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Journal of Virology
HB-3, a temperate bacteriophage of Streptococcus pneumoniae, synthesizes its own murein hydrolase activity when multiplying on cultures of pneumococcus. The enzyme (HBL) was purified and biochemically characterized as an N-acetylmuramoyl-L-alanine amidase of 36,000 daltons, and a 2.1-kilobase Dral fragment containing the lysin gene (hbl) was cloned and expressed in Escherichia coli. Our results demonstrated that the primary product of the hbl gene is a form with low enzyme activity that can bedoi:10.1128/jvi.64.1.137-142.1990 fatcat:d3hvysxqg5bd3ju7fynww4wlgi