Methionine synthesis from 5'-S-Methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S methylthioribulose.
作者： P C Trackman , R H Abeles
DOI: 10.1016/S0021-9258(18)32277-4
关键词:
摘要: 5'-S-Methylthioadenosine is converted to methionine in mammalian systems, microorganisms and plants. first 1-phospho-5-S-methylthioribofuranoside (1-PMTR) which then 2-keto-4-S-methylthiobutyrate, the precursor of methionine. We have now investigated conversion 1-PMTR keto acid. This requires at least three protein fractions designated A, B, C. Fraction A catalyzes an isomerization form 1-phospho-5-S-methylthioribulose. The identification this compound based part on products obtained after NaIO4 oxidation, i.e. S-methylthioacetaldehyde, formate, phosphoglycolic When B are added 1-PMTR, two additional compounds, II III, were detected. No O2 was consumed formation compounds III. These are, therefore, oxidation state 5-S-methylthioribose. Compound phosphorylated as evidenced by its electrophoretic behavior before alkaline phosphatase treatment. Addition fraction C III leads consumption these 2-keto-4-S-methylthiobutyrate. Thus, precursors not been fully characterized.
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