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. Gln15, Gly65 and Gln104 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.
Dementiev
A A
AA
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
Moiseyev
G P
GP
Shlyapnikov
S V
SV
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D007700:Kinetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D010446:Peptide Fragments; D012260:Ribonucleases; C084264:ribonuclease Bci