Enzymatic activity of circular sortase A under denaturing conditions: An advanced tool for protein ligation

Biochemical Engineering Journal

Volumn 82, Issue , 2014, Pages 200-209

  Zhulenkovs, D ^a,b   Jaudzems, K ^c   Zajakina, A ^a   Leonchiks, A ^a  

^a LATVIAN BIOMEDICAL RESEARCH AND STUDY CENTRE   (Latvia)

^b UNIVERSITY OF LATVIA   (Latvia)

^c LATVIAN INSTITUTE OF ORGANIC SYNTHESIS   (Latvia)

Author keywords

Denaturing conditions; Enzyme stability; Intein mediated cyclization; Protein ligation; Sortase A

Indexed keywords

BACTERIA; BIOMATERIALS; CYCLIZATION; DESIGN; ENZYMES; ESCHERICHIA COLI; SUBSTRATES; UREA;

BIOCHEMICAL CHARACTERISTICS; DENATURING CONDITIONS; ENZYME STABILITY; ESCHERICHIA COLI EXPRESSION SYSTEMS; GLUTATHIONE-S-TRANSFERASE; GREEN FLUORESCENCE PROTEINS; PROTEIN LIGATION; SORTASE A;

PROTEINS;

ENHANCED GREEN FLUORESCENT PROTEIN; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE TRANSFERASE; SORTASE; SORTASE A; UNCLASSIFIED DRUG; UREA;

ARTICLE; CYCLIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; ESCHERICHIA COLI; GENE EXPRESSION SYSTEM; IN VITRO STUDY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN LIGATION; PROTEIN METABOLISM; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN SYNTHESIS; PROTEIN UNFOLDING; SYNECHOCYSTIS;

ESCHERICHIA COLI; STAPHYLOCOCCUS AUREUS; SYNECHOCYSTIS SP.;

EID: 84890332539     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2013.11.018     Document Type: Article

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