Open AccessColivirus‐T3‐Coded S ‐Adenosylmethionine Hydrolase
Author(s) -
SPOEREL Nikolaus,
HERRLICH Peter
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb12957.x
Subject(s) - hydrolase , computer science , chemistry , biochemistry , enzyme
Bacteriophage T3 induces an enzyme activity which hydrolyzes S ‐adenosylmethionine. This S ‐adenosylmethionine hydrolase is interesting, not only because of its unique activity, but also because the protein has to overcome host restriction [F. W. Studier and N. R. Movva (1976) J. Virol. 19 , 136–145]. S ‐Adenosylmethionine hydrolase was purified to homogeneity using affinity chromatography on S ‐adenosylhomocysteine‐Sepharose. The enzyme occurs in two forms, A and B. Form A consists of the viral peptide chain only; its native and subunit molecular weight is 17000. Form B contains, in addition, a host subunit with a molecular weight of 49000. The host subunit does not modify S ‐adenosylmethionine cleavage in vitro and no apparent relationship to the host‐restriction system could be detected.