Molecular characterization of novel pyridoxal‐5′‐phosphate‐dependent enzymes from the human microbiome. (14th June 2014)

• Record Type: Journal Article
• Authors: 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.
• Is Part Of: Protein science. Volume 23:Number 8(2014:Aug.)
• Page Start: 1060
• Page End: 1076
• Publication Date: 2014-06-14
• Subjects: Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.2493
• Languages: English
• ISSNs: 0961-8368

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <p>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 <italic>Eubacterium rectale, </italic> a dominant, nonpathogenic, fecal, Gram‐positive bacteria, and the third is from <italic>Porphyromonas gingivalis, </italic> 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.</p> </abstract>