Effect of different compounds on 1-aspartamido-β-N-acetylglucosamine amidohydrolase from human liver-Reference-Cited by-同舟云学术

Effect of different compounds on 1-aspartamido-β-N-acetylglucosamine amidohydrolase from human liver

Published:1978-06-01 Issue:3 Volume:171 Page:799-802
ISSN:0264-6021
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Dugal B

Abstract

The effect of varous compounds on 1-aspartamido-beta-N-acetylglucosamine amidohydrolase (aspartylglucosylaminase, EC 3.5.1.26) was studied. N-Acetylcysteine inhibited the nezyme non-competitively (Ki 3.2 mM), whereas 3-hydroxybutanone inhibited competitively (Ki 4.1 mM). Methionine, isoleucine and cystathionine apparently enhanced the enzyme activity. The enzyme had a mol. wt. of 63000 as determined by gel filtration. The present studies differentiate between the aspartylglucosylaminase from human liver and that obtained from various other sources.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://portlandpress.com/biochemj/article-pdf/171/3/799/625805/bj1710799.pdf

Cited by 8 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Carbohydrate-Processing Enzymes of the Lysosome;Advances in Carbohydrate Chemistry and Biochemistry;2016

2. Glycolipid and Glycoprotein Degradation;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

3. Glycosylasparaginase Inhibition Studies: Competitive Inhibitors, Transition State Mimics, Noncompetitive Inhibitors;Journal of Enzyme Inhibition;2001-01

4. Purification and structure of human liver aspartylglucosaminidase;Biochemical Journal;1992-12-15

5. Spectrum of mutations in aspartylglucosaminuria.;Proceedings of the National Academy of Sciences;1991-12-15