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Protein Sci. 2014 Aug;23(8):1060-76. doi: 10.1002/pro.2493. Epub 2014 Jun 14.

Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.

Author information

1
Department of Chemistry, University of California, Davis, California, 95616.

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.

KEYWORDS:

PLP-dependent enzymes; Protein Structure Initiative; biochemical characterization; crystal structure; human microbiome; structural genomics

PMID:
24888348
PMCID:
PMC4116655
DOI:
10.1002/pro.2493
[Indexed for MEDLINE]
Free PMC Article

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