Colivirus-T3-coded S-adenosylmethionine hydrolase.
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.
D001426:Bacterial Proteins / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D003090:Coliphages; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006867:Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D005779:Immunodiffusion; D008970:Molecular Weight; D009154:Mutation; D012436:S-Adenosylmethionine / Q000378:metabolism*
D001426:Bacterial Proteins; D012436:S-Adenosylmethionine; D006867:Hydrolases; C019614:adenosylmethionine hydrolase