Title : Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase.

Pub. Date : 1988 Aug 25

PMID : 3042777






3 Functional Relationships(s)
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Protein Name
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1 Both this toxin-resistant EF-2 and its modifying enzyme have been partially purified and evidence is presented that the modifying enzyme is a specific S-adenosylmethionine:EF-2 methyltransferase. S-Adenosylmethionine elongation factor 2 Saccharomyces cerevisiae S288C
2 Both this toxin-resistant EF-2 and its modifying enzyme have been partially purified and evidence is presented that the modifying enzyme is a specific S-adenosylmethionine:EF-2 methyltransferase. S-Adenosylmethionine elongation factor 2 Saccharomyces cerevisiae S288C
3 We conclude that the S-adenosylmethionine:EF-2 methyltransferase adds at least the last two of the three methyl groups present in diphthine and that this modification is sufficient to create diphtheria toxin sensitivity. S-Adenosylmethionine elongation factor 2 Saccharomyces cerevisiae S288C