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

Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophage.

FEMS microbiology letters - 15 Dec 1992

López R, García J L, García E, Ronda C, García P

Abstract excerpt

The development of an appropriate technique for the identification of autolysin-defective mutants of pneumococcus has been a fundamental step to carry out studies on the molecular characteristics of the lytic enzymes of Streptococcus pneumoniae and its bacteriophage. Our results show that the principal pneumococcal autolysin (an amidase) is responsible for the separation of the daughter cells at the end of the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cell Wall
Share to Genes, Bacterial

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

Share to Molecular Sequence Data

Share to N-Acetylmuramoyl-L-alanine Amidase

Share to Phenotype

Share to Sequence Homology, Amino Acid

Share to Streptococcus pneumoniae

Source

Identifiers

PMID: 1362174
DOI: 10.1111/j.1574-6968.1992.tb14074.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

Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophage.PMID 1362174Read ↗

The Pneumococcal Cell Wall Degrading Enzymes: A Modular Design to Create New Lysins?Semantic proximity Read ↗

Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophageSemantic proximity Read ↗

The lytic enzyme of the pneumococcal phage Dp‐1: a chimeric lysin of intergeneric originSemantic proximity Read ↗

Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin.Semantic proximity Read ↗

Pneumococcal surface proteins: when the whole is greater than the sum of its partsSemantic proximity Read ↗

Lysogeny in Streptococcus pneumoniaeSemantic proximity Read ↗

The Autolysin LytA Contributes to Efficient Bacteriophage Progeny Release in <i>Streptococcus pneumoniae</i>Semantic proximity Read ↗

PL3 Amidase, a Tailor-made Lysin Constructed by Domain Shuﬄing with Potent Killing Activity against Pneumococci and Related SpeciesSemantic proximity Read ↗

Dynamic capsule restructuring by the main pneumococcal autolysin LytA in response to the epithelium.Semantic proximity Read ↗

Structure-based functional studies for the cellular recognition and cytolytic mechanism of pneumolysin from Streptococcus pneumoniae.Semantic proximity Read ↗

The autolysin-encoding gene (lytA) of Streptococcus pneumoniae displays restricted allelic variation despite localized recombination events with genes of pneumococcal bacteriophage encoding cell wall lytic enzymes.Semantic proximity Read ↗

Structure of the pneumococcal l,d-carboxypeptidase DacB and pathophysiological effects of disabled cell wall hydrolases DacA and DacB.Semantic proximity Read ↗

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