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Information on EC 2.3.1.65 - bile acid-CoA:amino acid N-acyltransferase and Organism(s) Homo sapiens and UniProt Accession Q14032
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2.3.1.65 bile acid-CoA:amino acid N-acyltransferaseIUBMB Comments
Also acts on CoA derivatives of other bile acids. Taurine and 2-fluoro-beta-alanine can act as substrates, but more slowly . The enzyme can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase . Bile-acid---amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono- and diglycerides, fat-soluble vitamins and cholesterol . This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalysed by EC 6.2.1.7, cholate---CoA ligase.
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Word Map
- 2.3.1.65
- peroxisomal
-
unconjugated
- acyl-coas
-
thioesterases
- cholyl-coa
-
acid-conjugating
-
hbats
- gallbladder
- proliferator
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
bile acid-coa:amino acid n-acyltransferase, bacat, bile acid coa:amino acid n-acyltransferase, baatp1, bile acid coa amino acid n-acyltransferase, bile acid coenzyme a-amino acid n-acyltransferase, bile acid coenzyme a:amino acid n-acyltransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, glycine-taurine N-
-
-
-
-
amino acid N-choloyltransferase
-
-
-
-
BAT
glycine-taurine N-acyltransferase
-
-
-
-
BAT
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
choloyl-CoA:glycine N-choloyltransferase
Also acts on CoA derivatives of other bile acids. Taurine and 2-fluoro-beta-alanine can act as substrates, but more slowly [4]. The enzyme can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase [7]. Bile-acid---amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono- and diglycerides, fat-soluble vitamins and cholesterol [4]. This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalysed by EC 6.2.1.7, cholate---CoA ligase.
CAS REGISTRY NUMBER
COMMENTARY
74506-32-4
-
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
choloyl-CoA + 2-fluoro-beta-alanine
CoA + 2-fluoro-beta-alanylcholate
-
2-fluoro-beta-alanine is an excellent substrate like taurine
-
-
?
choloyl-CoA + D-alpha-alanine
CoA + D-alpha-alanylcholate
-
about 10% of the rate with glycine
-
-
?
deoxycholoyl-CoA + glycine
CoA + glycodeoxycholate
-
92.4% of activity with choloyl-CoA
-
-
?
deoxycholoyl-CoA + taurine
CoA + taurodeoxycholate
-
81.7% of activity with choloyl-CoA
-
-
?
lithocholoyl-CoA + glycine
CoA + glycolithocholate
-
58.4% of activity with choloyl-CoA
-
-
?
lithocholoyl-CoA + taurine
CoA + taurolithocholate
-
43% of activity with choloyl-CoA
-
-
?
ursodeoxycholoyl-CoA + glycine
CoA + glycoursodeoxycholate
-
24.8% of activity with choloyl-CoA
-
-
?
ursodeoxycholoyl-CoA + taurine
CoA + tauroursodeoxycholate
-
35.3% of activity with choloyl-CoA
-
-
?
chenodeoxycholoyl-CoA + glycine
CoA + glycochenodeoxycholate
-
91.4% of activity with choloyl-CoA
-
-
?
chenodeoxycholoyl-CoA + glycine
CoA + glycochenodeoxycholate
-
glycine is a slightly better substrate than taurine, thioesterase activity in absence of glycine is about 20% of the conjugation activity
-
-
?
chenodeoxycholoyl-CoA + taurine
CoA + taurochenodeoxycholate
-
101.4% of activity with choloyl-CoA
-
-
?
choloyl-CoA + beta-alanine
CoA + beta-alanylcholate
-
beta-alanine is a poor substrate
-
-
?
choloyl-CoA + beta-alanine
CoA + beta-alanylcholate
-
about 10% of the rate with glycine
-
-
?
choloyl-CoA + glycine
CoA + glycocholate
-
ratio of glycine-/taurine-dependent activity is 1.0-1.4
-
?
choloyl-CoA + glycine
CoA + glycocholate
-
conjugation of bile acids with glycine or taurine favors their excretion into bile and uptake from portal blood into the liver, it promotes absorption of fat and fat-soluble vitamins in the acidic environment of the small intestine by lowering the pKa of the bile acids and hence maintaining its solubility
-
-
?
choloyl-CoA + glycine
CoA + glycocholate
-
taurine can replace glycine, involved in conjugation of bile acids
-
-
?
choloyl-CoA + glycine
CoA + glycocholate
-
cholesterol degradation, glycine conjugates of bile acids occur in adult
-
-
?
choloyl-CoA + glycine
CoA + glycocholate
-
glycine is a slightly better substrate than taurine, thioesterase activity in absence of glycine is about 20% of the conjugation activity
-
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
ratio of glycine-/taurine-dependent activity is 1.0-1.4
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
taurine is an excellent substrate
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
conjugation of bile acids with glycine or taurine favors their excretion into bile and uptake from portal blood into the liver, it promotes absorption of fat and fat-soluble vitamins in the acidic environment of the small intestine by lowering the pKa of the bile acids and hence maintaining its solubility
-
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
taurine can replace glycine, involved in conjugation of bile acids
-
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
cholesterol degradation, bile acids are secreted as taurine conjugates in fetus and neonatus
-
-
?
additional information
?
-
-
not: L-alpha-alanine, DL-cysteic acid, 4-aminobutyric acid, cysteine, sulfanilic acid
-
-
?
additional information
?
-
-
essential catalytic triad consisting of Cys-235, His-362 and Asp-328 with Cys-235 serving as the probable nucleophile and thus the site of covalent attachment of the bile acid molecule
-
-
?
additional information
?
-
-
may play important roles in protection against toxicity by accumulation of unconjugated bile acids and non-esterified very long-chain fatty acids
-
-
?
additional information
?
-
-
in addition to its bile acid conjugating activity, the enzyme also possesses thioesterase and glycine conjugating activities with long- and very long-chain acyl-CoAs, at least in vitro. The enzyme can also hydrolyze long- and very-long-chain saturated acyl-CoAs (mainly C16:0-C26:0), the enzyme also conjugates fatty acids to glycine
-
-
?
additional information
?
-
-
bile acidcoenzyme A:amino acid N-acyltransferase is the sole enzyme responsible for conjugation of primary and secondary bile acids to taurine and glycine
-
-
?
additional information
?
-
-
identification of three novel single nucleotide polymorphisms, 147C>T in exon 2 (silent), 602G>C in exon 3 (Arg201Pro), and 1134C>T in exon 4 (silent), in the gene of bile acid CoA: amino acid N-acyltransferase. The allelic frequencies are 0.005 for 147C>T, 0.095 for 602G>C, and 0.015 for 1134C>T. The two known SNPs, 59G>A (Arg20Gln, rs1572983) and UTR1513G>A (rs2229594), are detected at a frequency of 0.500 and 0.425, respectively. In the haplotype analysis for the 59G>A and 602G>C polymorphisms, the allelic frequency of 59G-602G, 59G-602C, 59A-602G and 59A-602C is 0.405, 0.095, 0.500 and 0.000, respectively. The allelic frequency of the nonsynonymous SNP 602G>C is 0.194 in a Caucasian population
-
-
?
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
choloyl-CoA + glycine
CoA + glycocholate
-
conjugation of bile acids with glycine or taurine favors their excretion into bile and uptake from portal blood into the liver, it promotes absorption of fat and fat-soluble vitamins in the acidic environment of the small intestine by lowering the pKa of the bile acids and hence maintaining its solubility
-
-
?
choloyl-CoA + glycine
CoA + glycocholate
-
taurine can replace glycine, involved in conjugation of bile acids
-
-
?
choloyl-CoA + glycine
CoA + glycocholate
-
cholesterol degradation, glycine conjugates of bile acids occur in adult
-
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
conjugation of bile acids with glycine or taurine favors their excretion into bile and uptake from portal blood into the liver, it promotes absorption of fat and fat-soluble vitamins in the acidic environment of the small intestine by lowering the pKa of the bile acids and hence maintaining its solubility
-
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
taurine can replace glycine, involved in conjugation of bile acids
-
-
?
choloyl-CoA + taurine
CoA + taurocholate
-
cholesterol degradation, bile acids are secreted as taurine conjugates in fetus and neonatus
-
-
?
additional information
?
-
-
may play important roles in protection against toxicity by accumulation of unconjugated bile acids and non-esterified very long-chain fatty acids
-
-
?
additional information
?
-
-
bile acidcoenzyme A:amino acid N-acyltransferase is the sole enzyme responsible for conjugation of primary and secondary bile acids to taurine and glycine
-
-
?
additional information
?
-
-
identification of three novel single nucleotide polymorphisms, 147C>T in exon 2 (silent), 602G>C in exon 3 (Arg201Pro), and 1134C>T in exon 4 (silent), in the gene of bile acid CoA: amino acid N-acyltransferase. The allelic frequencies are 0.005 for 147C>T, 0.095 for 602G>C, and 0.015 for 1134C>T. The two known SNPs, 59G>A (Arg20Gln, rs1572983) and UTR1513G>A (rs2229594), are detected at a frequency of 0.500 and 0.425, respectively. In the haplotype analysis for the 59G>A and 602G>C polymorphisms, the allelic frequency of 59G-602G, 59G-602C, 59A-602G and 59A-602C is 0.405, 0.095, 0.500 and 0.000, respectively. The allelic frequency of the nonsynonymous SNP 602G>C is 0.194 in a Caucasian population
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxynonenal
-
inactivated by 4HNE in a dose-dependent manner. The active-site His (His362) dose-dependently forms a 4-hydroxynonenal adduct, contributing to loss of activity
N-ethylmaleimide
-
10 min, at 0.2 mM: 90% loss of activity, preincubation with cholyl-CoA before NEM-treatment protects
additional information
-
not inhibited by 2-mercaptoethanol, CaCl2, EDTA, glutathione
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 8.2
-
taurine: about half-maximal activity at pH 5.2 and pH 8.2, glycine: 80% of maximal activity at pH 8.2
TEMPERATURE OPTIMUM
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
additional information
-
when expressed in fibroblasts, GFP-tagged hBAAT localizes to the cytosol
-
-
the cytosolic enzyme localization is due to a carboxyterminal non-consensus peroxisomal targeting signal, SQL, since mutation of the SQL to SKL results in BAAT being efficiently imported into peroxisomes
-
the cytosolic enzyme localization is due to a carboxyterminal non-consensus peroxisomal targeting signal, SQL, since mutation of the SQL to SKL results in BAAT being efficiently imported into peroxisomes
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). BAAT_HUMAN
418
0
46299
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
BAAT-12AA Trunc
-
mutant enzyme BAAT-12AA Trunc with 12 removed carboxy-terminal amino acids (407-418)
BAAT-Ex1Del
-
the amino (N)-terminal truncated mutant enzyme BAAT-Ex1Del possess no detectable N-acyltransferase activity
BAAT-S
-
the mutant BAAT-S, lacking the final two amino acids, shows slightly reduced enzyme activity
BAAT-SKL
-
mutant BAAT-SKL with a canonical PTS sequence has greater than a 2.5fold increase in N-acyltransferase activity compared with wild type enzyme using cholyl-CoA and taurine as substrates
C235S
additional information
-
the cytosolic enzyme localization is due to a carboxyterminal non-consensus peroxisomal targeting signal, SQL, since mutation of the SQL to SKL results in BAAT being efficiently imported into peroxisomes
C235S
-
mutation converts the enzyme into an efficient bile acid-CoA thioesterase
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of GFP-tagged enzyme in HeLa cells, which is exclusively located in the cytosol, high mobility of the GFP-fusion proteins in the cytosol and absence of peroxisomal escape
-
gene/full-length cDNA is cloned and expressed in Escherichia coli XL1-Blue or BL21
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kimura, M.; Okuno, E.; Inada, J.; Ohyama, H.; Kido, R.
Purification and characterization of amino-acid N-choloyltransferase from human liver
Hoppe-Seyler's Z. Physiol. Chem.
364
637-645
1983
Homo sapiens
Sfakianos, M.K.; Wilson, L.; Sakalian, M.; Falany, C.N.; Barnes, S.
Conserved residues in the putative catalytic triad of human bile acid coenzyme A:amino acid N-acyltransferase
J. Biol. Chem.
277
47270-47275
2002
Homo sapiens
O'Byrne, J.; Hunt, M.C.; Rai, D.K.; Saeki, M.; Alexson, S.E.H.
The Human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine
J. Biol. Chem.
278
34237-34244
2003
Homo sapiens, Mus musculus
Pellicoro, A.; van den Heuvel, F.A.; Geuken, M.; Moshage, H.; Jansen, P.L.; Faber, K.N.
Human and rat bile acid-CoA:amino acid N-acyltransferase are liver-specific peroxisomal enzymes: implications for intracellular bile salt transport
Hepatology
45
340-348
2007
Homo sapiens, Rattus norvegicus
Shonsey, E.M.; Sfakianos, M.; Johnson, M.; He, D.; Falany, C.N.; Falany, J.; Merkler, D.J.; Barnes, S.
Bile acid coenzyme A: amino acid N-acyltransferase in the amino acid conjugation of bile acids
Methods Enzymol.
400
374-394
2005
Homo sapiens (Q14032), Rattus norvegicus
Tougou, K.; Fukuda, T.; Ito, T.; Yamazaki, H.; Fujio, Y.; Azuma, J.
Genetic polymorphism of bile acid CoA: amino acid N-acyltransferase in Japanese individuals
Drug Metab. Pharmacokinet.
22
125-128
2007
Homo sapiens
Shonsey, E.M.; Eliuk, S.M.; Johnson, M.S.; Barnes, S.; Falany, C.N.; Darley-Usmar, V.M.; Renfrow, M.B.
Inactivation of human liver bile acid CoA:amino acid N-acyltransferase by the electrophilic lipid, 4-hydroxynonenal
J. Lipid Res.
49
282-294
2008
Homo sapiens
Buch, C.; Hunt, M.C.; Alexson, S.E.; Hallberg, E.
Localization of peroxisomal matrix proteins by photobleaching
Biochem. Biophys. Res. Commun.
388
355-359
2009
Homo sapiens
Kirilenko, B.M.; Hagey, L.R.; Barnes, S.; Falany, C.N.; Hiller, M.
Evolutionary analysis of bile acid-conjugating enzymes reveals a complex duplication and reciprocal loss history
Genome Biol. Evol.
11
3256-3268
2019
Bos taurus, Felis catus, Homo sapiens, Loxodonta africana, Mus musculus
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