Autolysis of a novel multidomain subtilase-cold-adapted deseasin MCP-01 is pH-dependent and the surface loops in its catalytic domain, the linker, and the P_proprotein domain are susceptible to proteolytic attack

Biochemical and Biophysical Research Communications

Volumn 358, Issue 3, 2007, Pages 704-709

  Chen, Xiu Lan ^a   Zhang, Yu Zhong ^a   Lu, Jing Tao ^a   Xie, Bin Bin ^a   Sun, Cai Yun ^a   Guo, Bing ^a  

^a SHANDONG UNIVERSITY   (China)

Author keywords

Autolysis; Autolytic mechanism; Autolytic sites; Cold adapted; Deseasin; Multidomain; pH dependent; Subtilases

Indexed keywords

GLYCINE DEHYDROGENASE (DECARBOXYLATING); MCP 01 ENZYME; PROTEINASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; AUTOLYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION;

AMINO ACID SEQUENCE; BINDING SITES; BUFFERS; CATALYTIC DOMAIN; COLD; ENDOPEPTIDASES; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBTILISINS; SURFACE PROPERTIES; TIME FACTORS;

EID: 34249079966     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.04.193     Document Type: Article

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