Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome
| Autor: | Fleischman, Nicholas M, Das, Debanu, Kumar, Abhinav, Xu, Qingping, Chiu, Hsiu-Ju, Jaroszewski, Lukasz, Knuth, Mark W, Klock, Heath E, Miller, Mitchell D, Elsliger, Marc-André, Godzik, Adam, Lesley, Scott A, Deacon, Ashley M, Wilson, Ian A, Toney, Michael D |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
crystal structure
Crystallography Eubacterium Protein Conformation Microbiota biochemical characterization 1.1 Normal biological development and functioning Biophysics Molecular human microbiome Computation Theory and Mathematics structural genomics Models PLP-dependent enzymes Underpinning research Pyridoxal Phosphate X-Ray Humans Biochemistry and Cell Biology Oxidoreductases Other Information and Computing Sciences Porphyromonas gingivalis Transaminases Protein Structure Initiative |
| Zdroj: | Protein science : a publication of the Protein Society, vol 23, iss 8 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|