Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 2, 2011, Pages 633-644

  Jung, Jong Hyun ^a   Jung, Tae Yang ^b,c   Seo, Dong Ho ^a   Yoon, Sei Mee ^b   Choi, Hyun Chang ^a   Park, Byoung Chul ^b   Park, Cheon Seok ^a   Woo, Eui Jeon ^b,c  

^a Kyung Hee University   (South Korea)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^c University of Science and Technology (UST)   (South Korea)

Author keywords

250s loop; Amylomaltase; Substrate binding sites; Thermus brockianus

Indexed keywords

4ALPHA GLUCANOTRANSFERASE; GLUCOSE; MALTOSE; MALTOTRIOSE; MUTANT PROTEIN;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR RECOGNITION; MUTATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; THERMUS; THERMUS BROCKIANUS; WILD TYPE;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GLUCOSE; GLUTAMINE; GLYCOGEN DEBRANCHING ENZYME SYSTEM; MALTOSE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; THERMUS; TRYPTOPHAN;

THERMUS BROCKIANUS;

EID: 78650789668     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22911     Document Type: Article

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