| Literature DB >> 666738 |
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.Entities:
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Year: 1978 PMID: 666738 PMCID: PMC1184029 DOI: 10.1042/bj1710799
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857