Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme.
The lysozyme of the marine bivalve, Tapes japonica (13.8 kDa), belongs to the invertebrate lysozyme family and displays both chitinase and isopeptidase activities. We determined the complete cDNA sequence and constructed effective expression systems for this enzyme using Escherichia coli (BL21) and Pichia pastoris. The native and recombinant proteins indicated lysozyme activity and isopeptidase activity, including the proteolysis of d-dimer, a plasminolytic product of stabilized polymeric fibrin. These results will be utilized for the structural and functional study of invertebrate lysozymes, and for the development of applications for thrombosis therapies.
Takeshita
Kouhei
K
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan.
Hashimoto
Yoshio
Y
Thujihata
Yoshiyuki
Y
So
Takanori
T
Ueda
Tadashi
T
Iomoto
Taiji
T
D000595:Amino Acid Sequence; D000818:Animals; D019759:Carbon-Nitrogen Lyases / Q000737:chemistry; D002688:Chitinases / Q000737:chemistry; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004926:Escherichia coli / Q000235:genetics; D005342:Fibrinolysis; D008969:Molecular Sequence Data; D008974:Mollusca / Q000201:enzymology* / Q000235:genetics*; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D010843:Pichia / Q000235:genetics
D018076:DNA, Complementary; D002688:Chitinases; D009113:Muramidase; D019759:Carbon-Nitrogen Lyases; C034300:isopeptidase