Two new extracellular serine proteases from Streptomyces fradiae.
1. Two new extracellular serine proteases have been purified to homogeneity from Streptomyces fradiae. 2. On amino acid sequencing, striking homology is observed between the first enzyme and Streptomyces griseus Protease A, and the second enzyme and S. griseus trypsin. 3. The sequence information shows for the first time that structurally and enzymatically related serine proteases are extracellularly expressed by different Streptomycetes. 4. Differential keratinolytic substrate specificity among these two microbes are probable due to a difference in disulfide reduction capacity.
Sinha
U
U
Genecor, Inc., South San Francisco, CA 94080.
Wolz
S A
SA
Lad
P J
PJ
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013302:Streptomyces / Q000201:enzymology*
D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases