α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]

Alpha-amylase begins the process of starch digestion. It takes starch chains and breaks them into smaller pieces with two or three glucose units. Two similar types of amylase are made in your body--one is secreted in saliva, where it starts to break down starch grains as you chew, and the other is secreted by the pancreas, where it finishes its ...

The structure of human pancreatic alpha-amylase has been determined to 1.8 A resolution using X-ray diffraction techniques. This enzyme is found to be composed of three structural domains. The largest is Domain A (residues 1-99, 169-404), which forms a central eight-stranded parallel beta-barrel, to one end of which are located the active site ...

1998年12月3日 · Crystal structures of human pancreatic alpha-amylase (HPA) in complex with naturally occurring inhibitors have been solved. The tetrasaccharide acarbose and a pseudo-pentasaccharide of the trestatin family produced identical continuous electron densities corresponding to a pentasaccharide species, spanning the -3 to +2 subsites of the enzyme ...

The structure of human pancreatic alpha-amylase has been determined to 1.8 A resolution using X-ray diffraction techniques. This enzyme is found to be composed of three structural domains. The largest is Domain A (residues 1-99, 169-404), which forms a central eight-stranded parallel beta-barrel, to one end of which are located the active site ...

Two computerized methods of predicting protein secondary structure from amino acid sequences are evaluated by using them on the alpha-amylase of Aspergillus oryzae, for which the three-dimensional structure has been determined. The methods are then used, with amino acid alignments, to predict the st …

α-Amylase (EC 3.2.1.1) represents the best known amylolytic enzyme. It catalyzes the hydrolysis of α-1,4-glucosidic bonds in starch and related α-glucans. In general, the α-amylase is an enzyme with a broad substrate preference and product specificity.

2020年7月1日 · Generally, the elements of α-amylase structure that provides an optimum activity at lower or higher pH are related to the sum of each aspect affecting the overall pKa of the enzyme, such as electrostatic and hydrophobic effects, hydrogen bonding and the global dynamics of the active center.

2001年3月9日 · In the crystal structure of the closely related maltogenic ‘amylase’ (also referred to as cyclodextrinase or CDase) from Thermus sp., the domain N of one monomer of a dimer has been suggested to be involved in the enzyme specificity through its interaction with the active site region of the other monomer [18].

On this page, you can see the structure of human salivary α-amylase. In general, α-amylase is an enzyme that catalyzes the hydrolysis of α-1,4 gulcan linkages in starch. It is found widely among all three kingdoms of life. The following will highlight important structural aspects related to the function of α-amylase.