Crystal structure of α-amylase from Oryza sativa: Molecular insights into enzyme activity and thermostability

Bioscience, Biotechnology and Biochemistry

Volumn 78, Issue 6, 2014, Pages 989-997

  Ochiai, Akihito ^a   Sugai, Hiroshi ^a   Harada, Kazuki ^a   Tanaka, Seiya ^a   Ishiyama, Yohei ^a   Ito, Kosuke ^a   Tanaka, Takaaki ^a   Uchiumi, Toshio ^a   Taniguchi, Masayuki ^a   Mitsui, Toshiaki ^a  

^a NIIGATA UNIVERSITY   (Japan)

Author keywords

Crystal structure; Glycoprotein; Rice; Thermostability; Amylase

Indexed keywords

AMINO ACIDS; AMYLASES; BINDING SITES; CARBOHYDRATES; ENZYME ACTIVITY; ENZYMES; GLYCOPROTEINS; STABILITY;

AMINO ACID RESIDUES; BIOLOGICAL FUNCTIONS; CARBOHYDRATE BINDING; CARBOHYDRATE CHAINS; GLYCOSIDE HYDROLASES; N-LINKED GLYCOSYLATION; RICE; THERMOSTABILITY;

CRYSTAL STRUCTURE;

HORDEUM; ORYZA SATIVA;

AMYLASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYMOLOGY; GLYCOSYLATION; METABOLISM; MOLECULAR GENETICS; RICE; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

ALPHA-AMYLASES; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GLYCOSYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; ORYZA SATIVA; RECOMBINANT PROTEINS; TEMPERATURE;

EID: 84925618282     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1080/09168451.2014.917261     Document Type: Article

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