RCSB PDB - 1HNY: The structure of human pancreatic alpha-amylase …
1995年6月28日 — 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 ...
Alpha-Amylase - an overview | ScienceDirect Topics
Alpha-amylase (EC 3.2.1.1) is a low-molecular-weight enzyme (approximately 45kDa) that cleaves the alpha-D- (1–4) glycan linkage of starch and glycogen. It has been in use as a diagnostic enzyme longer than any of the other enzymes. It is found in very high concentration in the pancreas in dogs and cats.
The concept of the α-amylase family: Structural similarity and …
1999年1月1日 — We proposed a general concept for an enzyme family, the α-amylase family including most of the amylases and related enzymes in 1992, based on the structural similarity and the common catalytic mechanisms. The study on neopullulanase was the key to open the door for the formulation of the concept.
The Active Center of a Mammalian .alpha.-Amylase. Structure of …
1994年5月1日 — The surface structure of a complex substrate revealed by enzyme kinetics and Freundlich constants for α-amylase interaction with the surface of starch. Biochimica et Biophysica Acta (BBA) - General Subjects 2013 , 1830 (4) , 3095-3101.
The structure of human pancreatic alpha-amylase at 1.8 A …
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 ...
The concept of the alpha-amylase family: structural similarity and ...
We proposed a general concept for an enzyme family, the alpha-amylase family including most of the amylases and related enzymes in 1992, based on the structural similarity and the common catalytic mechanisms. The study on neopullulanase was the key to open the door for the formulation of the concept.
Crystal structure of a raw-starch-degrading bacterial α-amylase ...
2017年3月17日 — α-Amylases (EC 3.2.1.1) are endo-hydrolases that act on α- (1,4)-glucosidic linkages in starch and other related oligo- and polysaccharides, thus causing the release of malto-oligosaccharides and...
Microbial α-amylase: A biomolecular overview - ScienceDirect
2017年2月1日 — Amylase is divided roughly into two categories, exoamylase and endoamylase, in terms of its distinct modes of catalysis. α-Amylase (EC.3.2.1.1), one of the most important industrial endoamylases, is capable of hydrolyzing the internal α-1,4 glycosidic linkages to glucose, maltose and dextrin while retaining the α-anomeric configuration in the pr...
The structure of human pancreatic α‐amylase at 1.8 Å resolution …
The structure of human pancreatic α-amylase has been determined to 1.8 Å resolution using X-ray diffraction techniques. This enzyme is found to be composed of three structural domains.
α-Amylase - Wikipedia
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]