Matern H, Bolz R, Marschall H U, Sjövall J, Matern S
Department of Internal Medicine III, Aachen University of Technology, FRG.
FEBS Lett. 1990 Sep 17;270(1-2):11-4. doi: 10.1016/0014-5793(90)81223-b.
Bile acid N-acetylglucosaminyltransferase activity has been identified in microsomes from human liver and kidney. In both organs the transferases required UDP-N-acetylglucosamine as sugar donor and were mainly active towards ursodeoxycholic acid. Minor activities were observed towards amidated ursodeoxycholic, hyodeoxycholic and beta-muricholic acids. No N-acetylglucosaminidation was detectable with the major primary and secondary bile acids suggesting a specific requirement of the enzymes for bile acids containing 7 beta-or 6 alpha-hydroxyl groups. Kinetic parameters and other catalytic properties of liver and kidney microsomal N-acetylglucosaminyltransferase activities towards ursodeoxycholic acid are described.
在人肝脏和肾脏的微粒体中已鉴定出胆汁酸N-乙酰葡糖胺基转移酶活性。在这两个器官中，转移酶都需要UDP-N-乙酰葡糖胺作为糖供体，并且主要对熊去氧胆酸具有活性。对酰胺化熊去氧胆酸、猪去氧胆酸和β-鼠胆酸观察到较小的活性。对于主要的初级和次级胆汁酸，未检测到N-乙酰葡糖胺化，这表明这些酶对含有7β-或6α-羟基的胆汁酸有特定需求。本文描述了肝脏和肾脏微粒体N-乙酰葡糖胺基转移酶对熊去氧胆酸的动力学参数和其他催化特性。
