ArticleJournal of bacteriology2001
Isolation of PDX2, a second novel gene in the pyridoxine biosynthesis pathway of eukaryotes, archaebacteria, and a subset of eubacteria.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 81 citations in OpenAlex.
- Production of l-Theanine by Escherichia coli in the Absence of Supplemental Ethylamine.Applied and environmental microbiology · 2021Article
- Underground metabolism facilitates the evolution of novel pathways for vitamin B6 biosynthesis.Applied microbiology and biotechnology · 2021Review
- A Survey of Pyridoxal 5'-Phosphate-Dependent Proteins in the Gram-Positive Model BacteriumFrontiers in molecular biosciences · 2019Review
- De Novo Transcriptome Assembly in Shiraia bambusicola to Investigate Putative Genes Involved in the Biosynthesis of Hypocrellin A.International journal of molecular sciences · 2016Article
- Consequences of a deficit in vitamin B6 biosynthesis de novo for hormone homeostasis and root development in Arabidopsis.Plant physiology · 2015Article
- Genes of the de novo and Salvage Biosynthesis Pathways of Vitamin B6 are Regulated under Oxidative Stress in the Plant Pathogen Rhizoctonia solani.Frontiers in microbiology · 2015Article
- The pseudoenzyme PDX1.2 boosts vitamin B6 biosynthesis under heat and oxidative stress in Arabidopsis.The Journal of biological chemistry · 2014Article
- Strategies for vitamin B6 biofortification of plants: a dual role as a micronutrient and a stress protectant.Frontiers in plant science · 2013Article
- It takes two to tango: defining an essential second active site in pyridoxal 5'-phosphate synthase.PloS one · 2011Article
- Article
- Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima.Biochemistry · 2006Article
- Flavin adenine dinucleotide-dependent 4-phospho-D-erythronate dehydrogenase is responsible for the 4-phosphohydroxy-L-threonine pathway in vitamin B6 biosynthesis in Sinorhizobium meliloti.Journal of bacteriology · 2006Article
- Vitamin B6 biosynthesis in higher plants.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Amiloride uptake and toxicity in fission yeast are caused by the pyridoxine transporter encoded by bsu1+ (car1+).Eukaryotic cell · 2005Article
- Pyridoxine biosynthesis in yeast: participation of ribose 5-phosphate ketol-isomerase.The Biochemical journal · 2004Article
- Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis.Journal of bacteriology · 2004Article
- Cercosporin-deficient mutants by plasmid tagging in the asexual fungus Cercospora nicotianae.Molecular genetics and genomics : MGG · 2003Article
- Expression of the cercosporin toxin resistance gene ( CRG1) as a dicistronic mRNA in the filamentous fungus Cercospora nicotianae.Current genetics · 2003Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper we describe the isolation of a second gene in the newly identified pyridoxine biosynthesis pathway of archaebacteria, some eubacteria, fungi, and plants. Although pyridoxine biosynthesis has been thoroughly examined in Escherichia coli, recent characterization of the Cercospora nicotianae biosynthesis gene PDX1 led to the discovery that most organisms contain a pyridoxine synthesis gene not found in E. coli. PDX2 was isolated by a degenerate primer strategy based on conserved sequences of a gene specific to PDX1-containing organisms. The role of PDX2 in pyridoxine biosynthesis was confirmed by complementation of two C. nicotianae pyridoxine auxotrophs not mutant in PDX1. Also, targeted gene replacement of PDX2 in C. nicotianae results in pyridoxine auxotrophy. Comparable to PDX1, PDX2 homologues are not found in any of the organisms with homologues to the E. coli pyridoxine genes, but are found in the same archaebacteria, eubacteria, fungi, and plants that contain PDX1 homologues. PDX2 proteins are less well conserved than their PDX1 counterparts but contain several protein motifs that are conserved throughout all PDX2 proteins.
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