3.4.21.63	evolution	the enzyme belongs to the gluzincin family	731961	
3.4.21.63	additional information	compared to papain (8.7%) and alcalase (12.2%), the degree of hydrolysis of rAp to soy protein isolate is 16.5%	-, 755309	
3.4.21.63	additional information	enzyme structure homology modeling. The active center of the alkaline protease is established by three amino acid residues Asp41, His72, and Ser228, based on the result of protein sequence alignment between the alkaline protease and cuticle-degrading protease from north american fungi, three-dimensional structures, overview	-, 754496	
3.4.21.63	additional information	structure-function analysis, three-dimensional structure and comparative and homology modeling, overview	731392	
3.4.21.63	additional information	the enzyme is a serine protease	-, 754276	
3.4.21.63	additional information	the enzyme retains 80% of its original activity in the presence of non ionic and ionic surfactants after 1 h of incubation at 30°C, overview	-, 717055	
3.4.21.63	additional information	the enzyme sequence cotains conserved Asp156, His187, and Ser339 residues of alkaline protease. The enzyme is a serine protease	754408	
3.4.21.63	physiological function	secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins C3, C4, and C5. C3b is an important opsonin, but other complement proteins also have essential functions in the defense against microbes. C5b, a cleavage product of C5, initiates formation of the membrane attack complex at a later stage of complement activation, and C5a represents a potent anaphylatoxin. C1q initiates the classical pathway of complement activation, and C4 is part of the C3 convertase of the classical pathway. The enzyme is involved in the mechanism that contributes to evasion from the host complement attack, overview	-, 717658	
3.4.21.63	physiological function	the enzyme is a virulence factor for the organism infecting the human eye cornea and causing keratitis	732387