 N-Acetylmuramoyl-L-alanine Amidase
"N-Acetylmuramoyl-L-alanine Amidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.
| Descriptor ID |
D009238
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| MeSH Number(s) |
D08.811.277.087.030
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| Concept/Terms |
N-Acetylmuramoyl-L-alanine Amidase- N-Acetylmuramoyl-L-alanine Amidase
- Amidase, N-Acetylmuramoyl-L-alanine
- N Acetylmuramoyl L alanine Amidase
- Mucopeptide Amidohydrolase
- Amidohydrolase, Mucopeptide
- Peptidoglycan Hydrolase
- Hydrolase, Peptidoglycan
- LE-Enzyme
- LE Enzyme
- Murein Hydrolase
- Hydrolase, Murein
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Below are MeSH descriptors whose meaning is more general than "N-Acetylmuramoyl-L-alanine Amidase".
Below are MeSH descriptors whose meaning is more specific than "N-Acetylmuramoyl-L-alanine Amidase".
This graph shows the total number of publications written about "N-Acetylmuramoyl-L-alanine Amidase" by people in this website by year, and whether "N-Acetylmuramoyl-L-alanine Amidase" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
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| 1996 | 1 | 0 | 1 | | 1997 | 1 | 0 | 1 | | 2003 | 0 | 1 | 1 | | 2006 | 1 | 0 | 1 | | 2011 | 1 | 0 | 1 | | 2012 | 0 | 2 | 2 | | 2013 | 1 | 0 | 1 | | 2015 | 1 | 0 | 1 | | 2018 | 1 | 0 | 1 |
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Below are the most recent publications written about "N-Acetylmuramoyl-L-alanine Amidase" by people in Profiles.
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Bobrovskyy M, Willing SE, Schneewind O, Missiakas D. EssH Peptidoglycan Hydrolase Enables Staphylococcus aureus Type VII Secretion across the Bacterial Cell Wall Envelope. J Bacteriol. 2018 10 15; 200(20).
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Hwang J, Kim HS. Cell Wall Recycling-Linked Coregulation of AmpC and PenB ß-Lactamases through ampD Mutations in Burkholderia cenocepacia. Antimicrob Agents Chemother. 2015 Dec; 59(12):7602-10.
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Chen C, Krishnan V, Macon K, Manne K, Narayana SV, Schneewind O. Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus. J Biol Chem. 2013 Oct 11; 288(41):29440-52.
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Paganelli FL, Willems RJ, Jansen P, Hendrickx A, Zhang X, Bonten MJ, Leavis HL. Enterococcus faecium biofilm formation: identification of major autolysin AtlAEfm, associated Acm surface localization, and AtlAEfm-independent extracellular DNA Release. mBio. 2013 Apr 16; 4(2):e00154.
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Lunderberg JM, Nguyen-Mau SM, Richter GS, Wang YT, Dworkin J, Missiakas DM, Schneewind O. Bacillus anthracis acetyltransferases PatA1 and PatA2 modify the secondary cell wall polysaccharide and affect the assembly of S-layer proteins. J Bacteriol. 2013 Mar; 195(5):977-89.
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Wang YT, Oh SY, Hendrickx AP, Lunderberg JM, Schneewind O. Bacillus cereus G9241 S-layer assembly contributes to the pathogenesis of anthrax-like disease in mice. J Bacteriol. 2013 Feb; 195(3):596-605.
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Frankel MB, Schneewind O. Determinants of murein hydrolase targeting to cross-wall of Staphylococcus aureus peptidoglycan. J Biol Chem. 2012 Mar 23; 287(13):10460-10471.
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Frankel MB, Hendrickx AP, Missiakas DM, Schneewind O. LytN, a murein hydrolase in the cross-wall compartment of Staphylococcus aureus, is involved in proper bacterial growth and envelope assembly. J Biol Chem. 2011 Sep 16; 286(37):32593-605.
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Stojkovic EA, Rothman-Denes LB. Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. J Mol Biol. 2007 Feb 16; 366(2):406-19.
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Marraffini LA, Schneewind O. Anchor structure of staphylococcal surface proteins. V. Anchor structure of the sortase B substrate IsdC. J Biol Chem. 2005 Apr 22; 280(16):16263-71.
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