ArticleThe Biochemical journal1994
Purification and some properties of an IMP-specific 5'-nucleotidase from yeast.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- Nitric oxide plays a role as second messenger in the ultraviolet-B irradiated green alga Chlorella pyrenoidosa.Folia microbiologica · 2010Article
- The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5'-nucleotidase.BMC biochemistry · 2003Article
- YLR209c encodes Saccharomyces cerevisiae purine nucleoside phosphorylase.Journal of bacteriology · 2001Article
- Ecto-5'-nucleotidase from a human colon adenocarcinoma cell line. Correlation between enzyme activity and levels in intact cells.Molecular and cellular biochemistry · 1998Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An IMP-hydrolysing enzyme was purified to homogeneity from yeast extract. It was a soluble protein with an apparent molecular mass of 220 kDa, with a subunit molecular mass of 55 kDa. It was highly specific for IMP, and there was virtually no detectable activity with the other purine and pyrimidine nucleotides tested, including AMP and dIMP. The enzyme had a pH optimum of 6.0-6.5. Its activity was absolutely dependent on bivalent metal salts: Mg2+ was most potent, followed by Co2+ and Mn2+. The velocity/substrate-concentration plot of the enzyme was slightly sigmoidal (h = 1.7) and the s0.5 was 0.4 mM. ATP stimulated the enzyme by decreasing both h and s0.5. Diadenosine tetraphosphate stimulated the enzyme as effectively as ATP. Although the properties of the enzyme are similar to those of the IMP/GMP 5'-nucleotidase identified in various animals [Itoh (1993) Comp. Biochem. Physiol. 105B, 13-19], the substrate specificity of the former was much more strict than the latter.
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Registered trials
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