A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch

FEBS Letters

Volumn 588, Issue 7, 2014, Pages 1161-1167

  Peng, Hui ^a   Zheng, Yunyun ^a   Chen, Maojiao ^a   Wang, Ying ^a   Xiao, Yazhong ^a   Gao, Yi ^a  

^a ANHUI UNIVERSITY   (China)

Author keywords

Binding preference; Carbohydrate binding module; Soluble starch hydrolysis; Starch binding domain; Amylase

Indexed keywords

AMYLASE; STARCH;

ARTICLE; BINDING AFFINITY; CARBOHYDRATE BINDING MODULE; CARBOHYDRATE BINDING MODULE 20; CARBOHYDRATE BINDING MODULE 48; CARBOHYDRATE BINDING MODULE 69; CATALYSIS; CONTROLLED STUDY; ENZYME SPECIFICITY; HYDROLYSIS; MARINE BACTERIUM; MOLECULAR PHYLOGENY; PRIORITY JOURNAL; PROTEIN DOMAIN; STARCH BINDING DOMAIN;

BINDING PREFERENCE; CARBOHYDRATE-BINDING MODULE; SOLUBLE STARCH HYDROLYSIS; STARCH-BINDING DOMAIN; Α-AMYLASE;

ADSORPTION; ALPHA-AMYLASES; AMINO ACID SEQUENCE; AQUATIC ORGANISMS; BACTERIAL PROTEINS; BINDING SITES; HYDROLYSIS; KINETICS; MARKOV CHAINS; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STARCH; SUBSTRATE SPECIFICITY; VIBRIO;

EID: 84897060453     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.02.050     Document Type: Article

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