Effect of different compounds on 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver.
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.
D000111:Acetylcysteine / Q000494:pharmacology; D000581:Amidohydrolases / Q000037:antagonists & inhibitors*; D000596:Amino Acids / Q000494:pharmacology; D001227:Aspartylglucosylaminase / Q000037:antagonists & inhibitors*; D002074:Butanones / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology*
D000596:Amino Acids; D002074:Butanones; D000581:Amidohydrolases; D001227:Aspartylglucosylaminase; D000111:Acetylcysteine