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

Preferential and rapid degradation of raw rice starch by an α-amylase of glycoside hydrolase subfamily GH13_37

(2012) Yin Lei et al.   APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals

(2011) Štefan Janeček et al.   ENZYME AND MICROBIAL TECHNOLOGY

Identification and Phylogenetic Characterization of a New Subfamily of α-Amylase Enzymes from Marine Microorganisms

(2011) Yang Liu et al.   MARINE BIOTECHNOLOGY

CDD: a Conserved Domain Database for the functional annotation of proteins

(2010) A. Marchler-Bauer et al.   NUCLEIC ACIDS RESEARCH

SusG: A Unique Cell-Membrane-Associated α-Amylase from a Prominent Human Gut Symbiont Targets Complex Starch Molecules

(2010) Nicole M. Koropatkin et al.   STRUCTURE

Recent Advances in Microbial Raw Starch Degrading Enzymes

(2009) Haiyan Sun et al.   APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY

The carbohydrate-binding module family 20 - diversity, structure, and function

(2009) Camilla Christiansen et al.   FEBS Journal

Domain evolution in the GH13 pullulanase subfamily with focus on the carbohydrate-binding module family 48

(2008) Martin Machovič et al.   BIOLOGIA

Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues

(2008) Hsu-Yang Lin et al.   EXTREMOPHILES

The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

(2008) B. L. Cantarel et al.   NUCLEIC ACIDS RESEARCH