Enhancing the thermostability of Escherichia coli l-asparaginase II by substitution with pro in predicted hydrogen-bonded turn structures

Enzyme and Microbial Technology

Volumn 41, Issue 4, 2007, Pages 523-527

  Li, Liang Zhu ^a   Xie, Tian Hong ^a   Li, Hong Jun ^a   Qing, Chen ^b   Zhang, Guang Ming ^a   Sun, Mao Sheng ^a  

^a INSTITUTE OF MEDICAL BIOLOGY   (China)

^b KUNMING MEDICAL UNIVERSITY   (China)

Author keywords

Amino acids; Bioinformatics analysis; Enzyme activity; l Asparaginase II; Site directed mutagenesis; Thermostability

Indexed keywords

AMINO ACIDS; BIOINFORMATICS; DISEASE CONTROL; ESCHERICHIA COLI; HYDROGEN BONDS; MUTAGENESIS; PATIENT TREATMENT; TOXIC MATERIALS;

ASPARAGINASE THERAPY; BIOINFORMATICS ANALYSIS; LYMPHOBLASTIC LEUKAEMIA; SITE-DIRECTED MUTAGENESIS; THERMOSTABILITY;

ENZYME ACTIVITY;

ASPARAGINASE; ASPARTIC ACID; HYDROGEN; MUTANT PROTEIN; PROLINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DRUG STABILITY; DRUG SYNTHESIS; ENZYME STABILITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; NUCLEOTIDE SEQUENCE; THERMOSTABILITY; WILD TYPE;

ESCHERICHIA COLI;

EID: 34447096370     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2007.04.004     Document Type: Article

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