The University of Southampton
University of Southampton Institutional Repository

Two independent routes of de novo vitamin B6 biosynthesis: not that different after all

Two independent routes of de novo vitamin B6 biosynthesis: not that different after all
Two independent routes of de novo vitamin B6 biosynthesis: not that different after all
Vitamin B6 is well known in its biochemically active form as pyridoxal 5'-phosphate, an essential cofactor of numerous metabolic enzymes. The vitamin is also implicated in numerous human body functions ranging from modulation of hormone function to its recent discovery as a potent antioxidant. Its de novo biosynthesis occurs only in bacteria, fungi and plants, making it an essential nutrient in the human diet. Despite its paramount importance, its biosynthesis was predominantly investigated in Escherichia coli, where it is synthesized from the condensation of deoxyxylulose 5-phosphate and 4-phosphohydroxy-L-threonine catalysed by the concerted action of PdxA and PdxJ. However, it has now become clear that the majority of organisms capable of producing this vitamin do so via a different route, involving precursors from glycolysis and the pentose phosphate pathway. This alternative pathway is characterized by the presence of two genes, Pdx1 and Pdx2. Their discovery has sparked renewed interest in vitamin B6, and numerous studies have been conducted over the last few years to characterize the new biosynthesis pathway. Indeed, enormous progress has been made in defining the nature of the enzymes involved in both pathways, and important insights have been provided into their mechanisms of action. In the present review, we summarize the recent advances in our knowledge of the biosynthesis of this versatile molecule and compare the two independent routes to the biosynthesis of vitamin B6. Surprisingly, this comparison reveals that the key biosynthetic enzymes of both pathways are, in fact, very similar both structurally and mechanistically.
1470-8728
1-13
Fitzpatrick, Teresa B
ba3eee8b-d3e5-4a18-9845-64f5e56962f5
Amrhein, Nikolaus
2669a3df-0561-47ae-b5ae-db36911eb618
Kappes, Barbara
10edf779-dc81-4973-878b-d3177273f86a
Macheroux, Peter
e1c49266-c971-42f7-86ae-394bd128d040
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Raschle, Thomas
72f8f1f6-516f-4610-a14b-5b82ea03204f
Fitzpatrick, Teresa B
ba3eee8b-d3e5-4a18-9845-64f5e56962f5
Amrhein, Nikolaus
2669a3df-0561-47ae-b5ae-db36911eb618
Kappes, Barbara
10edf779-dc81-4973-878b-d3177273f86a
Macheroux, Peter
e1c49266-c971-42f7-86ae-394bd128d040
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Raschle, Thomas
72f8f1f6-516f-4610-a14b-5b82ea03204f

Fitzpatrick, Teresa B, Amrhein, Nikolaus, Kappes, Barbara, Macheroux, Peter, Tews, Ivo and Raschle, Thomas (2007) Two independent routes of de novo vitamin B6 biosynthesis: not that different after all. Biochemical Journal, 407 (1), 1-13. (doi:10.1042/BJ20070765). (PMID:17822383)

Record type: Article

Abstract

Vitamin B6 is well known in its biochemically active form as pyridoxal 5'-phosphate, an essential cofactor of numerous metabolic enzymes. The vitamin is also implicated in numerous human body functions ranging from modulation of hormone function to its recent discovery as a potent antioxidant. Its de novo biosynthesis occurs only in bacteria, fungi and plants, making it an essential nutrient in the human diet. Despite its paramount importance, its biosynthesis was predominantly investigated in Escherichia coli, where it is synthesized from the condensation of deoxyxylulose 5-phosphate and 4-phosphohydroxy-L-threonine catalysed by the concerted action of PdxA and PdxJ. However, it has now become clear that the majority of organisms capable of producing this vitamin do so via a different route, involving precursors from glycolysis and the pentose phosphate pathway. This alternative pathway is characterized by the presence of two genes, Pdx1 and Pdx2. Their discovery has sparked renewed interest in vitamin B6, and numerous studies have been conducted over the last few years to characterize the new biosynthesis pathway. Indeed, enormous progress has been made in defining the nature of the enzymes involved in both pathways, and important insights have been provided into their mechanisms of action. In the present review, we summarize the recent advances in our knowledge of the biosynthesis of this versatile molecule and compare the two independent routes to the biosynthesis of vitamin B6. Surprisingly, this comparison reveals that the key biosynthetic enzymes of both pathways are, in fact, very similar both structurally and mechanistically.

Text
BiochemJ_407-1.pdf - Version of Record
Restricted to Repository staff only
Request a copy

More information

Published date: 1 October 2007
Additional Information: Funded by European Commission - FP6: Vitamin biosynthesis as a target for antimalarial therapy (VITBIOMAL) (12158)
Organisations: Centre for Biological Sciences

Identifiers

Local EPrints ID: 200575
URI: http://eprints.soton.ac.uk/id/eprint/200575
ISSN: 1470-8728
PURE UUID: f1d0bf92-8ac3-42b8-a4be-ae9cd8512e44
ORCID for Ivo Tews: ORCID iD orcid.org/0000-0002-4704-1139

Catalogue record

Date deposited: 01 Nov 2011 14:00
Last modified: 17 Dec 2019 01:41

Export record

Altmetrics

Download statistics

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

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×