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Colivirus-T3-coded S-adenosylmethionine hydrolase.

N Spoerel·P Herrlich
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Abstract

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 17,000. Form B contains, in addition, a host subunit with a molecular weight of 49,000. The host subunit does not modify S-adenosylmethionine cleavage in vitro and no apparent relationship to the host-restriction system could be detected.

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Bacterial ProteinsChemical PhenomenaChemistryChromatography, AffinityColiphagesEscherichia coliHydrolasesImmunodiffusionMolecular WeightMutationS-AdenosylmethionineJournal Article

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BibTeXRIS

N Spoerel, P Herrlich. 1979-04-02. Colivirus-T3-coded S-adenosylmethionine hydrolase.. https://doi.org/10.1111/j.1432-1033.1979.tb12957.x

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