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| {{enzyme
| | My name is Courtney Etienne. I life in Fort Saskatchewan (Canada).<br><br>my webpage ... [http://generaldatamedical.com/what-is-the-benefit-of-an-electronic-health-record/ Electronic Health Record] |
| | Name = glycine N-choloyltransferase
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| | EC_number = 2.3.1.65
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| | CAS_number = 74506-32-4
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| | IUBMB_EC_number = 2/3/1/65
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| | GO_code = 0047963
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| In [[enzymology]], a '''bile acid-CoA:amino acid N-acyltransferase''' ({{EC number|2.3.1.65}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :choloyl-CoA + glycine <math>\rightleftharpoons</math> CoA + glycocholate
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[choloyl-CoA]] and [[glycine]], whereas its two [[product (chemistry)|products]] are [[coenzyme A|CoA]] and [[glycocholate]].
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| This enzyme belongs to the family of [[transferase]]s, specifically those [[acyltransferase]]s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is '''choloyl-CoA:glycine N-choloyltransferase'''. Other names in common use include '''glycine-taurine N-acyltransferase''', '''amino acid N-choloyltransferase''', '''BAT''', '''glycine N-choloyltransferase''', '''BACAT''', '''cholyl-CoA glycine-taurine N-acyltransferase''', and '''cholyl-CoA:taurine N-acyltransferase'''. This enzyme participates in [[bile acid biosynthesis]] and [[taurine and hypotaurine metabolism]].
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = Czuba B, Vessey DA | date = 1980 | title = Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver | journal = J. Biol. Chem. | volume = 255 | pages = 5296–9 | pmid = 7372637 | issue = 11 }}
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| * {{cite journal | author = Jordan TW, Lee R and Lim WC | date = 1980 | title = Isoelectric focussing of soluble and particulate benzoyl-CoA and cholyl-CoA:amino acid N-acyltransferases from rat liver | journal = Biochem. Int. | volume = 1 | pages = 325–330 }}
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| * {{cite journal | author = Vessey DA | date = 1979 | title = The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver | journal = J. Biol. Chem. | volume = 254 | pages = 2059–63 | pmid = 422567 | issue = 6 }}
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| * {{cite journal | author = Johnson MR, Barnes S, Kwakye JB, Diasio RB | date = 1991 | title = Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver | journal = J. Biol. Chem. | volume = 266 | pages = 10227–33 | pmid = 2037576 | issue = 16 }}
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| * {{cite journal | author = Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S | date = 2002 | title = Molecular cloning and expression of rat liver bile acid CoA ligase | journal = J. Lipid. Res. | volume = 43 | pages = 2062–71 | pmid = 12454267 | doi = 10.1194/jlr.M200260-JLR200 | issue = 12 }}
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| * {{cite journal | author = He D, Barnes S, Falany CN | date = 2003 | title = Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization | journal = J. Lipid. Res. | volume = 44 | pages = 2242–9 | pmid = 12951368 | doi = 10.1194/jlr.M300128-JLR200 | issue = 12 }}
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| * {{cite journal | author = O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE | date = 2003 | title = The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine | journal = J. Biol. Chem. | volume = 278 | pages = 34237–44 | pmid = 12810727 | doi = 10.1074/jbc.M300987200 | issue = 36 }}
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| {{transferase-stub}}
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| [[Category:EC 2.3.1]]
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| [[Category:Enzymes of unknown structure]]
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My name is Courtney Etienne. I life in Fort Saskatchewan (Canada).
my webpage ... Electronic Health Record