title: Amino acid sequence of alkaliphilic serine protease from silkworm, Bombyx mori, larval digestive juice.
abstract: 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 mu = 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.
authors: Department of Food Science and Technology, School of Agriculture, Nagoya University, Aichi, Japan.
authors: T
authors: T
authors: Sasaki
authors: T
authors: T
authors: Hishida
authors: K
authors: K
authors: Ichikawa
authors: S
authors: S
authors: Asari
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx; D005750:Gastric Juice / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007814:Larva; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry*
chemical_list: D012697:Serine Endopeptidases