Isolation of a chymotrypsinogen B-like enzyme from the archaeon Natronomonas pharaonis and other halobacteria

• Published in: Extremophiles : life under extreme conditions Vol. 3; no. 2; pp. 153 - 161
• Main Authors: STAN-LOTTER, H, DOPPLER, E, JAROSCH, M, RADAX, C, GRUBER, C, INATOMI, K.-I
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer 01.05.1999; Tokyo
• Subjects: Amino Acid Sequence; Animals; Bacteriology; Biological and medical sciences; Cattle; Chymotrypsinogen - chemistry; Chymotrypsinogen - isolation & purification; Chymotrypsinogen - metabolism; Endopeptidases - isolation & purification; Enzyme Precursors; Fundamental and applied biological sciences. Psychology; Humans; Metabolism. Enzymes; Microbiology; Molecular Sequence Data; Natronobacterium - enzymology; Sequence Homology, Amino Acid; Space life sciences; Serine endopeptidases; Archaeobacteria; Enzyme; Alkalophily; Homology; Chymotrypsinogen; Peptidases; Enzymatic activity; Halophily; Halobacteriales; Bacteria; Hydrolases; Aminoacid sequence; Non-programmatic

A protease of a molecular mass of approximately 30kDa was isolated and purified from the haloalkaliphilic archaeon Natronomonas (formerly Natronobacterium) pharaonis. The enzyme hydrolyzed synthetic peptides, preferentially at the carboxyl terminus of phenylalanine or leucine, as well as large prote...