Primary structure and catalytic properties of extracellular ribonuclease of bacillus circulans

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...

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Bibliographic Details
Published in:FEBS letters 1993-11, Vol.334 (2), p.247-249
Main Authors: Dementiev, A.A., Moiseyev, G.P., Shlyapnikov, S.V.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
B. amyloliquefaciens
B. intermedius and B. thuringiensis (EC 3.1.27.1)
Bacillus - enzymology
Bacillus circulans
Bi and Bth
Catalytic property
Chromatography, High Pressure Liquid
Kinetics
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Peptide Fragments - chemistry
Peptide Fragments - isolation & purification
respectively
Ribonucleases - chemistry
Ribonucleases - isolation & purification
Ribonucleases - metabolism
ribonucleases of Bacillus circulans
RNase
RNase Bci
Sequence
Substrate Specificity
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)81721-B