Purification and some properties of NAD-degrading purine nucleosidase from Aspergillus niger
- 1 May 1978
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 56 (5) , 345-348
- https://doi.org/10.1139/o78-054
Abstract
An enzyme which degrades NAD at the adenine–ribose linkage has been purified from the mycelial extract of Aspergillus niger. NADP, deamido-NAD, and purine nucleosides and nucleotides were also susceptible to the hydrolytic cleavage. Pyrimidine- and nicotinamide–ribose linkages were not attacked. The substrate specificity showed that the enzyme may be classified as a N-ribosyl-purine ribohydrolase (EC 3.2.2.1). The enzyme had a maximum activity in the pH range of 4.0–4.5 toward NAD. The Km values for NAD, 5′-AMP, and inosine were 3.0, 2.9, and 1.6 mM respectively.This publication has 2 references indexed in Scilit:
- Studies of the enzymes involved in nicotinamide adenine dinucleotide metabolism in Aspergillus nigerBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951