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Amino acid sequence of alkaliphilic serine protease from silkworm, Bombyx mori , larval digestive juice
Author(s) -
Sasaki Takuji,
Hishida Tomoaki,
Ichikawa Katsuomi,
Asari Shin-ichiro
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81652-g
Subject(s) - bombyx mori , proteases , serine protease , biochemistry , serine , protease , midgut , bombycidae , amino acid , cysteine , chemistry , enzyme , catalytic triad , biology , larva , botany , gene
Alkaliphilic protease, P‐IIc, from silkworm, Bombyx mori, larval midgut digestive juice consists of 232 amino acids. It has a catalytic triad, Asp‐His‐Ser, invariably found in a serine protease. A shift of optimal pH value towards the alkaline side diminished at μ=1.0. This suggests the existence of an electrostatic interaction that affects the proteolytic activity. The higher Arg content may be responsible for this phenomenon. Two cysteine residues probably exist unpaired in a novel position among serine proteases.