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Metalloenzyme active site

Fig. 19. The carboxylate-histidine-zinc triad appears in the active site of carboxypeptidase A as Asp-142-His-69—and this interaction may contribute to zinc affinity in the metalloenzyme active site. Atomic coordinates were retrieved from the structure of the native enzyme (Rees et al, 1983) deposited in the Brookhaven Protein Data Bank. Fig. 19. The carboxylate-histidine-zinc triad appears in the active site of carboxypeptidase A as Asp-142-His-69—and this interaction may contribute to zinc affinity in the metalloenzyme active site. Atomic coordinates were retrieved from the structure of the native enzyme (Rees et al, 1983) deposited in the Brookhaven Protein Data Bank.
Modeling Phenoxyl Radical Metalloenzyme Active Sites... [Pg.71]

Complexes of N-heterocycles as models of metalloenzyme active sites 86ACR363. [Pg.301]

Goldberg, D. P. Lippard, S. J. Modeling Phenoxyl Radical Metalloenzyme Active Sites. In Mechanistic Bioinorganic Chemistry, Thorp, H. H. Pecoraro, V. L., Eds., American Chemical Society Washington, D.C., 1995 Vol. 246,... [Pg.738]

Y. Rondelez, M.-N. Rager, A. Duprat, O. Reinaud, Calix[6]arene-based cuprous funnel complexes a mimic for the substrate access channel to metalloenzyme active sites, J. Am. Chem. Soc., 2002, 124, 1334-1340. [Pg.223]

Potentially acting between these extremes are synthetic metal complexes that mimic the metalloenzyme active sites and catalyze reactions imder relatively mild conditions. [Pg.429]


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