Publications

• Characterization of a defect in the pathway for converting 5'-deoxy-5'-methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma.

  Ghoda L.Y., Savarese T.M., Dexter D.L., Parks R.E. Jr., Trackman P.C., Abeles R.H.

  5'-Deoxy-5'-methylthioadenosine (methylthioadenosine) is cleaved to adenine and 5-methylthioribose-1-phosphate (methylthioribose-1-P). Methylthioribose-1-P is converted to 2-keto-4-methylthiobutyrate ( ketomethylthiobutyrate ) which is transaminated to methionine. We report that one subline of a h ... >> More

  5'-Deoxy-5'-methylthioadenosine (methylthioadenosine) is cleaved to adenine and 5-methylthioribose-1-phosphate (methylthioribose-1-P). Methylthioribose-1-P is converted to 2-keto-4-methylthiobutyrate ( ketomethylthiobutyrate ) which is transaminated to methionine. We report that one subline of a heterogeneous human colon carcinoma, DLD-1 Clone D, only forms methylthioribose-1-P from methylthioadenosine or 5'-deoxy-5'-methylthioinosine (methylthioinosine), a deaminated derivative of methylthioadenosine, whereas Clone A converts methylthioadenosine and methylthioinosine to methionine, as shown by growth studies in culture of Clone A and Clone D cells and radioactive studies utilizing [methyl-14C]methylthioadenosine or [methyl-14C]methylthioinosine in the presence of extracts of these cells lines. To characterize this defect, we utilized three protein fractions isolated from rat liver which together convert methylthioribose-1-P to ketomethylthiobutyrate . Addition of only Fraction A to Clone D sonicates restores its ability to convert methylthioadenosine to methionine. This fraction is responsible for converting methylthioribose-1-P to 5-methylthioribulose -1-phosphate; radioactive studies confirm this observation. Thus, Clone D is deficient in an enzyme contained in Fraction A; this represents a qualitative biochemical difference between the two clones derived from a single human tumor. << Less

  J Biol Chem 259:6715-6719(1984) [PubMed] [EuropePMC]

• Methionine synthesis from 5'-S-Methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S methylthioribulose.

  Trackman P.C., Abeles R.H.

  5'-S-Methylthioadenosine is converted to methionine in mammalian systems, microorganisms and plants. 5'-S-Methylthioadenosine is first converted to 1-phospho-5-S-methylthioribofuranoside (1-PMTR) which is then converted to 2-keto-4-S-methylthiobutyrate, the precursor of methionine. We have now inv ... >> More

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

  J Biol Chem 258:6717-6720(1983) [PubMed] [EuropePMC]

• Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae.

  Furfine E.S., Abeles R.H.

  Extracts of Klebsiella pneumoniae oxidatively convert 1-phospho-5-S-methylthioribose (1-PMTR) to alpha-keto-gamma-methylthiobutyrate, a precursor of methionine, and to S-methylthiopropionate and formate. One equivalent of formate is produced per equivalent of alpha-keto-gamma-methylthiobutyrate an ... >> More

  Extracts of Klebsiella pneumoniae oxidatively convert 1-phospho-5-S-methylthioribose (1-PMTR) to alpha-keto-gamma-methylthiobutyrate, a precursor of methionine, and to S-methylthiopropionate and formate. One equivalent of formate is produced per equivalent of alpha-keto-gamma-methylthiobutyrate and two equivalents of formate per equivalent of methylthiopropionate. Two compounds were identified as intermediates in this reaction sequence: 1-phospho-5-S-methylthioribulose (1-PMT-ribulose) and 1-phospho-2,3-diketo-5-S-methylpentane. The enzyme, 1-PMTR isomerase, which converts 1-PMTR to 1-PMT-ribulose was highly purified. In addition, a protein fraction was isolated which converts 1-PMT-ribulose to the phosphodiketone. A second protein fraction was isolated that converts the phosphodiketone to an intermediate which has not been isolated so far. This intermediate is oxidatively converted to alpha-keto-gamma-methylthiobutyrate and S-methylthiopropionate by a third protein fraction. Methylthiopropionate is not derived from free alpha-keto-gamma-methylthiobutyrate. << Less

  J Biol Chem 263:9598-9606(1988) [PubMed] [EuropePMC]

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