| Literature DB >> 21305 |
Abstract
Bacteriophage T5 induced a deoxynucleoside 5'-monophosphatase during its infection of Escherichia coli. The enzyme was purified about 100-fold. It was clearly distinct from the host 5'-nucleotidase activity in its physical characteristics and substrate specificity. The enzyme was active on deoxynucleoside 5'-monophosphates but was not active as a phosphatase on ribonucleotides, deoxynucleoside 5'-triphosphates, deoxynucleoside 3'-monophosphates, or deoxyoligonucleotides. Furthermore, it did not have oligonucleotidase or exonuclease activity. The enzyme could exist in multimeric form but had a monomer molecular weight of about 25,000.Entities:
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Year: 1977 PMID: 21305 PMCID: PMC515975 DOI: 10.1128/JVI.24.2.635-641.1977
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103