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The first PGRP was discovered in 1996 by Masaaki Ashida and coworkers, who purified a 19 kDa protein present in the hemolymph and cuticle of a silkworm (Bombyx mori), and named it Peptidoglycan Recognition Protein, because it specifically bound peptidoglycan and activated the prophenoloxidase cascade. [5]
Location of human PGLYRP1 gene on chromosome 19 and schematic gene, cDNA, and protein structures with exons, introns, and protein domains indicated. Peptidoglycan recognition protein 1, PGLYRP1, also known as TAG7, is an antibacterial and pro-inflammatory innate immunity protein that in humans is encoded by the PGLYRP1 gene. [5] [6] [7] [8]
Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like layer (sacculus) that surrounds the bacterial cytoplasmic membrane. [1] The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM).
This layered structure is called peptidoglycan (formerly called murein). GlcNAc is the monomeric unit of the polymer chitin, which forms the exoskeletons of arthropods like insects and crustaceans. It is the main component of the radulas of mollusks, the beaks of cephalopods, and a major component of the cell walls of most fungi.
Lysozyme Identifiers EC no. 3.2.1.17 CAS no. 9001-63-2 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Gene Ontology AmiGO / QuickGO Search PMC articles PubMed articles NCBI proteins Protein family Glycoside hydrolase, family 22, lysozyme Lysozyme crystals stained with methylene ...
The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria comprises a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages: formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc).
For these 67 diseases, the median detection rate using the protein signature was 45.5% compared with 25% when just the clinical model was used, with a 10% false positive rate. These diseases included:
N-acetylmuramoyl-L-alanine amidase cwlA precursor (cell wall hydrolase, autolysin, EC 3.5.1.28) Autolytic lysozyme (1,4-beta-N-acetylmuramidase, autolysin, EC 3.2.1.17) Membrane-bound lytic murein transglycosylase B; Zinc-containing D-alanyl-D-alanine-cleaving carboxypeptidase, VanX. [5] Many of the proteins having this domain are as yet ...