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Primary structure and evolution of calcium-activated neutral protease (CANP)

  • Structure-Function Relations in Enzymes
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Abstract

The amino acid sequences of two subunits (80K and 30K) of calcium-activated neutral protease (CANP) were examined to clarify the structure-function relationship of CANP. The 80K subunit is composed of four clear domains (I–IV from the N-terminus). Domain II is a cysteine proteinase domain homologous to cathepsins B, L, and H. Domain IV is a calcium binding domain with four consecutive EF-hand structures known as typical calcium-binding sites found in calmodulin. The 30K subunit also has a clear domain structure (two domains). The N-terminal domain, a Gly-rich hydrophobic domain, probably determines the location of CANP through association with cellular membrane. The C-terminal domain is a calmodulinlike calcium-binding domain highly homologous to IV in the 80K subunit. The protease activity ascribable to II is regulated by 2 moles of built-in “calmodulins,” though its precise regulation mechanism is unknown. These results are discussed together with the molecular evolution of CANP on the basis of the gene structures of the two subunits.

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This article was presented during the proceedings of the International Conference on Macromolecular Structure and Function, held at the National Defence Medical College, Tokorozawa, Japan, December 1985.

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Suzuki, K., Ohno, S., Emori, Y. et al. Primary structure and evolution of calcium-activated neutral protease (CANP). J Protein Chem 6, 7–15 (1987). https://doi.org/10.1007/BF00248823

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  • DOI: https://doi.org/10.1007/BF00248823

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