Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzyme responsible for all of the isomaltase activity and much of the maltase activity in the small intestine of the Californian sea lion (Zalophus californianus) was isolated by detergent solubilization of the brush-border membrane, followed by immunoadsorption chromatography using antibodies directed against rabbit sucrase-isomaltase. In 0.1% Triton X-100, sea lion isomaltase occurs as a monomer of Mr = 245,000 and is composed of a single polypeptide chain. As judged from the stoichiometry of the covalent binding of the affinity label, conduritol-B-epoxide, this polypeptide chain carries two enzymatically active sites; they are apparently identical and do not show either positive or negative cooperativity. In addition to cross-reacting immunologically with rabbit sucrase-isomaltase, sea lion isomaltase has similar overall enzymatic properties, with the exception of not hydrolyzing sucrose. The Alaskan fur seal (Collarhinus ursinus) has a two-active site isomaltase; however, in contrast to the sea lion, this animal is endowed with a small but significant sucrase activity. Along with (fully active) pro-sucrase-isomaltase, sea lion isomaltase is one of the very few examples of enzymes with more than one active site on a single polypeptide chain acting "in parallel" (rather than "in series"). Furthermore, this enzyme triggers some interesting questions on the phylogenetical pedigree of small intestinal sucrase-isomaltase.
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PMID:A two-active site one-polypeptide enzyme: the isomaltase from sea lion small intestinal brush-border membrane. Its possible phylogenetic relationship with sucrase-isomaltase. 671 26

Dengue virus (DENV) is a mosquito-borne flavivirus responsible for 50-100 million human infections each year. The development of DENV chemotherapy requires high-throughput screening (HTS) assays. A dengue virus-like particle (VLP) has been constructed using viral structural proteins to package a Renilla luciferase reporter replicon. VLP could be produced by either the sequential electroporation of the replicon RNAs and the structural gene RNAs or by electroporating replicon RNA into a stable cell line expressing the structural proteins. In both approaches, the key to produce high titer VLP (3x10(6)foci-forming unit/ml) is to use low temperature (30 degrees C) in the packaging step. In addition, exogenous expression of host protease furin increased VLP infectivity. The infection could be blocked by antibodies against viral envelope protein and by an inhibitor of viral NS5 polymerase, but not by an inhibitor of host alpha-glucosidase (castanospermine). The VLP infection assay was optimized for HTS in a 384-well format with consistent and robust signal, providing a simple and rapid cell-based assay for screening inhibitors against DENV entry, translation, and replication in an HTS format.
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PMID:A high-throughput assay using dengue-1 virus-like particles for drug discovery. 2015 77