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

Mutational analyses reveal PLP-independent functions at PipY, the cyanobacterial paradigm for pyridoxal-phosphate binding proteins.

Scientific reports - 12 Mar 2026

Llop Antonio, Tremiño Lorena, Contreras Asunción

Abstract excerpt

Pyridoxal-phosphate binding proteins (PLPBP) are involved in the homeostasis of B6 vitamers and amino/keto acids, share a high degree of sequence conservation and are represented in all three domains of life. Despite the obligate presence of the catalyst cofactor PLP, attempts to show enzymatic activity have been unsuccessful. Instead, evidence of RNA binding activity has been provided for several members of the...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Carrier Proteins

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

Share to DNA Mutational Analysis

Share to Mutation

Share to Phenotype

Share to Protein Binding

Share to Pyridoxal Phosphate

Share to Synechococcus

Source

Open in PubMed Open full text

Identifiers

PMID: 41820517
DOI: 10.1038/s41598-026-43837-6
PMCID: PMC13102913

Genes

PLPBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 19 Oct 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

Mutational analyses reveal PLP-independent functions at PipY, the cyanobacterial paradigm for pyridoxal-phosphate binding proteins.PMID 41820517Read ↗

Mutational analyses reveal PLP-independent functions at PipY, the cyanobacterial paradigm for pyridoxal-phosphate binding proteinsSemantic proximity Read ↗

Purine limitation prevents the exogenous pyridoxal 5'-phosphate accumulation of Salmonella enterica yggS mutants.Semantic proximity Read ↗

Mutations at pipX suppress lethality of PII-deficient mutants of Synechococcus elongatus PCC 7942.Semantic proximity Read ↗

Protein-protein interfaces as druggable targets: A common motif of the pyridoxal-5’-phosphate-dependent enzymes to receive the coenzyme from its producersSemantic proximity Read ↗

Identification of six new photoactive yellow proteins--diversity and structure-function relationships in a bacterial blue light photoreceptor.Semantic proximity Read ↗

Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: a flexible flap subdomain controls access to the catalytic site.Semantic proximity Read ↗

PLPMDB: pyridoxal-5'-phosphate dependent enzymes mutants database.Semantic proximity Read ↗

The Role of YggS in Vitamin B6 Homeostasis in Salmonella enterica Is Informed by Heterologous Expression of Yeast SNZ3.Semantic proximity Read ↗

Structure-function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria.Semantic proximity Read ↗

Evaluation of the effects of P(II) deficiency and the toxicity of PipX on growth characteristics of the P(II)-Less mutant of the cyanobacterium Synechococcus elongatus.Semantic proximity Read ↗

Polyphosphate Kinase 2 (PPK2) Enzymes: Structure, Function, and Roles in Bacterial Physiology and VirulenceSemantic proximity Read ↗

The inhibitory mechanism of Hal3 on the yeast Ppz1 phosphatase: A mutagenesis analysis.Semantic proximity Read ↗

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