Abstract
AN increasing number of hydrolytic enzymes have been reported to be inhibited by diisopropylphosphorofluoridate. Where the resulting diisopropylphosphoenzyme has been investigated, the phosphate was isolated in the form of phospho-serine peptides and the amino-acid sequence about the reactive serine has been determined in several cases. Trypsin1 chymotrypsin2–4, elastase5,6 and thrombin7 have the sequence Gly.Asp.Ser.Gly., while horse liver aliesterase8 and pseudocholinesterase9 have Gly.Glu.Ser.-Ala.Gly. The proteolytic enzyme subtilisin was isolated from a strain of B. subtilis by Güntelberg and Ottesen10 and they recorded its inhibition by diisopropylphosphorofluoridate, while Matsubara11 obtained a phospho-peptide from strain N1 but did not report any sequence. The present communication deals with an investigation of the enzyme from Novo Terapeutisk Laboratorium known as ‘bacterial trypsin’, which is similar to, but distinguishable from, the original subtilisin.
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SANGER, F., SHAW, D. Amino-acid Sequence about the Reactive Serine of a Proteolytic Enzyme from Bacillus subtilis. Nature 187, 872–873 (1960). https://doi.org/10.1038/187872a0
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DOI: https://doi.org/10.1038/187872a0
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