Functional analysis of PDX2 from arabidopsis, a glutaminase involved in vitamin B6 biosynthesis

Tambasco-Studart, Marina, Tews, Ivo, Amrhein, Nikolaus and Fitzpatrick, Teresa B (2007) Functional analysis of PDX2 from arabidopsis, a glutaminase involved in vitamin B6 biosynthesis. Plant Physiology, 144, (2), 915-925. (doi:10.1104/pp.107.096784). (PMID:17144654).


[img] PDF (Original Article) - Version of Record
Restricted to System admin

Download (977Kb) | Request a copy
[img] PDF (Supplement) - Supplemental Material
Restricted to System admin

Download (3595Kb) | Request a copy


Vitamin B6 is an essential metabolite in all organisms, being required as a cofactor for a wide variety of biochemical reactions. De novo biosynthesis of the vitamin occurs in microorganisms and plants, but animals must obtain it from their diet. Two distinct and mutually exclusive de novo pathways have been identified to date, namely deoxyxylulose 5-phosphate dependent, which is restricted to a subset of eubacteria, and deoxyxylulose 5-phosphate independent, present in archaea, fungi, plants, protista, and most eubacteria. In these organisms, pyridoxal 5'-phosphate (PLP) formation is catalyzed by a single glutamine amidotransferase (PLP synthase) composed of a glutaminase domain, PDX2, and a synthase domain, PDX1. Despite plants being an important source of vitamin B6, very little is known about its biosynthesis. Here, we provide information for Arabidopsis thaliana. The functionality of PDX2 is demonstrated, using both in vitro and in vivo analyses. The expression pattern of PDX2 is assessed at both the RNA and protein level, providing insight into the spatial and temporal pattern of vitamin B6 biosynthesis. We then provide a detailed biochemical analysis of the plant PLP synthase complex. While the active sites of PDX1 and PDX2 are remote from each other, coordination of catalysis is much more pronounced with the plant proteins than its bacterial counterpart, Bacillus subtilis. Based on a model of the PDX1/PDX2 complex, mutation of a single residue uncouples enzyme coordination and in turn provides tangible evidence for the existence of the recently proposed ammonia tunnel through the core of PDX1.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1104/pp.107.096784
ISSNs: 0032-0889 (print)
0032-0889 (electronic)
Related URLs:
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QK Botany
Divisions : Faculty of Natural and Environmental Sciences > Biological Sciences
ePrint ID: 200597
Accepted Date and Publication Date:
June 2007Published
Date Deposited: 01 Nov 2011 14:11
Last Modified: 31 Mar 2016 13:45
Vitamin biosynthesis as a target for antimalarial therapy (VITBIOMAL)
Funded by: European Commission - FP6 (12158)
1 June 2005 to 31 August 2007

Actions (login required)

View Item View Item

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics