Directed evolution and structural analysis of N-carbamoyl-D-amino acid amidohydrolase provide insights into recombinant protein solubility in Escherichia coli

Biochemical Journal

Volumn 402, Issue 3, 2007, Pages 429-437

  Jiang, Shimin ^a   Li, Chunhong ^a   Zhang, Weiwen ^b   Cai, Yuanheng ^a   Yang, Yunliu ^a   Yang, Sheng ^a   Jiang, Weihong ^a,c  

^a Shanghai Jiao Tong University Affiliated Sixth People s Hospital   (China)

^b PACIFIC NORTHWEST NATIONAL LABORATORY   (United States)

^c INSTITUTE PASTEUR OF SHANGHAI   (China)

Author keywords

Directed evolution; N carbamoyl D amino acid amidohydrolase; Negative charge; Protein folding; Protein solubility

Indexed keywords

DIRECTED EVOLUTION; N-CARBAMOYL-D-AMINO ACID AMIDOHYDROLASE; NEGATIVE CHARGE; PROTEIN SOLUBILITY;

AMINO ACIDS; ANTIBIOTICS; BIOACTIVITY; ESCHERICHIA COLI; PROTEIN FOLDING; SOLUBILITY;

ENZYME KINETICS;

AMINO ACID; HYDROLASE; N CARBAMOYL DEXTRO AMINO ACID AMINOHYDROLASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; COMPUTER MODEL; ENZYME ACTIVE SITE; ENZYME KINETICS; ESCHERICHIA COLI; HYDROPHILICITY; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; SOLUBILITY; THERMODYNAMICS;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; AMINO ACIDS; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; GENE EXPRESSION; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; RHIZOBIUM; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY; STRUCTURAL HOMOLOGY, PROTEIN; THERMODYNAMICS; VARIATION (GENETICS);

ESCHERICHIA COLI;

EID: 33947266127     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061457     Document Type: Article

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