Role of the conserved pyridoxal 5ʹ-phosphate-binding protein YggS/PLPBP in vitamin B6 and amino acid homeostasis

Author:

Ito Tomokazu1

Affiliation:

1. Department of Applied Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University , Furou-chou, Chikusa, Nagoya, Aichi, Japan

Abstract

ABSTRACT The YggS/PLPBP protein (also called COG0325 or PLPHP) is a conserved pyridoxal 5ʹ-phosphate (PLP)-binding protein present in all 3 domains of life. Recent studies have demonstrated that disruption or mutation of this protein has multifaceted effects in various organisms, including vitamin B6-dependent epilepsy in humans. In Escherichia coli, disruption of this protein—encoded by yggS—perturbs Thr-Ile/Val metabolism, one-carbon metabolism, coenzyme A synthesis, and vitamin B6 homeostasis. This protein is critical for maintaining low levels of pyridoxine 5ʹ-phosphate (PNP) in various organisms. In the yggS-deficient E. coli strain, inhibition of PLP-dependent enzymes, such as the glycine cleavage system by PNP, is the root cause of metabolic perturbation. Our data suggest that the YggS/PLPBP protein may be involved in the balancing of B6 vitamers by mediating efficient turnover of protein-bound B6 vitamers. This paper reviews recent findings on the function of the YggS/PLPBP protein.

Funder

JSPS

Asahi Glass Foundation

Institute for Fermentation, Osaka

Lotte Foundation

Amano Enzyme Foundation

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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