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B6db references: 26872910.

type Journal Article
authors Prunetti L, El Yacoubi B, Schiavon CR, Kirkpatrick E, Huang L, Bailly M, ElBadawi-Sidhu M, Harrison K, Gregory JF, Fiehn O, Hanson AD, de Crécy-Lagard V
title Evidence That COG0325 Proteins are involved in PLP Homeostasis
journal Microbiology
Activity unclassified
sel selected
ui 26872910
year (2016)
volume 195
number 162
pages 694-706
keywords doi: 10.1099/mic.0.000255
abstract Pyridoxal 5'-phosphate (PLP) is an essential cofactor for nearly 60 Escherichia coli enzymes but is a highly reactive molecule that is toxic in its free form. How PLP levels are regulated and how PLP is delivered to target enzymes are still open questions. The COG0325 protein family belongs to the fold-type III class of PLP enzymes and binds PLP but has no known biochemical activity although it occurs in all kingdoms of life. Various pleiotropic phenotypes of the Escherichia coli COG0325 (yggS) mutant have been reported, some of which were reproduced and extended in this study. Comparative genomic, genetic and metabolic analyses suggest that these phenotypes reflect an imbalance in pyridoxal 5'-phosphate (PLP) homeostasis. The E. coli yggS mutant accumulates the PLP precursor pyridoxine 5'-phosphate (PNP), and is sensitive to an excess of pyridoxine but not of pyridoxal. The pyridoxine toxicity phenotype is complemented by the expression of eukaryotic yggS orthologs. It is also suppressed by the presence of amino acids specifically isoleucine, threonine and leucine suggesting the PLP dependent enzyme transaminase B (IlvE) is affected. These genetic results lay a foundation for future biochemical studies of the role of COG0325 proteins in PLP homeostasis.
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last changed 2019/05/28 09:44

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