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Identification of the positions of disulfide bonds of chitinase from a marine bacterium, Alteromonas sp. strain O-7.

Extracellular chitinase from marine Alteromonas sp. strain O-7 is unique because of the activation by four major cations contained in sea water, such as Na+, K+, Mg2+, and Ca2+. The positions of S-S bonds of Alteromonas chitinase were identified. Alteromonas chitinase was fragmented by TPCK-trypsin and Staphylococcus aureus V8 protease. The amino acid and sequence analyses of three peptides showed that the positions of disulfide bonds are Cys(94)-Cys(99), Cys(174)-Cys(196), and Cys(386)-Cys(395).