Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification and molecular characterization of an N-acetylmuramyl-L-alanine amidase Sle1 involved in cell separation of Staphylococcus aureus.

Molecular microbiology - 1 Nov 2005

Kajimura Junko, Fujiwara Tamaki, Yamada Sakuo, Suzawa Yoshika, Nishida Tetsuya, Oyamada Yoshihiro, Hayashi Ikue, Yamagishi Jun-ichi, Komatsuzawa Hitoshi, Sugai Motoyuki

Abstract excerpt

We purified a peptidoglycan hydrolase involved in cell separation from a Staphylococcus aureus atl null mutant and identified its gene. Characterization of the gene product shows a 32 kDa N-acetylmuramyl-L-alanine amidase that we designated Sle1. Analysis of peptidoglycan digests showed Sle1 preferentially cleaved N-acetylmuramyl-L-Ala bonds in dimeric cross-bridges that interlink the two murein strands in the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to Microscopy, Electron

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Weight

Share to N-Acetylmuramoyl-L-alanine Amidase

Share to Peptidoglycan

Share to Staphylococcal Infections

Share to Staphylococcus aureus

Share to Virulence Factors

Source

Identifiers

PMID: 16262792
DOI: 10.1111/j.1365-2958.2005.04881.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and molecular characterization of an N-acetylmuramyl-L-alanine amidase Sle1 involved in cell separation of Staphylococcus aureus.PMID 16262792Read ↗

Functional and structural analysis of the major amidase (Atl) in Staphylococcus.Semantic proximity Read ↗

Molecular characterization of an atl null mutant of Staphylococcus aureus.Semantic proximity Read ↗

Functional profiling of CHAP domain-containing peptidoglycan hydrolases of Staphylococcus aureus USA300 uncovers potential targets for anti-staphylococcal therapiesSemantic proximity Read ↗

Contribution of the Staphylococcus aureus Atl AM and GL murein hydrolase activities in cell division, autolysis, and biofilm formation.Semantic proximity Read ↗

New insights in the coordinated amidase and glucosaminidase activity of the major autolysin (Atl) in Staphylococcus aureus.Semantic proximity Read ↗

Determinants of murein hydrolase targeting to cross-wall of Staphylococcus aureus peptidoglycan.Semantic proximity Read ↗

The Sle1 Cell Wall Amidase Controls Daughter Cell Splitting, Cell Size, and β-Lactam Resistance in Community Acquired Methicillin Resistant <i>Staphylococcus aureus</i> USA300Semantic proximity Read ↗

Functional Characterization of the N-Acetylmuramyl-l-Alanine Amidase, Ami1, from Mycobacterium abscessus.Semantic proximity Read ↗

LytN, a murein hydrolase in the cross-wall compartment of Staphylococcus aureus, is involved in proper bacterial growth and envelope assembly.Semantic proximity Read ↗

Staphylococcus aureus cell wall structure and dynamics during host-pathogen interactionSemantic proximity Read ↗

Subcellular localization of the major autolysin, ATL and its processed proteins in Staphylococcus aureus.Semantic proximity Read ↗

The active repertoire of <i>Escherichia coli</i> peptidoglycan amidases varies with physiochemical environmentSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.