期刊
PROTEIN SCIENCE
卷 23, 期 8, 页码 1060-1076出版社
WILEY
DOI: 10.1002/pro.2493
关键词
human microbiome; PLP-dependent enzymes; crystal structure; biochemical characterization; structural genomics; Protein Structure Initiative
资金
- Protein Structure Initiative [U54 GM094586]
- NIGMS Administrative Supplement for Functional Studies [3R01GM054779-13S1]
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 similar to 1.5% of most prokaryotic genomes and are estimated to be involved in similar to 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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