Affiliation:
1. Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104
Abstract
The dCTP deaminase induced by
Bacillus subtilis
bacteriophage PBS2, whose DNA contains uracil instead of thymine, requires metal ion and thiol activators and has a molecular weight of 125,000. The enzyme displays sigmoidal substrate saturation kinetics and inhibition by dUTP, consistent with the deaminase's proposed role of providing balanced levels of dUTP and dCTP for PBS2 uracil-DNA synthesis.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Cited by
11 articles.
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