3.4.22.10	proteolytic modification	SPE B produced from group A Streptococcus (GAS) is released extracellularly to culture medium as a zymogen (proSPE B) with a molecular mass of 40 kDa. The conversion of proSPE B to the 28 kDa active mature SPE B (mSPE B) is achieved by autoproteolysis and exogenous proteases	698880	
3.4.22.10	proteolytic modification	Spe is expressed as a propeptide. Zinc blocks the maturation of the SpeB zymogen and thereby the proteolytic degradation of proteins by SpeB	733967	
3.4.22.10	proteolytic modification	SpeB is secreted as a 40000 Da proenzyme that is converted into a mature 28000 Da active proteinase by autocatalytic cleavage	650988	
3.4.22.10	proteolytic modification	streptopain is initially expressed as a 40 kDa zymogen. Maturation is caused by cleavage of the 138 N-terminal amino acids, resulting in a 28000 active protease	755296	
3.4.22.10	proteolytic modification	the enzyme performs autolytic processing to the 28 kDa mature protein, the 12 kDa pro-sequence domain, residues 28-145, directs the folding of the mature enzyme, overview	667311	
3.4.22.10	proteolytic modification	the enzyme performs autolytic processing to the mature 28 kDa protein by removal of an about 117 amino-acid peptide from the N-terminus	-, 667426, 668772, 668911	
3.4.22.10	side-chain modification	-	81451, 81464	
3.4.22.10	side-chain modification	autocatalytic maturation of the zymogen proceeds through the sequential appearance of at least six intermediates, resulting from cleavage after Lys26, Asn41, Lys101, Ala112 and Lys118	-, 81453	
3.4.22.10	side-chain modification	autocatalytic processing of the 40000 Da zymogen to the 28000 Da mature form	81463	
3.4.22.10	side-chain modification	complete removal of the 118 amino acids from the SCP zymogen results in formation of SCP	81456