Concurrent mutations in six amino acids in β-glucuronidase improve its thermostability

Protein Engineering, Design and Selection

Volumn 20, Issue 7, 2007, Pages 319-325

  Xiong, Ai Sheng ^a,d   Peng, Ri He ^a   Cheng, Zong Ming ^b   Li, Yi ^c   Liu, Jin Ge ^a,d   Zhuang, Jing ^a,d   Gao, Feng ^a   Xu, Fang ^a,d   Qiao, Yu Shan ^d   Zhang, Zhen ^d   Chen, Jian Min ^e   Yao, Quan Hong ^a  

^a INSTITUTE OF EDIBLE FUNGI   (China)

^b UNIVERSITY OF TENNESSEE   (United States)

^c UNIVERSITY OF CONNECTICUT   (United States)

^d NANJING AGRICULTURAL UNIVERSITY   (China)

^e YANGZHOU UNIVERSITY   (China)

Author keywords

glucuronidase; Directed evolution; Enzyme properties; Structure function analysis; Thermostability

Indexed keywords

DNA; ENZYMES; GENES; THERMODYNAMIC STABILITY;

DIRECTED EVOLUTION; ENZYME PROPERTIES; STRUCTURE-FUNCTION ANALYSIS;

AMINO ACIDS;

AMINO ACID DERIVATIVE; BETA GLUCURONIDASE; PYROXYLIN;

ARTICLE; CONTROLLED STUDY; DNA SHUFFLING; ENZYME STABILITY; GENE MUTATION; HUMAN; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; DNA SHUFFLING; ENZYME STABILITY; ESCHERICHIA COLI; GLUCURONIDASE; HEAT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED;

EID: 34548227042     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzm023     Document Type: Article

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