X-ray crystallographic studies of amylase 1A and 2A proteins show them to be monomers, complexed with single calcium and chloride ions (Ramasubbu et al. 1996; Brayer et al. 2000). Biochemical characterization of amylase 2A indicates that the enzyme efficiently cleaves poly-glucose chains so as to release maltose - a glucose disaccharide - from the reducing end of the chain (Braun et al. 1993; Brayer et al. 2000).
Caldwell, RM, Meisler, MH, Samuelson, LC, Wiebauer, K, Gumucio, DL
Ramasubbu, N, Luo, Y, Paloth, V, Levine, MJ, Brayer, GD
Braun, C, Wang, Y, Nguyen, NT, Brayer, GD, Overall, CM, Sidhu, G, Maurus, R, Withers, SG, Rydberg, EH
alpha-amylase activity of alpha-amylase [extracellular region]
© 2025 Reactome