Terminal methylation reactions in Saccharomyces cerevisiae Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/k930c1114

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  • A cell-free system for assessing the role of S-adenosyl-methionine in the methylation of homocysteine deriving the methyl group from serine has been developed. No role for S-adenosyl-methionine could be shown in the in vitro reaction The enzyme serine transhydroxymethylase has been studied in crude and partially purified cell extracts. Evidence was obtained that this activity provides the one carbon fragment for the methylation of homocysteine. The activity was found to be inhibited by S-adenosyl-methionine and methionine. When cells are cultured in excess methionine, the methylation of homocysteine in cell-free extracts is not affected. Serine trans-hydroxymethylase is repressed to a limited degree. The enzyme S-adenosylmethionine:homocysteine methyltransferase is induced under these conditions.
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  • File scanned at 300 ppi using ScandAll PRO 1.8.1 on a Fi-6670 in PDF format. CVista PdfCompressor 5.0 was used for pdf compression and textual OCR.
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  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2014-03-12T14:53:38Z (GMT) No. of bitstreams: 1 BotsfordJamesL1968.pdf: 1103359 bytes, checksum: ffef78ea5c2ce0a57dbd39be71081533 (MD5)
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