Remarkable improvements of a neutral protease activity and stability share the same structural origins

Protein Engineering, Design and Selection

Volumn 23, Issue 8, 2010, Pages 599-606

  Asghari, S Mohsen ^a   Pazhang, Mohammad ^a   Ehtesham, Somayeh ^a   Karbalaei Heidari, Hamid Reza ^b   Taghdir, Majid ^c   Sadeghizadeh, Majid ^a   Naderi Manesh, Hossein ^a   Khajeh, Khosro ^a  

^a TARBIAT MODARES UNIVERSITY   (Iran)

^b SHIRAZ UNIVERSITY   (Iran)

^c UNIVERSITY OF GUILAN   (Iran)

Author keywords

hinge angle; neutral proteases; Salinovibrio proteolyticus protease; surface regions; thermostability

Indexed keywords

AMINO ACIDS; CALCIUM; ORGANIC ACIDS;

AMINO ACID SUBSTITUTION; BENDING ANGLE; CALCIUM BINDING; CATALYTIC EFFICIENCIES; EXTENDED SURFACES; NEUTRAL PROTEASE; OPTIMUM TEMPERATURE; PARALLEL IMPROVEMENT; POINT MUTATIONS; PROTEOLYTICUS; SITE DIRECTED MUTAGENESIS; STRUCTURAL ORIGIN; SURFACE REGION; SURFACE REGIONS; THEORETICAL STUDY; TRADE OFF; WILD TYPES;

ENZYME ACTIVITY;

CALCIUM; NEUTRAL PROTEINASE; BACTERIAL PROTEIN; PEPTIDE HYDROLASE; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CALCIUM BINDING; CATALYSIS; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; THERMOSTABILITY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; TEMPERATURE; VIBRIONACEAE;

BACTERIAL PROTEINS; CALCIUM; ENZYME ACTIVATION; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEPTIDE HYDROLASES; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; TEMPERATURE; VIBRIONACEAE;

EID: 77954964961     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq031     Document Type: Article

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