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Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)

 BAAT_HUMAN              Reviewed;         418 AA.
Q14032; Q3B7W9; Q96L31;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
16-OCT-2019, entry version 155.
RecName: Full=Bile acid-CoA:amino acid N-acyltransferase {ECO:0000303|PubMed:8034703};
Short=BACAT {ECO:0000303|PubMed:12810727};
Short=BAT {ECO:0000303|PubMed:8034703};
EC=2.3.1.65 {ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576, ECO:0000269|PubMed:8034703};
AltName: Full=Bile acid-CoA thioesterase {ECO:0000303|PubMed:12239217, ECO:0000303|PubMed:12810727};
AltName: Full=Choloyl-CoA hydrolase;
EC=3.1.2.27 {ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:8034703};
AltName: Full=Glycine N-choloyltransferase;
AltName: Full=Long-chain fatty-acyl-CoA hydrolase {ECO:0000303|PubMed:12810727};
EC=3.1.2.2 {ECO:0000269|PubMed:12810727};
Name=BAAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-17, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
LOCATION.
TISSUE=Liver;
PubMed=8034703;
Falany C.N., Johnson M.R., Barnes S., Diasio R.B.;
"Glycine and taurine conjugation of bile acids by a single enzyme.
Molecular cloning and expression of human liver bile acid CoA:amino
acid N-acyltransferase.";
J. Biol. Chem. 269:19375-19379(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-20.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-20.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-20.
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBUNIT, AND
BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
PubMed=2037576;
Johnson M.R., Barnes S., Kwakye J.B., Diasio R.B.;
"Purification and characterization of bile acid-CoA:amino acid N-
acyltransferase from human liver.";
J. Biol. Chem. 266:10227-10233(1991).
[7]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-235; ASP-328 AND
HIS-362, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12239217; DOI=10.1074/jbc.m207463200;
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).
[8]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, MUTAGENESIS OF CYS-235; ASP-328; HIS-362 AND GLN-417, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12810727; DOI=10.1074/jbc.m300987200;
O'Byrne J., Hunt M.C., Rai D.K., Saeki M., Alexson S.E.;
"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).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
VARIANT FHCA VAL-76.
PubMed=12704386; DOI=10.1038/ng1147;
Carlton V.E.H., Harris B.Z., Puffenberger E.G., Batta A.K.,
Knisely A.S., Robinson D.L., Strauss K.A., Shneider B.L., Lim W.A.,
Salen G., Morton D.H., Bull L.N.;
"Complex inheritance of familial hypercholanemia with associated
mutations in TJP2 and BAAT.";
Nat. Genet. 34:91-96(2003).
-!- FUNCTION: Catalyzes the amidation of bile acids (BAs) with the
amino acids taurine and glycine (PubMed:12810727, PubMed:8034703,
PubMed:2037576, PubMed:12239217). More than 95% of the BAs are N-
acyl amidates with glycine and taurine (PubMed:8034703). Amidation
of BAs in the liver with glycine or taurine prior to their
excretion into bile is an important biochemical event in bile acid
metabolism (PubMed:12810727). This conjugation (or amidation)
plays several important biological roles in that it promotes the
secretion of BAs and cholesterol into bile and increases the
detergent properties of BAs in the intestine, which facilitates
lipid and vitamin absorption (PubMed:12810727). May also act as an
acyl-CoA thioesterase that regulates intracellular levels of free
fatty acids (PubMed:12810727, PubMed:8034703, PubMed:12239217). In
vitro, catalyzes the hydrolysis of long- and very long-chain
saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH),
and conjugates glycine to these acyl-CoAs (PubMed:12810727).
{ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727,
ECO:0000269|PubMed:2037576, ECO:0000269|PubMed:8034703,
ECO:0000303|PubMed:12810727, ECO:0000303|PubMed:8034703}.
-!- CATALYTIC ACTIVITY:
Reaction=choloyl-CoA + glycine = CoA + glycocholate + H(+);
Xref=Rhea:RHEA:14001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57373;
EC=2.3.1.65; Evidence={ECO:0000269|PubMed:12239217,
ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576,
ECO:0000269|PubMed:8034703};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14002;
Evidence={ECO:0000305|PubMed:12239217,
ECO:0000305|PubMed:12810727, ECO:0000305|PubMed:2037576,
ECO:0000305|PubMed:8034703};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
EC=3.1.2.2; Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=choloyl-CoA + H2O = cholate + CoA + H(+);
Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373;
EC=3.1.2.27; Evidence={ECO:0000269|PubMed:12239217,
ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:8034703};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542;
Evidence={ECO:0000305|PubMed:12239217,
ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA +
H(+); Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287,
ChEBI:CHEBI:62989; EC=3.1.2.27;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+);
Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate;
Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate;
Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=choloyl-CoA + taurine = CoA + H(+) + taurocholate;
Xref=Rhea:RHEA:47100, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:507393;
Evidence={ECO:0000269|PubMed:12810727,
ECO:0000269|PubMed:8034703};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47101;
Evidence={ECO:0000305|PubMed:12810727,
ECO:0000305|PubMed:8034703};
-!- CATALYTIC ACTIVITY:
Reaction=chenodeoxycholoyl-CoA + glycine = CoA +
glycochenodeoxycholate + H(+); Xref=Rhea:RHEA:49788,
ChEBI:CHEBI:15378, ChEBI:CHEBI:36252, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57305, ChEBI:CHEBI:62989;
Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49789;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=chenodeoxycholoyl-CoA + taurine = CoA + H(+) +
taurochenodeoxycholate; Xref=Rhea:RHEA:49784, ChEBI:CHEBI:9407,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989,
ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49785;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=eicosanoyl-CoA + glycine = CoA + H(+) + N-
eicosanoylglycinate; Xref=Rhea:RHEA:49792, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57380,
ChEBI:CHEBI:87391; Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49793;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=glycine + hexacosanoyl-CoA = CoA + H(+) + N-
hexacosanoylglycine; Xref=Rhea:RHEA:49772, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:64868,
ChEBI:CHEBI:87414; Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49773;
Evidence={ECO:0000305|PubMed:12810727};
-!- CATALYTIC ACTIVITY:
Reaction=docosanoyl-CoA + glycine = CoA + H(+) + N-
docosanoylglycine; Xref=Rhea:RHEA:49780, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:65059,
ChEBI:CHEBI:87410; Evidence={ECO:0000269|PubMed:12810727};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49781;
Evidence={ECO:0000305|PubMed:12810727};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.1 mM for taurine toward choloyl-CoA
{ECO:0000269|PubMed:2037576};
KM=1.8 mM for taurine toward choloyl-CoA
{ECO:0000269|PubMed:8034703};
KM=5.6 mM for glycine toward choloyl-CoA
{ECO:0000269|PubMed:8034703};
KM=5.8 mM for glycine toward choloyl-CoA
{ECO:0000269|PubMed:2037576};
KM=2.2 mM for 2-fluoro-beta-alanine toward choloyl-CoA
{ECO:0000269|PubMed:2037576};
KM=19.3 uM for glycine toward arachidoyl-CoA
{ECO:0000269|PubMed:12810727};
KM=50.02 uM for choloyl-CoA (acyl-CoA thioesterase activity)
{ECO:0000269|PubMed:12239217};
Vmax=0.33 umol/min/mg enzyme with taurine as substrate for
acyltransferase activity {ECO:0000269|PubMed:2037576};
Vmax=0.19 umol/min/mg enzyme with 2-fluoro-beta-alanine as
substrate for acyltransferase activity
{ECO:0000269|PubMed:2037576};
Vmax=0.77 umol/min/mg enzyme with glycine as substrate for
acyltransferase activity {ECO:0000269|PubMed:2037576};
Vmax=223 nmol/min/mg enzyme with arachidoyl-CoA as substrate for
acyl-CoA thioesterase activity {ECO:0000269|PubMed:12810727};
Vmax=1.48 umol/min/ug enzyme for acyl-CoA thioesterase activity
{ECO:0000269|PubMed:12239217};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2037576}.
-!- INTERACTION:
Q0D2H9:GOLGA8DP; NbExp=5; IntAct=EBI-8994378, EBI-10181276;
Q08AF8:GOLGA8G; NbExp=3; IntAct=EBI-8994378, EBI-10181260;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:8034703}.
Peroxisome {ECO:0000250|UniProtKB:Q63276}.
-!- TISSUE SPECIFICITY: Expressed in liver, gallbladder mucosa and
pancreas. {ECO:0000269|PubMed:12810727,
ECO:0000269|PubMed:2037576}.
-!- DISEASE: Familial hypercholanemia (FHCA) [MIM:607748]: A disorder
characterized by elevated serum bile acid concentrations, itching,
and fat malabsorption. {ECO:0000269|PubMed:12704386}. Note=The
disease may be caused by mutations affecting distinct genetic
loci, including the gene represented in this entry.
-!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
{ECO:0000305}.
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EMBL; L34081; AAC37550.1; -; mRNA.
EMBL; CR541918; CAG46716.1; -; mRNA.
EMBL; AL359893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471105; EAW58943.1; -; Genomic_DNA.
EMBL; BC009567; AAH09567.1; -; mRNA.
EMBL; BC107424; AAI07425.1; -; mRNA.
CCDS; CCDS6752.1; -.
PIR; A53965; A53965.
RefSeq; NP_001121082.1; NM_001127610.1.
RefSeq; NP_001692.1; NM_001701.3.
SMR; Q14032; -.
BioGrid; 107046; 5.
IntAct; Q14032; 22.
MINT; Q14032; -.
STRING; 9606.ENSP00000259407; -.
DrugBank; DB00145; Glycine.
DrugBank; DB05990; Obeticholic acid.
DrugBank; DB01956; Taurine.
SwissLipids; SLP:000001309; -.
ESTHER; human-BAAT; Acyl-CoA_Thioesterase.
MEROPS; S09.A50; -.
CarbonylDB; Q14032; -.
iPTMnet; Q14032; -.
PhosphoSitePlus; Q14032; -.
BioMuta; BAAT; -.
DMDM; 74739811; -.
MassIVE; Q14032; -.
MaxQB; Q14032; -.
PaxDb; Q14032; -.
PeptideAtlas; Q14032; -.
PRIDE; Q14032; -.
ProteomicsDB; 59802; -.
DNASU; 570; -.
Ensembl; ENST00000259407; ENSP00000259407; ENSG00000136881.
Ensembl; ENST00000395051; ENSP00000378491; ENSG00000136881.
Ensembl; ENST00000621712; ENSP00000484063; ENSG00000276559.
GeneID; 570; -.
KEGG; hsa:570; -.
UCSC; uc010mtd.3; human.
CTD; 570; -.
DisGeNET; 570; -.
GeneCards; BAAT; -.
HGNC; HGNC:932; BAAT.
HPA; HPA021251; -.
HPA; HPA021330; -.
MalaCards; BAAT; -.
MIM; 602938; gene.
MIM; 607748; phenotype.
neXtProt; NX_Q14032; -.
OpenTargets; ENSG00000136881; -.
Orphanet; 238475; Familial hypercholanemia.
PharmGKB; PA25231; -.
eggNOG; ENOG410II3X; Eukaryota.
eggNOG; COG1073; LUCA.
GeneTree; ENSGT00950000182784; -.
HOGENOM; HOG000116219; -.
InParanoid; Q14032; -.
KO; K00659; -.
OMA; TDDGSWP; -.
OrthoDB; 1260385at2759; -.
PhylomeDB; Q14032; -.
TreeFam; TF314911; -.
BRENDA; 2.3.1.65; 2681.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-9033241; Peroxisomal protein import.
SABIO-RK; Q14032; -.
GeneWiki; BAAT; -.
GenomeRNAi; 570; -.
Pharos; Q14032; -.
PRO; PR:Q14032; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136881; Expressed in 54 organ(s), highest expression level in right lobe of liver.
Genevisible; Q14032; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0047963; F:glycine N-choloyltransferase activity; IDA:UniProtKB.
GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016410; F:N-acyltransferase activity; IDA:MGI.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016746; F:transferase activity, transferring acyl groups; TAS:Reactome.
GO; GO:0052817; F:very long chain acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
GO; GO:0002152; P:bile acid conjugation; IDA:UniProtKB.
GO; GO:0008206; P:bile acid metabolic process; TAS:Reactome.
GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
GO; GO:0006544; P:glycine metabolic process; IDA:UniProtKB.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0019530; P:taurine metabolic process; IDA:UniProtKB.
Gene3D; 2.60.40.2240; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
InterPro; IPR014940; BAAT_C.
InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
InterPro; IPR042490; Thio_Ohase/BAAT_N.
Pfam; PF08840; BAAT_C; 1.
Pfam; PF04775; Bile_Hydr_Trans; 1.
PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Fatty acid metabolism;
Hydrolase; Lipid metabolism; Peroxisome; Phosphoprotein; Polymorphism;
Reference proteome; Serine esterase; Transferase.
CHAIN 1 418 Bile acid-CoA:amino acid N-
acyltransferase.
/FTId=PRO_0000202159.
ACT_SITE 235 235 Charge relay system. {ECO:0000305}.
ACT_SITE 328 328 Charge relay system. {ECO:0000305}.
ACT_SITE 362 362 Charge relay system. {ECO:0000305}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:Q63276}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:Q63276}.
VARIANT 20 20 R -> Q (in dbSNP:rs1572983).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_052303.
VARIANT 76 76 M -> V (in FHCA; dbSNP:rs28937579).
{ECO:0000269|PubMed:12704386}.
/FTId=VAR_023737.
MUTAGEN 235 235 C->A: Abolishes N-acyltransferase
activity. {ECO:0000269|PubMed:12239217,
ECO:0000269|PubMed:12810727}.
MUTAGEN 235 235 C->S: Lowers N-acyltransferase activity;
enhanced thioesterase activity presumably
dependent on the formation of a bile
acid-enzyme covalent intermediate via a
thioester bond.
{ECO:0000269|PubMed:12239217,
ECO:0000269|PubMed:12810727}.
MUTAGEN 328 328 D->A: Abolishes N-acyltransferase
activity. {ECO:0000269|PubMed:12239217,
ECO:0000269|PubMed:12810727}.
MUTAGEN 362 362 H->A: Abolishes N-acyltransferase
activity. {ECO:0000269|PubMed:12239217}.
MUTAGEN 362 362 H->Q: Abolishes N-acyltransferase
activity. {ECO:0000269|PubMed:12810727}.
MUTAGEN 372 372 C->A: Retains N-acyltransferase activity.
{ECO:0000269|PubMed:12810727}.
MUTAGEN 417 417 Q->K: Translocation to peroxisomes.
{ECO:0000269|PubMed:12810727}.
SEQUENCE 418 AA; 46299 MW; 4B290BAEE97F23B3 CRC64;
MIQLTATPVS ALVDEPVHIR ATGLIPFQMV SFQASLEDEN GDMFYSQAHY RANEFGEVDL
NHASSLGGDY MGVHPMGLFW SLKPEKLLTR LLKRDVMNRP FQVQVKLYDL ELIVNNKVAS
APKASLTLER WYVAPGVTRI KVREGRLRGA LFLPPGEGLF PGVIDLFGGL GGLLEFRASL
LASRGFASLA LAYHNYEDLP RKPEVTDLEY FEEAANFLLR HPKVFGSGVG VVSVCQGVQI
GLSMAIYLKQ VTATVLINGT NFPFGIPQVY HGQIHQPLPH SAQLISTNAL GLLELYRTFE
TTQVGASQYL FPIEEAQGQF LFIVGEGDKT INSKAHAEQA IGQLKRHGKN NWTLLSYPGA
GHLIEPPYSP LCCASTTHDL RLHWGGEVIP HAAAQEHAWK EIQRFLRKHL IPDVTSQL


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WP1996: Linoleate Biosynthesis
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WP521: amino acid conjugation of benzoic acid
WP1577: amino acid conjugation of benzoic acid
WP2102: Fatty acid metabolism
WP91: Fatty acid oxidation
WP137: Fatty Acid Biosynthesis, Initial Steps
WP662: Amino Acid metabolism
WP336: Fatty Acid Biosynthesis
WP1237: Fatty Acid Beta Oxidation
WP498: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP989: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1020: Fatty Acid Biosynthesis
WP506: Fatty Acid Beta Oxidation 1
WP1788: Bile acid and bile salt metabolism
WP368: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP763: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP126: Fatty Acid Beta Oxidation 1
WP1648: Fatty acid metabolism
WP39: Fatty Acid Beta Oxidation 1
WP825: Fatty Acid Beta Oxidation
WP16: Fatty Acid Elongation, Unsaturated
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Related Genes :
[Baat] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[BAAT] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[Baat] Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Kan-1) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
[SLC27A5 ACSB ACSVL6 FACVL3 FATP5] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Fatty-acid-coenzyme A ligase, very long-chain 3) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase homolog 2) (VLCS-H2) (VLCSH2) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)
[Slc27a5 Acsb Acsvl6 Fatp5 Vlacsr] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)
[Slc27a5 Acsb Fatp5 Vlacsr] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON66_15955 BON93_14110 BUE81_10670 BvCms12BK_01457 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP008_02510 BvCmsKSP015_01352 BvCmsKSP036_04668 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSNP027_04914 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP039_03266 BvCmsNSP047_03567 BvCmsNSP078_03451 BvCmsSINP011_04162 BvCmsSIP006_05510 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9025_17620 C9083_21590 C9212_13125 C9Y80_10480 C9Y95_17520 C9Z12_18550 CDL37_00765 CI694_25210 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DEN89_24995 DEO11_07425 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 EVY21_22520 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[GLYAT ACGNAT CAT GAT] Glycine N-acyltransferase (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase) (AAc) (Aralkyl acyl-CoA N-acyltransferase) (Aralkyl acyl-CoA:amino acid N-acyltransferase) (Benzoyl-coenzyme A:glycine N-acyltransferase) (Glycine N-benzoyltransferase) (EC 2.3.1.71) (HRP-1(CLP))
[Acsl1 Acsl2 Facl2] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Phytanate--CoA ligase) (EC 6.2.1.24)
[ACSL1 FACL1 FACL2 LACS LACS1 LACS2] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Acyl-CoA synthetase 1) (ACS1) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain acyl-CoA synthetase 2) (LACS 2) (Long-chain fatty acid-CoA ligase 2) (Palmitoyl-CoA ligase 1) (Palmitoyl-CoA ligase 2) (Phytanate--CoA ligase) (EC 6.2.1.24)
[Acot1 Cte1] Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2)
[Acsl1 Acs1 Acsl2 Facl2] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain-fatty-acid--CoA ligase, liver isozyme) (Phytanate--CoA ligase) (EC 6.2.1.24)
[ELOVL5 ELOVL2 PRO0530] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Fatty acid elongase 1) (hELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)
[Gpat4 Agpat6 Tsarg7] Glycerol-3-phosphate acyltransferase 4 (GPAT4) (EC 2.3.1.15) (1-acylglycerol-3-phosphate O-acyltransferase 6) (1-AGP acyltransferase 6) (1-AGPAT 6) (Acyl-CoA:glycerol-3-phosphate acyltransferase 4) (Lysophosphatidic acid acyltransferase zeta) (LPAAT-zeta) (Testis spermatogenesis apoptosis-related protein 7)
[Acsl3 Acs3 Facl3] Long-chain-fatty-acid--CoA ligase 3 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Brain acyl-CoA synthetase II) (Long-chain acyl-CoA synthetase 3) (LACS 3)
[ACSL1 FACL1 LACS1] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Palmitoyl-CoA ligase) (Phytanate--CoA ligase) (EC 6.2.1.24)
[ELOVL4] Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4)
[Elovl4] Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4)
[Acot8 Pte1] Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.1) (EC 3.1.2.11) (EC 3.1.2.2) (EC 3.1.2.3) (EC 3.1.2.5) (Choloyl-coenzyme A thioesterase) (EC 3.1.2.27) (Peroxisomal acyl-CoA thioesterase 2) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1)
[FAA2 FAM1 YER015W] Long-chain-fatty-acid--CoA ligase 2 (EC 6.2.1.3) (Fatty acid activator 2) (Long-chain acyl-CoA synthetase 2)
[Elovl7] Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
[ELOVL5 QflA-11914] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)
[ACSL4 ACS4 FACL4 LACS4] Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 4) (LACS 4)
[ACSL5 ACS5 FACL5 UNQ633/PRO1250] Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 5) (LACS 5)
[ELOVL7] Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
[fadD13 Rv3089] Long-chain-fatty-acid--CoA ligase FadD13 (EC 6.2.1.3) (Fatty acyl-CoA ligase) (FACL) (FACL13) (Fatty acyl-CoA synthetase) (ACS) (FACS) (Very-long-chain fatty-acyl-CoA synthetase) (ACSVL)
[ACSBG2 BGR UNQ2443/PRO5005] Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Arachidonate--CoA ligase ACSBG2) (EC 6.2.1.15) (Bubblegum-related protein) (PRTD-NY3)
[Acot1 Cte1] Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (LACH2) (ACH2) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2)
[fadD oldD b1805 JW1794] Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain acyl-CoA synthetase) (Acyl-CoA synthetase)
[Awat2 Dgat2l4 Ws] Acyl-CoA wax alcohol acyltransferase 2 (EC 2.3.1.75) (11-cis-specific retinyl-ester synthase) (11-cis-RE-synthase) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 2-like protein 4) (Long-chain-alcohol O-fatty-acyltransferase 2) (Wax synthase) (mWS)

Bibliography :