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Structural Calcium (Trypsin, Subtilisin)

Published

Author(s)

G L. Gilliland, A Teplyakov

Abstract

There are about 40 families of serine proteases defined by amino acid sequence similarities that can be further grouped into 7 clans on the basis of their tertiary structure and the order of the catalytic triad.1 Members of clans SA and SB are characterized by the presence of calcium ions that stabilize the structure against proteolysis and thermal denaturation, but are not involved in catalysis or substrate recognition. Clan SA, which includes trypsin-like proteases, and clan SB, which includes subtilisins, are examples of proteins that are stabilized by the presence of calcium. Members of each enzyme family bind calcium in different ways with the same end result, stabilization of the tertiary structure.
Citation
Handbook of Metalloproteins
Publisher Info
John Wiley & Sons, Ltd, Hoboken, NJ

Keywords

calcium-binding, endopepidase, hydrolase, non-structural calcium, serine protease, structural stability, subtilisin, trypsin

Citation

Gilliland, G. and Teplyakov, A. (2017), Structural Calcium (Trypsin, Subtilisin), John Wiley & Sons, Ltd, Hoboken, NJ (Accessed May 22, 2024)

Issues

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Created February 19, 2017