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Colivirus-T3-coded S-adenosylmethionine hydrolase.

N Spoerel, P Herrlich

    European Journal of Biochemistry
    |April 2, 1979
    PubMed
    Summary
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    Bacteriophage T3 produces an S-adenosylmethionine hydrolase enzyme. This enzyme, crucial for overcoming host restriction, was purified and characterized in two distinct forms.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Virology

    Background:

    • Bacteriophage T3 encodes an enzyme that hydrolyzes S-adenosylmethionine (SAM).
    • This SAM hydrolase is notable for its unique enzymatic activity and its role in circumventing host restriction mechanisms.

    Purpose of the Study:

    • To purify and characterize the S-adenosylmethionine hydrolase induced by bacteriophage T3.
    • To investigate the enzyme's properties and its potential relationship with host restriction systems.

    Main Methods:

    • Purification of S-adenosylmethionine hydrolase to homogeneity using affinity chromatography on S-adenosylhomocysteine-Sepharose.
    • Characterization of the enzyme's molecular weight and subunit composition.

    Main Results:

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    • The enzyme was purified and found to exist in two forms: Form A (viral peptide chain only, MW 17,000) and Form B (viral peptide plus a host subunit, MW 49,000).
    • The host subunit in Form B did not affect S-adenosylmethionine cleavage activity in vitro.
    • No direct link between the host subunit and the host-restriction system was identified.

    Conclusions:

    • Bacteriophage T3 S-adenosylmethionine hydrolase exists in two forms with distinct subunit compositions.
    • The host-associated subunit does not influence the enzyme's catalytic activity in vitro and its role in host restriction remains unclear.