The enzyme carbonic anhydrase has been well characterized in mammalian systems, but the structural properties of the plant isozymes remain elusive. To investigate the nature of the zinc-binding site in spinach carbonic anhydrase, we targeted potential zinc ligands for mutagenesis and examined the resulting enzymes for catalytic activity and stoichiometric zinc binding. In addition, we examined the wild-type protein using extended X-ray absorption fine structure analysis. Our results suggest that spinach carbonic anhydrase utilizes a Cys-His-Cys-H2O ligand scheme to bind the zinc ion at the active site.
This paper describes a reproducible method for the induction of in vitro potato tubers in a wide range of genotypes. These in vitro tubers could be induced in all genotypes tested and show striking similarity to field produced tubers. In vitro tubers may prove most useful as material for International germplasm distribution.
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