Abstract: The present invention provides a polypeptide of 26 amino acid residues that comprises the minimal ankyrin binding (MAB) domain. The MAB domain is responsible for the interactions between a Na,K-ATPase and ankyrin. The present invention also provides the three dimensional structure of the MAB domain. Also provided by the present invention are methods for modulating the interaction of a Na,K-ATPase and ankyrin.

Abstract: The invention relates to a variant of a parent Termamyl-like a-amylase, which variant has a-amylase activity and exhibits an alteration in at least one of the following properties relative to parent a-amylase: substrate specificity, substrate binding, substrate cleavage pattern, thermal stability, pH/activity profile, pH/stability profile, stability towards oxidation, Ca2+ dependency and specific activity.

Abstract: The present invention relates to DNA sequences which, on the codogenic strand, code plant debranching enzymes whose transcripts formed in transgenic plants code new proteins with the enzymatic activity of debranching enzymes which in transgenic plants reduce the degree of branching of amylopectin starch. The invention also relates to DNA sequences which on the codogenic strand code plant debranching enzymes whose transcripts formed in transgenic plants prevent the synthesis of proteins with the enzymatic activity of debranching enzymes, which in transgenic plants increases the degree of branching of amylopectin starch, and also to recombinant plasmids on which these DNA sequences are localized and which can be introduced into plant cells and plants.

Abstract: A purified thermostable enzyme is derived from the archael bacterium Thermococcus GU5L5. The enzyme has a molecular weight of about 68.5 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used for the removal of arginine, phenylalanine, or methionine amino acids from the N-terminal end of peptides in peptide or peptidomimetic synthesis. The enzyme is selective for the L, or ‘natural’ enantiomer of the amino acid derivatives and is therefore useful for the production of optically active compounds. These reactions can be performed in the presence of the chemically more reactive ester functionally, a step which is very difficult to achieve with nonenzymatic methods.