Premium
Primary structure and catalytic properties of extracellular ribonuclease of bacillus circulans
Author(s) -
Dementiev A.A.,
Moiseyev G.P.,
Shlyapnikov S.V.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81721-b
Subject(s) - bacillus circulans , barnase , rnase p , bacillus amyloliquefaciens , ribonuclease , chemistry , biochemistry , extracellular , enzyme , rna , gene , fermentation
A complete amino acid sequence of extracellular Bacillus circulans RNase was established and compared with a structure of B. amyloliquefaciens RNase. Gln 15 , Gly 65 and Gln 104 in B. amyloliquefaciens RNase were found to be replaced by Leu, Ala and Lys, respectively, in B circulans RNase. Catalytic properties of B. circulans RNase were studied.