Structural analysis of threonine 342 mutants of soybean β-amylase: Role of a conformational change of the inner loop in the catalytic mechanism

Biochemistry

Volumn 44, Issue 13, 2005, Pages 5106-5116

  Kang, You Na ^a,b   Tanabe, Aiko ^a   Adachi, Motoyasu ^a,c   Utsumi, Shigeru ^a   Mikami, Bunzo ^a  

^a KYOTO UNIVERSITY   (Japan)

^b Department of Obstetrics Gynecology   (United States)

^c JAPAN ATOMIC ENERGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; ENZYMES; GLUCOSE; HYDROGEN BONDS; STRUCTURE (COMPOSITION);

DEPROTONATION; GLUCOSE RESIDUES; MUTANTS; WILD-TYPE ENZYMES;

CONFORMATIONS;

ALANINE; BETA AMYLASE; GLUCOSE; GLUTAMIC ACID; MALTOSE; SERINE; THREONINE; VALINE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME STRUCTURE; HYDROGEN BOND; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; SOYBEAN; STRUCTURE ANALYSIS; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BETA-AMYLASE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HYDROGEN BONDING; KINETICS; LIGANDS; MALTOSE; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SOYBEANS; THREONINE;

GLYCINE MAX;

EID: 16344376742     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0476580     Document Type: Article

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