Advances in Enzymology and Related Areas of Molecular - download pdf or read online

By Alton Meister

ISBN-10: 0470123028

ISBN-13: 9780470123027

ISBN-10: 047189012X

ISBN-13: 9780471890126

Keeps the authoritative sequence that studies study into enzymology and similar parts of molecular biology. offers six papers by means of top gurus.

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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 56

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This reaction is suppressed in the presence of sulfite or an adequate thiol cosubstrate. ' Concentration in incubation mix = 25 mM. 5 mM. ' Concentration added was -25 mM; actual concentration during incubation was lower, owing to the high volatility of CHsSH. This trend is evident from the data in Table XV. P 00 (white lupine) (67) (blue lupine) (20) (blue lupine) (93) 4. &Cyanoalanine synthase (human liver) (52) embryo yolk-sac) (32,33) 2. Serine sulfhydrase (chicken liver) (26,41) 2a. Serine sulfhydrase (baker's Yeast) (94) 3.

Considerable differences were observed in the coenzyme analog patterns of the individual lyases, but no characteristic contrast was revealed between those of replacement-specific type and the others, with the exception of the more stringent structural requirements of serine sulfhydrase, 2, and cystathionine P-synthase 3, for catalytically active analogs. Only two analogs were found active as substitutes for PLP with these lyases, namely, 2-norPLP and 5’-MePLP (36). The catalytic parameters of PLP itself, and a number of its analogs displaying activity either as coenzyme substitutes or as inhibitory quasicoenzymes, are compiled in Table XVII for lyases 2, 3, 4, 7, and 8 (see also refs.

Alliinase, y-cystathionase, and others). The stability of active oligomers is variable and usually depends on a number of factors, such as the concentrations of protein and coenzyme, pH, temperature, ionic environment, and so on. In most cases coenzyme removal, increase in pH, and low protein concentration displace the equilibrium in favor of smaller species (monoor dimers). Variations also occur in the ease of resolution (respectively, reassociation) of apo- and coenzymes. K,, values are often much higher then the true dissociation constants, KO;to estimate these is not easy because apo f* holo equilibrium is only slowly reached at low commensurate concentrations of apo- and coenzyme (14,15,79,113).

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Advances in Enzymology and Related Areas of Molecular Biology, Volume 56 by Alton Meister


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