| First Author | Gelius E | Year | 2003 |
| Journal | Biochem Biophys Res Commun | Volume | 306 |
| Issue | 4 | Pages | 988-94 |
| PubMed ID | 12821140 | Mgi Jnum | J:84303 |
| Mgi Id | MGI:2667291 | Doi | 10.1016/s0006-291x(03)01096-9 |
| Citation | Gelius E, et al. (2003) A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity. Biochem Biophys Res Commun 306(4):988-94 |
| abstractText | The family of peptidoglycan recognition proteins (PGRPs) is conserved from insects to mammals. Recently, Drosophila PGRP-SC1B was demonstrated to be an N-acetylmuramoyl-L-alanine amidase (NAMLAA), an enzyme that cleaves the lactylamide bond between muramic acid and the peptide chain in peptidoglycan (PGN). We now show an M x mPGRP-L mRNA to be expressed in the liver. The recombinant M x mPGRP-L protein has NAMLAA activity and degrades PGN from both Escherichia coli and Staphylococcus aureus; however, the Gram-positive PGN was a better substrate after lysozyme treatment. The activity of M x mPGRP-L was further analysed using Bordetella pertussis tracheal toxin as a substrate. Cleavage products were separated on HPLC and identified using mass spectrometry. From these results we conclude that M x mPGRP-L has activity and other properties identifying it as the NAMLAA protein present in mammalian sera. |
