ArticleProtein science : a publication of the Protein Society2014
Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Exploring the Causal Relationship Between Blood Metabolites and Chronic Periodontitis: Insights From Genetic Causal Analysis.Journal of cellular and molecular medicine · 2025Article
- Mining the cellular inventory of pyridoxal phosphate-dependent enzymes with functionalized cofactor mimics.Nature chemistry · 2018Article
- A Commensal Dipeptidyl Aminopeptidase with Specificity for N-Terminal Glycine Degrades Human-Produced Antimicrobial Peptides in Vitro.ACS chemical biology · 2018Article
- The Impact of Western Diet and Nutrients on the Microbiota and Immune Response at Mucosal Interfaces.Frontiers in immunology · 2017Review
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Authors and funding
15 authors at 5 institutions in 1 country.
Funding
Abstract
Pyridoxal-5'-phosphate or PLP, the active form of vitamin B6, is a highly versatile cofactor that participates in a large number of mechanistically diverse enzymatic reactions in basic metabolism. PLP-dependent enzymes account for ∼1.5% of most prokaryotic genomes and are estimated to be involved in ∼4% of all catalytic reactions, making this an important class of enzymes. Here, we structurally and functionally characterize three novel PLP-dependent enzymes from bacteria in the human microbiome: two are from Eubacterium rectale, a dominant, nonpathogenic, fecal, Gram-positive bacteria, and the third is from Porphyromonas gingivalis, which plays a major role in human periodontal disease. All adopt the Type I PLP-dependent enzyme fold and structure-guided biochemical analysis enabled functional assignments as tryptophan, aromatic, and probable phosphoserine aminotransferases.
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Registered trials
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