By Alton Meister
Keeps the authoritative sequence that reports study into enzymology and similar parts of molecular biology. offers six papers by means of major specialists.
Read Online or Download Advances in Enzymology and Related Areas of Molecular Biology, Volume 56 PDF
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 56
66)]. In the presence of Ala(CN) synthase, cysteine and thiocyanoalanine produced by the nonenzymic cyanolysis of cystine undergo concomitant enzymic @-replacement reactions with the excess of cyanide, releasing hydrogen B-REPLACEMENT-SPECIFICPLP-DEPENDENT LYASES 31 a 12 Figure 8. Interaction of (CN)Ala synthase with L-cystine and KCN. Production of hydrogen sulfide (curve 1) and thiocyanate (curve 2) versus L-cystine concentration (from ref. 28). Ordinate: AH2S and ACNS- in pmol from 0-20 min.
5. I. 14). Substantial liberation of thiocyanate in the complete test system was demonstrated by spectrophotometry of the Fe(II1)-thiocyanate (Table IX, sample 111). Pure Ala(CN) synthase has a pH-independent spectral absorption maximum at -410 nm (18,46). It shares the absence of significant circular dichroicity in absorption bands of the coenzyme chromo- 32 ALEXANDER E. BRAUNSTEIN AND ELIZABETH v. 1 0 0 0 - 0 - a From references 28 and 66. The products determined were ['4C]cyano-~-alanine (third column).
B. COMPARISON OF RELATIVE REACTION RATES AND SUBSTRATE AFFINITIES Such comparisons are roughly approximative in regard both to reaction rates (because the conditions for activity assay are widely different and often nonoptimal) and to substrate affinities-since the reported estimates are often based on Michaelis constants ( K m ) ,that is, the substrate concentration at which v = V/2), rather than on substrate constants, which are the true equilibrium (dissociation)constants of the active complex.