Back to search

Article

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

2025-12-30

Abstract excerpt

Pyridoxal-phosphate binding proteins (PLPBP) are involved in the homeostasis of B 6 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...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
3f246b55-4d8b-5b26-a808-bccd106cc569
DOI
10.64898/2025.12.29.696868
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Mutational analyses reveal PLP-independent functions at PipY, the cyanobacterial paradigm for pyridoxal-phosphate binding proteinsDOI 10.64898/2025.12.29.696868
Select a neighboring publication to make it the new centre.