Bile acid coenzyme A:: Amino acid N-acyltransferase in the amino acid conjugation of bile acids

被引:20
作者
Shonsey, EM [1 ]
Sfakianos, M
Johnson, M
He, DN
Falany, CN
Falany, J
Merkler, DJ
Barnes, S
机构
[1] Univ Alabama, Dept Pharmacol & Toxicol, Birmingham, AL 35294 USA
[2] Yale Univ, Sch Med, Dept Mol Biophys & Biochem, New Haven, CT 06510 USA
[3] Univ Alabama, Dept Pathol, Birmingham, AL 35294 USA
[4] Univ S Florida, Dept Chem, Tampa, FL 33620 USA
来源
PHASE II CONJUGATION ENZYMES AND TRANSPORT SYSTEMS | 2005年 / 400卷
关键词
D O I
10.1016/S0076-6879(05)00022-4
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Bile acids are converted to their glycine and taurine N-acyl amidates by enzymes in the liver in a two-step process. This increases their aqueous solubility, particularly in the acidic environment of the upper part of the small intestine. Bile acid coenzyme A (CoA) thioesters synthesized by bile acid CoA ligase (see Shonsey et al., 2005) are substrates of bile acid CoA: amino acid N-acyltransferases (BAT) in the formation of bile acid N-acyl amidates. This chapter describes the methods used to purify BAT from human liver, to isolate and clone cDNAs encoding BAT from human, mouse, and rat liver cDNA libraries, the expression of BAT, the assays used to measure BAT activity, and the chemical syntheses of bile acid N-acylamidates. In addition, an enzyme that catalyzes further metabolism of glycine-conjugated bile acids is described.
引用
收藏
页码:374 / 394
页数:21
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