Purification and characterization of a serine proteinase from senescent sporophores of the commercial mushroom Agaricus bisporus.
A proteinase has been purified from the stipes of senescent sporophores of the mushroom Agaricus bisporus. The proteinase was inhibited by PMSF. It has a broad pH optimum, 6.5-11.5, and a narrow substrate specificity, requiring both a hydrophobic amino acid in the P1 position and a minimum peptide chain length. The apparent molecular mass of the proteinase was 27 kDa when determined by SDS-PAGE and 14.1 kDa when measured by gel filtration. The isoelectric point of the proteinase was 9.0. Polyclonal antibodies have been raised to the proteinase. The proteinase from A. bisporus has similar properties to, and 60% N-terminal sequence identity with, proteinase K from the fungus Tritirachium album.
Burton
K S
KS
Horticulture Research International, Littlehampton, UK.
Wood
D A
DA
Thurston
C F
CF
Barker
P J
PJ
D000364:Agaricus / Q000201:enzymology* / Q000235:genetics; D000595:Amino Acid Sequence; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D003904:Mitosporic Fungi / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D013172:Spores, Fungal / Q000201:enzymology; D013379:Substrate Specificity
D009842:Oligopeptides; D012697:Serine Endopeptidases