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Literature summary for 3.4.24.55 extracted from

  • Alper, B.J.; Nienow, T.E.; Schmidt, W.K.
    A common genetic system for functional studies of pitrilysin and related M16A proteases (2006), Biochem. J., 398, 145-152.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D79A no effect on function Escherichia coli
E91A no proteolytic activity Escherichia coli
F198A enzyme remains functional Escherichia coli
H193A enzyme remains functional Escherichia coli
K197A enzyme remains functional Escherichia coli
additional information heterologous expression of enzyme in yeast, enzyme functionally substitutes for yeast Ax11p and Ste23p in pheromone production. Independent heterologous expression of N-terminal domain with amino acids 1-515 or C-terminal domain with amino acids 516-962 does not promote yeast mating. Co-expression of both domains restores yeast mating Escherichia coli
N119A promotion of yeast mating factor in heterologous expression is disabled Escherichia coli
N317A/R318A/S319A enzyme remains functional Escherichia coli
R792A no proteolytic activity Escherichia coli
R792A/T793A/E794A/E795A no proteolytic activity Escherichia coli
S117A enzyme remains functional Escherichia coli
S117A/H118A/N119A promotion of yeast mating factor in heterologous expression is disabled Escherichia coli
S196A/K197A/F198A/S199A promotion of yeast mating factor in heterologous expression is disabled Escherichia coli
T127A enzyme remains functional Escherichia coli
T322A/L323A enzyme remains functional Escherichia coli
Y799A no proteolytic activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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