Primary structure and catalytic properties of extracellular ribonuclease of bacillus circulans

FEBS Letters

Moiseyev, G.P.¹  Shlyapnikov, S.V.¹  Dementiev, A.A.¹ 

[1] Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov stn 32, Moscow 117984, Russian Federation

关键词: RNase;    Bacillus circulans;    Sequence;    Catalytic property;    RNase Bci;    Ba;    Bi and Bth;    ribonucleases of Bacillus circulans;    B. amyloliquefaciens;    B. intermedius and B. thuringiensis (EC 3.1.27.1);    respectively;   

DOI  :  10.1016/0014-5793(93)81721-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown