphatic and aromatic acids, e.g. benzoyl-CoA and butyryl-CoA can act as acyl donor
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?
acyl-CoA + glycine
CoA + N-acylglycine
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salicyl-CoA acts as acyl donor
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?
additional information
?
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GLYAT exhibits mechanistic kinetic cooperativity
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additional information
?
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GLYAT exhibits mechanistic kinetic cooperativity
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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 SUBSTRATE
NATURAL 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0044
oleoyl-CoA
pH not specified in the publication, temperature not specified in the publication
0.038
benzoyl-CoA
mutant enzyme N156S, apparent value, at pH 8.0 and 37°C
0.053
benzoyl-CoA
mutant enzyme F168L, apparent value, at pH 8.0 and 37°C
0.071
benzoyl-CoA
mutant enzyme R131H, apparent value, at pH 8.0 and 37°C
30.42
benzoyl-CoA
K0.5 value at 2.5 mM gylcine, pH 8.0, temperature not specified in the publication
108.3
benzoyl-CoA
K0.5 value at 5 mM gylcine, pH 8.0, temperature not specified in the publication
305
benzoyl-CoA
K0.5 value at 20 mM gylcine, pH 8.0, temperature not specified in the publication
2.189
glycine
K0.5 value at 0.02 mM benzoyl-CoA, pH 8.0, temperature not specified in the publication
2.326
glycine
K0.5 value at 0.04 mM benzoyl-CoA, pH 8.0, temperature not specified in the publication
2.956
glycine
K0.5 value at 0.08 mM benzoyl-CoA, pH 8.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
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
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_HUMAN
296
0
33924
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Arg131His
polymorphism resulting in an amino acid change of Arg131His, in Japanese individuals
F168L
K16N
N156S
R131H
R199C
S17T
F168L
the mutant shows decreased activity compared to the wild type enzyme
F168L
the variant has a lower relative activity than the wild type enzyme
K16N
the variant has a greater relative activity than the wild type enzyme
N156S
the mutant shows increased activity compared to the wild type enzyme
N156S
the variant has a greater relative activity than the wild type enzyme
R131H
the variant has a greater relative activity than the wild type enzyme
R199C
the variant has a lower relative activity than the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Protino Ni-TED 2000 column chromatography and Sephadex G25 gel filtration
ammonium sulfate, hydroxylapatite, Biogel P 100, Blue-dextran agarose, chromatofocusing
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
the enzyme is overexpressed in primary prostate cancer compared with metastatic prostate cancer and benign prostatic tissue. Low-grade cancers have higher enzyme expression compared to high-grade prostate tumors
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
determination of kinetic parameters of recombinant human enzyme using the traditional colorimetric method and a HPLC-ESI-MS/MSmethod
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Webster, L.T.; Siddiqui, U.A.; Lucas, S.V.; Strong, J.M.; Mieyal, J.J.
Identification of separate acyl-CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man
J. Biol. Chem.
251
3352-3358
1976
Homo sapiens, Macaca mulatta
Mawal, Y.R.; Qureshi, I.A.
An immunodetection method for the quantitation of human acyl CoA: glycine N-acyltransferase in biological samples
Biochem. Mol. Biol. Int.
34
595-601
1994
Ovis aries, Homo sapiens
Mawal, Y.R.; Qureshi, I.A.
Purification to homogeneity of mitochondrial acyl CoA: glycine N-acyltransferase from human liver
Biochem. Biophys. Res. Commun.
205
1373-1379
1994
Ovis aries, Homo sapiens
Mawal, Y.; Paradis, K.; Qureshi, I.A.
Developmental profile of mitochondrial glycine N-acyltransferase in human liver
J. Pediatr.
130
1003-1007
1997
Homo sapiens
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
Zhang, H.; Lang, Q.; Li, J.; Zhong, Z.; Xie, F.; Ye, G.; Wan, B.; Yu, L.
Molecular cloning and characterization of a novel human glycine-N-acyltransferase gene GLYATL1, which activates transcriptional activity of HSE pathway
Int. J. Mol. Sci.
8
433-444
2007
Homo sapiens (Q969I3)
-
Yamamoto, A.; Nonen, S.; Fukuda, T.; Yamazaki, H.; Azuma, J.
Genetic polymorphisms of glycine N-acyltransferase in Japanese individuals
Drug Metab. Pharmacokinet.
24
114-117
2009
Homo sapiens (Q6IB77)
Matsuo, M.; Terai, K.; Kameda, N.; Matsumoto, A.; Kurokawa, Y.; Funase, Y.; Nishikawa, K.; Sugaya, N.; Hiruta, N.; Kishimoto, T.
Designation of enzyme activity of glycine-N-acyltransferase family genes and depression of glycine-N-acyltransferase in human hepatocellular carcinoma
Biochem. Biophys. Res. Commun.
420
901-906
2012
Homo sapiens (Q6IB77), Homo sapiens
Waluk, D.P.; Schultz, N.; Hunt, M.C.
Identification of glycine N-acyltransferase-like 2 (GLYATL2) as a transferase that produces N-acyl glycines in humans
FASEB J.
24
2795-2803
2010
Homo sapiens (Q8WU03)
Badenhorst, C.P.; van der Sluis, R.; Erasmus, E.; van Dijk, A.A.
Glycine conjugation: importance in metabolism, the role of glycine N-acyltransferase, and factors that influence interindividual variation
Expert. Opin. Drug Metab. Toxicol.
9
1139-1153
2013
Homo sapiens (Q6IB77)
Van der Sluis, R.; Badenhorst, C.; Van der Westhuizen, F.; Van Dijk, A.
Characterisation of the influence of genetic variations on the enzyme activity of a recombinant human glycine N-acyltransferase
Gene
515
447-453
2013
Homo sapiens (Q6IB77), Homo sapiens
van der Sluis, R.; Badenhorst, C.P.; Erasmus, E.; van Dyk, E.; van der Westhuizen, F.H.; van Dijk, A.A.
Conservation of the coding regions of the glycine N-acyltransferase gene further suggests that glycine conjugation is an essential detoxification pathway
Gene
571
126-134
2015
Homo sapiens (Q6IB77), Homo sapiens
van der Sluis, R.; Ungerer, V.; Nortje, C.; A van Dijk, A.; Erasmus, E.
New insights into the catalytic mechanism of human glycine N-acyltransferase
J. Biochem. Mol. Toxicol.
31
e21963
2017
Homo sapiens (Q6IB77), Homo sapiens
Eich, M.L.; Chandrashekar, D.S.; Rodriguez Pen A, M.D.C.; Robinson, A.D.; Siddiqui, J.; Daignault-Newton, S.; Chakravarthi, B.V.S.K.; Kunju, L.P.; Netto, G.J.; Varambally, S.
Characterization of glycine-N-acyltransferase like 1 (GLYATL1) in prostate cancer
Prostate
79
1629-1639
2019
Homo sapiens
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