Thermal stabilization of penicillolysin, a thermolabile 19 kDa Zn 2+-protease, obtained by site-directed mutagenesis

Protein Engineering, Design and Selection

Volumn 17, Issue 3, 2004, Pages 261-266

  Doi, Yuko ^a   Akiyama, Hidetoshi ^a   Yamada, Yoshiteru ^a   Ee, Ch'ng Ewe ^b   Lee, Byung Rho ^a   Ikeguchi, Masamichi ^a   Ichishima, Eiji ^a,b  

^a SOKA UNIVERSITY   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

Author keywords

Aspzincin; M35 protease; Mutagenesis; Penicillolysin; Thermal stabilization; Zn2+ protease

Indexed keywords

DEUTEROLYSIN; ENZYME; FUNGAL ENZYME; METALLOPROTEINASE; MUTANT PROTEIN; PENICILLOLYSIN; PEPTIDYLLYSINE METALLOPEPTIDASE; PROTEINASE; UNCLASSIFIED DRUG; ZINC PROTEASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME STABILITY; HEAT TOLERANCE; NONHUMAN; PENICILLIUM CITRINUM; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; TEMPERATURE SENSITIVITY;

AMINO ACID SEQUENCE; ASPERGILLUS; BASE SEQUENCE; CATALYSIS; CIRCULAR DICHROISM; DISULFIDES; ENZYME STABILITY; ESCHERICHIA COLI; FUNGAL PROTEINS; HEAT; ISOELECTRIC POINT; KINETICS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; PENICILLIUM; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY, ATOMIC; SPECTROPHOTOMETRY, ULTRAVIOLET; SUBSTRATE SPECIFICITY; ZINC;

ASPERGILLUS; ASPERGILLUS ORYZAE; BASIDIOMYCOTA; PENICILLIUM; PENICILLIUM CITRINUM;

EID: 2942648079     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzh034     Document Type: Article

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