PGLYRP2
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PGLYRP2
Peptidoglycan recognition protein 2 (PGLYRP2) is an enzyme (EC 3.5.1.28), N-acetylmuramoyl-L-alanine amidase, ''N''-acetylmuramoyl-L-alanine amidase (NAMLAA), that hydrolyzes Bacteria, bacterial cell wall peptidoglycan and is encoded by the ''PGLYRP2'' gene. Discovery The ''N''-acetylmuramoyl-L-alanine amidase enzymatic activity was first observed in human and mouse Serum (blood), serum in 1981 by Branko Ladešić and coworkers. The enzyme (abbreviated NAMLAA) was then purified from human serum by this and other groups. The sequence of 15 N-terminal amino acids of NAMLAA was identified, but the Complementary DNA, cDNA for the protein was not cloned and the gene encoding NAMLAA was not known. In 2000, Dan Hultmark and coworkers discovered a family of 12 Peptidoglycan recognition protein, Peptidoglycan Recognition Protein (PGRP) genes in Drosophila melanogaster, ''Drosophila'' ''melanogaster'' and by homology searches of available human and mouse sequences predicted the presence of ...
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Peptidoglycan Recognition Protein
Peptidoglycan recognition proteins (PGRPs) are a group of highly conserved pattern recognition receptors with at least one peptidoglycan recognition domain capable of recognizing the peptidoglycan component of the cell wall of bacteria. They are present in insects, mollusks, echinoderms and chordates. The mechanism of action of PGRPs varies between taxa. In insects, PGRPs kill bacteria indirectly by activating one of four unique effector pathways: prophenoloxidase cascade, Toll pathway, IMD pathway, and induction of phagocytosis. In mammals, PGRPs either kill bacteria directly by interacting with their cell wall or outer membrane, or hydrolyze peptidoglycan. They also modulate inflammation and microbiome and interact with host receptors. Discovery 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 specif ...
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