A novel GH13 subfamily of α-amylases with a pair of tryptophans in the helix α3 of the catalytic TIM-barrel, the LPDlx signature in the conserved sequence region V and a conserved aromatic motif at the C-terminus

Domain C of thermostable α-amylase of Geobacillus thermoleovorans mediates raw starch adsorption

(2014) Deepika Mehta et al.   APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase fromPyrococcussp. ST04

(2014) Kwang-Hyun Park et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

The carbohydrate-active enzymes database (CAZy) in 2013

(2013) Vincent Lombard et al.   NUCLEIC ACIDS RESEARCH

GenBank

(2013) Dennis A. Benson et al.   NUCLEIC ACIDS RESEARCH

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

Cloning and characterization of two new thermostable and alkalitolerant α-amylases from the Anoxybacillus species that produce high levels of maltose

(2012) Yen Yen Chai et al.   JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY

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

(2011) Yang Liu et al.   MARINE BIOTECHNOLOGY