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Human, [18] [58] mouse, [57] and porcine [74] PGLYRP2 are enzymes, N-acetylmuramoyl-L-alanine amidases, that hydrolyze the amide bond between the MurNAc and L-alanine, the first amino acid in the stem peptide in bacterial cell wall peptidoglycan. The minimal peptidoglycan fragment hydrolyzed by PGLYRP2 is MurNAc-tripeptide. [58]
Peptidoglycan. The peptidoglycan layer within the bacterial cell wall is a crystal lattice structure formed from linear chains of two alternating amino sugars, namely N-acetylglucosamine (GlcNAc or NAG) and N-acetylmuramic acid (MurNAc or NAM).
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.
In 2000, Dan Hultmark and coworkers discovered a family of 12 Peptidoglycan Recognition Protein (PGRP) genes in Drosophila melanogaster and by homology searches of available human and mouse sequences predicted the presence of long forms of human and mouse PGRPs, which they named PGRP-L by analogy to long forms of insect PGRPs.
Lysozyme (EC 3.2.1.17, muramidase, N-acetylmuramide glycanhydrolase; systematic name peptidoglycan N-acetylmuramoylhydrolase) is an antimicrobial enzyme produced by animals that forms part of the innate immune system. It is a glycoside hydrolase that catalyzes the following process:
Muramyl dipeptide is a component of bacterial peptidoglycan, a recognition structure or activator for nucleotide-binding oligomerization domain 2 (NOD2) protein. [1] It is a constituent of both Gram-positive and Gram-negative bacteria composed of N-acetylmuramic acid linked by its lactic acid moiety to the N-terminus of an L-alanine D-isoglutamine dipeptide. [1]