Molecular characterization of cathepsin L from hepatopancreas of the carp Cyprinus carpio.
Purified cathepsin L from carp, Cyprinus carpio, consists of a 28 kDa single-chain form that is different from the 24 and 5 kDa mammalian two-chain form. We cloned cathepsin L from carp hepatopancreas. The sequence consisted of a 1490 bp cDNA and a 1014 bp open reading frame, encoding a deduced protein of 337 amino acids that is likely processed to an active enzyme (single-chain form) with 222 amino acids. Its similarity to other types of vertebrate cathepsin L is less than 69%. Mammalian cathepsin L is further processed to a two-chain form, but possibly this is not the case with carp cathepsin L: the P1 site where cleavage occurred in the two-chain form of mammalian cathepsin L contains a serine, while carp cathepsin L processes a valine. Therefore, carp cathepsin L may have a different mechanism of action from mammalian cathepsin L.
Tsunemoto
Kazunobu
K
Graduate School of Science and Technology, Nagasaki University, Bunkyo, Nagasaki, Nagasaki 852-8521, Japan.
Osatomi
Kiyoshi
K
Nozaki
Yukinori
Y
Hara
Kenji
K
Ishihara
Tadashi
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002347:Carps / Q000235:genetics* / Q000378:metabolism; D056668:Cathepsin L; D002403:Cathepsins / Q000235:genetics* / Q000302:isolation & purification; D003546:Cysteine Endopeptidases; D018076:DNA, Complementary; D043143:Hepatopancreas / Q000378:metabolism*; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D018076:DNA, Complementary; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D056668:Cathepsin L