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).
Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology, Japan.
K
K
Hayashi
S
S
Sato
R
R
Takano
H
H
Tsujibo
H
H
Orikoshi
C
C
Imada
Y
Y
Okami
Y
Y
Inamori
S
S
Hara
D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D008969:Molecular Sequence Data; D012623:Seawater / Q000382:microbiology
D004220:Disulfides; D002688:Chitinases