Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop

Applied Microbiology and Biotechnology

Volumn 95, Issue 3, 2012, Pages 661-669

  Cheng, Ya Shan ^a   Ko, Tzu Ping ^b   Huang, Jian Wen ^c   Wu, Tzu Hui ^a   Lin, Cheng Yen ^c   Luo, Wenhua ^d   Li, Qian ^e   Ma, Yanhe ^e   Huang, Chun Hsiang ^e   Wang, Andrew H J ^b   Liu, Je Ruei ^a,f   Guo, Rey Ting ^a,e  

^a NATIONAL TAIWAN UNIVERSITY   (Taiwan)

^b INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^c Genozyme Biotechnology Inc   (Taiwan)

^d AsiaPac Biotechnology Co Ltd   (China)

^e SOUTH CHINA AGRICULTURAL UNIVERSITY   (China)

^f Chinese Academy of Sciences   (China)

Author keywords

Crystal structure; Endoglucanase; Enzyme kinetics; Protein engineering; Thermostability

Indexed keywords

ACTIVITY ENHANCEMENT; CATALYTIC EFFICIENCIES; CRYSTALLOGRAPHIC ANALYSIS; DELETION MUTATIONS; ENDOGLUCANASES; HYPERTHERMOSTABILITY; HYPERTHERMOSTABLE; KINETIC DATA; LOCAL PERTURBATION; PRODUCT RELEASE; PROTEIN ENGINEERING; PROTEIN STRUCTURES; REDUCING ENDS; SINGLE MUTATION; SITE DIRECTED MUTAGENESIS; STACKING INTERACTION; SUBSTRATE BINDING; SUBSTRATE COMPLEXES; SUGAR MOIETY; SURFACE LOOPS; THERMOSTABILITY; THERMOTOGA MARITIMA; WILD TYPES; WILD-TYPE ENZYMES; WORKING TEMPERATURES;

CRYSTAL STRUCTURE; ENZYME KINETICS; GENETIC ENGINEERING; HYDROGEN BONDS; INDUSTRIAL APPLICATIONS;

SUBSTRATES;

ARGININE; CELLULASE; CELLULASE 12A; TYROSINE; UNCLASSIFIED DRUG;

BACTERIUM; CARBOHYDRATE; CRYSTALLOGRAPHY; ENZYME ACTIVITY; HYDROGEN; MUTATION; PROTEIN; REACTION KINETICS; TEMPERATURE EFFECT;

ARTICLE; CRYSTAL STRUCTURE; GENE MUTATION; HYDROGEN BOND; HYPERTHERMOSTABILITY; MOLECULAR INTERACTION; MUTANT; NONHUMAN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; THERMOTOGA MARITIMA; WILD TYPE;

AMINO ACID SUBSTITUTION; CELLULASE; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; KINETICS; METABOLIC ENGINEERING; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN CONFORMATION; TEMPERATURE; THERMOTOGA MARITIMA;

THERMOTOGA MARITIMA;

EID: 84864618029     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3791-4     Document Type: Article

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