The pyridoxal kinase gene TaPdxK from wheat complements vitamin B6 synthesis-defective Escherichia coli

Pyridoxal kinase (EC 2.7.1.35) is a key enzyme in the conversion of vitamin B6 to pyridoxal 5'-phosphate (PLP). PLP is the crucial cofactor required by numerous enzymes involved in amino acids metabolism. Recently, studies with Arabidopsis salt overly sensitive 4 mutants demonstrated that pyrid...

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Veröffentlicht in:Journal of plant physiology. - 1979. - 161(2004), 9 vom: 20. Sept., Seite 1053-60
1. Verfasser: Wang, Huabo (VerfasserIn)
Weitere Verfasser: Liu, Dongcheng, Liu, Chunguang, Zhang, Aimin
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Comparative Study Journal Article Research Support, Non-U.S. Gov't DNA, Complementary Vitamin B 6 8059-24-3 Pyridoxal Kinase EC 2.7.1.35
Beschreibung
Zusammenfassung:Pyridoxal kinase (EC 2.7.1.35) is a key enzyme in the conversion of vitamin B6 to pyridoxal 5'-phosphate (PLP). PLP is the crucial cofactor required by numerous enzymes involved in amino acids metabolism. Recently, studies with Arabidopsis salt overly sensitive 4 mutants demonstrated that pyridoxal kinase is a novel salt tolerance determinant important for the regulation of Na+ and K+ homeostasis in plants. We describe here the TaPdxK gene which encodes a pyridoxal kinase, cloned from Triticum aestivum by RACE PCR method. The putative amino acid sequence of TaPdxK is 78% identical to Arabidopsis AtSOS4. Southern analysis suggests that there are at least two copies of pyridoxal kinase genes in wheat genome. The expression of TaPdxK cDNAs complements an Escherichia coli mutant defective in pyridoxal kinase. TaPdxK transcripts were detected in roots, shoots, spikes and anthers by RT-PCR analysis. TaPdxK expression level was not regulated by salt, ABA, and osmotic stress
Beschreibung:Date Completed 12.04.2005
Date Revised 30.09.2020
published: Print
Citation Status MEDLINE
ISSN:1618-1328