ArticlePloS one2011
It takes two to tango: defining an essential second active site in pyridoxal 5'-phosphate synthase.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- PLP Homeostasis Protein Is Required for Efficient Maturation of Aromatic Amino Acid Aminotransferase in Salmonella enterica.Molecular microbiology · 2026Article
- Functional analysis ofFrontiers in plant science · 2025Article
- Increasing 1,4-Diaminobutane Production inMolecules (Basel, Switzerland) · 2024Article
- Enhancement of vitamin BThe Plant journal : for cell and molecular biology · 2019Article
- Article
- Multiple roles for Vitamin BScientific reports · 2019Article
- Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis.Nature chemical biology · 2017Article
- PipY, a Member of the Conserved COG0325 Family of PLP-Binding Proteins, Expands the Cyanobacterial Nitrogen Regulatory Network.Frontiers in microbiology · 2017Article
- Structural definition of the lysine swing in Arabidopsis thaliana PDX1: Intermediate channeling facilitating vitamin B6 biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Inactive mutants of human pyridoxine 5'-phosphate oxidase: a possible role for a noncatalytic pyridoxal 5'-phosphate tight binding site.FEBS open bio · 2016Article
- Engineering a pyridoxal 5'-phosphate supply for cadaverine production by using Escherichia coli whole-cell biocatalysis.Scientific reports · 2015Article
- Crystal structures capture three states in the catalytic cycle of a pyridoxal phosphate (PLP) synthase.The Journal of biological chemistry · 2015Article
- The pseudoenzyme PDX1.2 boosts vitamin B6 biosynthesis under heat and oxidative stress in Arabidopsis.The Journal of biological chemistry · 2014Article
- Pyridoxal 5'-phosphate is a slow tight binding inhibitor of E. coli pyridoxal kinase.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prevalent de novo biosynthetic pathway of vitamin B6 involves only two enzymes (Pdx1 and Pdx2) that form an ornate multisubunit complex functioning as a glutamine amidotransferase. The synthase subunit, Pdx1, utilizes ribose 5-phosphate and glyceraldehyde 3-phosphate, as well as ammonia derived from the glutaminase activity of Pdx2 to directly form the cofactor vitamer, pyridoxal 5'-phosphate. Given the fact that a single enzyme performs the majority of the chemistry behind this reaction, a complicated mechanism is anticipated. Recently, the individual steps along the reaction co-ordinate are beginning to be unraveled. In particular, the binding of the pentose substrate and the first steps of the reaction have been elucidated but it is not known if the latter part of the chemistry, involving the triose sugar, takes place in the same or a disparate site. Here, we demonstrate through the use of enzyme assays, enzyme kinetics, and mutagenesis studies that indeed a second site is involved in binding the triose sugar and moreover, is the location of the final vitamin product, pyridoxal 5'-phosphate. Furthermore, we show that product release is triggered by the presence of a PLP-dependent enzyme. Finally, we provide evidence that a single arginine residue of the C terminus of Pdx1 is responsible for coordinating co-operativity in this elaborate protein machinery.
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