Biased mutagenesis in the N-terminal region by degenerate oligonucleotide gene shuffling enhances secretory expression of barley α-amylase 2 in yeast

Protein Engineering, Design and Selection

Volumn 18, Issue 11, 2005, Pages 515-526

  Fukuda, Kenji ^a,b,c   Jensen, Malene H ^d   Haser, Richard ^d   Aghajari, Nushin ^d   Svensson, Birte ^a,b  

^a CARLSBERG LABORATORY   (Denmark)

^b TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^c INSTITUT DE BIOLOGIE ET CHIMIE DES PROTÉINES   (France)

^d OBIHIRO UNIVERSITY OF AGRICULTURE AND VETERINARY MEDICINE   (Japan)

Author keywords

Codon usage; Isozyme sequence guided mutagenesis; Stability; X ray crystallography; Yeast

Indexed keywords

CODON USAGE; ISOZYME SEQUENCE-GUIDED MUTAGENESIS; LIQUID CULTURE; OLIGONUCLEOTIDES;

CLONING; CRYSTAL STRUCTURE; ENZYME KINETICS; GENES; PROTEINS; X RAY CRYSTALLOGRAPHY; YEAST;

MUTAGENESIS;

ALPHA AMYLASE 2; GLUTAMINE; GUANINE NUCLEOTIDE; HISTIDINE; OLIGONUCLEOTIDE; PROLINE; PYRIMIDINE NUCLEOTIDE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BARLEY; CATALYSIS; CHIMERA; CRYSTAL STRUCTURE; CULTURE MEDIUM; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME STABILITY; FUNGAL STRAIN; FUNGUS CULTURE; FUNGUS MUTANT; GENE; GENE ACTIVITY; GENE LIBRARY; GENE MUTATION; GENE STRUCTURE; GENETIC ANALYSIS; HOMOLOGOUS RECOMBINATION; MOLECULAR CLONING; MUTAGENESIS; NONHUMAN; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN DOMAIN; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; SUBSTITUTION REACTION; TRANSLATION REGULATION; WILD TYPE; YEAST;

ALPHA-AMYLASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; ENZYME STABILITY; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PICHIA; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; STARCH; VARIATION (GENETICS);

FUNGI; HORDEUM VULGARE SUBSP. VULGARE; PICHIA PASTORIS; SACCHAROMYCES CEREVISIAE;

EID: 27544473723     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzi057     Document Type: Article

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