Advances in Enzymology and Related Areas of Molecular by Alton Meister

By Alton Meister

Keeps the authoritative sequence that stories learn into enzymology and similar parts of molecular biology. provides six papers by way of best experts.

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5 and 3 hr, with adequate cosubstrate and ~-[@-~H]serine or ~-[@-~H]cysteine, the specific radioactivity of the reaction end-products was the same as in the initial amino-substrates, and no tritium appeared in the solvent 52 ALEXANDER E. BRAUNSTEIN AND ELIZABETH v. GORYACHENKOVA water. The same lyases were incubated with nonlabeled L-serine and cosubstrate in 3H2'80 ("0was 32% of the total oxygen content). 5 atom-% of H had been labeled (evidently in the a-position), which required 3 h incubation with serine sulfhydrase and 24 h with cysteine lyase, analysis in a photoionization mass-spectrometer failed to reveal uptake of l8O in the hydroxyl group of serine (within the 1% sensitivity limits for detection).

9 in ref. 112). E complexes of other PLP-enzymes, for example, transaminases, amino acid decarboxylases, serine hydroxymethylase, and others (4,12,14, 15,110). Such peaks, indicating an extended conjugated mystem, 50 z ALEXANDER E. BRAUNSTEIN AND ELIZABETH V. GORYACHENKOVA 100 -A 3 L f 60 20 0 2 Tlms l h ) 4 I I Time (h Figure 11. Incorporation by cysteine lyase (A) and serine sulfhydrase (B) of 3H into amino acid substrates and reaction products (27). Relative specific radioactivities (percentage of specific radioactivity of 'HHO in incubation medium) calculated for a-H atom in L-serine (l), L-cysteine (2), and the preplacement product Shydroxyethyl-cysteine (3 from cysteine, and 3a from serine) in assay samples with cysteine lyase (A) and serine sulhydrase (B).

Values; M, thesis is the cause of the human hereditary metabolic error known as homocystinuria (see refs. 53a-56). The allelozymic common derivation of serine sulfhydrase and cystathionine P-synthase was further confirmed by Pieniazek et al. (51). , refs. 53a-56). Soda, Tanaka et al. 2). * The same authors (1 17) discovered a strictly specific PLP-dependent hepatic lyase, selenocysteine lyase, which catalyzes the reductive cleavage of 3-selenoalanine to HzSe + L-Ala, using dithiothreitol or a second molecule of selenoalanine as the reductant.

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