TY - JOUR
T1 - A small chimerically bifunctional monomeric protein
T2 - Tapes japonica lysozyme
AU - Takeshita, K.
AU - Hashimoto, Y.
AU - Ueda, Tadashi
AU - Imoto, T.
PY - 2003/9/1
Y1 - 2003/9/1
N2 - The lysozyme of the marine bilave Tapes japonica (13.8 kDa) is a novel protein. The protein has 46% homology with the destabilase from medicinal leech that has isopeptidase activity. Based on these data, we confirmed hydrolysis activity of T. japonica lysozyme against three substrates: L-γ-Glu-pNA, D-γ-Glu-pNA, and ε-(γ-Glu)-L-Lys. The optimal pH of chitinase and isopeptidase activity was 5.0 and 7.0, respectively. The isopeptidase activity was inhibited with serine protease inhibitor, but the lytic and chitinase activities were not. Moreover, only isopeptidase activity is decreased by lyophilization, but lytic and chitinase activities were not. We conclude that T. japonica lysozyme expresses isopeptidase and chitinase activity at different active sites.
AB - The lysozyme of the marine bilave Tapes japonica (13.8 kDa) is a novel protein. The protein has 46% homology with the destabilase from medicinal leech that has isopeptidase activity. Based on these data, we confirmed hydrolysis activity of T. japonica lysozyme against three substrates: L-γ-Glu-pNA, D-γ-Glu-pNA, and ε-(γ-Glu)-L-Lys. The optimal pH of chitinase and isopeptidase activity was 5.0 and 7.0, respectively. The isopeptidase activity was inhibited with serine protease inhibitor, but the lytic and chitinase activities were not. Moreover, only isopeptidase activity is decreased by lyophilization, but lytic and chitinase activities were not. We conclude that T. japonica lysozyme expresses isopeptidase and chitinase activity at different active sites.
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U2 - 10.1007/s00018-003-3082-z
DO - 10.1007/s00018-003-3082-z
M3 - Article
C2 - 14523554
AN - SCOPUS:0141637403
VL - 60
SP - 1944
EP - 1951
JO - Cellular and Molecular Life Sciences
JF - Cellular and Molecular Life Sciences
SN - 1420-682X
IS - 9
ER -
