PMID: 8595869Jan 15, 1996Paper

4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12

FEMS Microbiology Letters
G Zhao, M E Winkler

Abstract

We show that thrB-encoded homoserine kinase is required for growth of Escherichia coli K-12 pdxB mutants on minimal glucose medium supplemented with 4-hydroxy-L-threonine (synonym, 3-hydroxyhomoserine) or D-glycolaldehyde. This result is consistent with a model in which 4-phospho-hydroxy-L-threonine (synonym, 3-hydroxyhomoserine phosphate), rather than 4-hydroxy-L-threonine, is an obligatory intermediate in pyridoxal 5'-phosphate biosynthesis. Ring closure using 4-phospho-hydroxy-L-threonine as a substrate would lead to formation of pyridoxine 5'-phosphate, and not pyridoxine, as the first B6-vitamer synthesized de novo. These considerations suggest that E. coli pyridoxal/pyridoxamine/pyridoxine kinase is not required for the main de novo pathway of pyridoxal 5'-phosphate biosynthesis, and instead plays a role only in the B6-vitamer salvage pathway.

References

Mar 1, 1976·European Journal of Biochemistry·B BurrG N Cohen
Apr 25, 1989·Biochimica Et Biophysica Acta·T Mizote, H Nakayama
Jun 1, 1989·Journal of Bacteriology·S LittleM K Robinson
Oct 13, 1970·Biochemistry·R S White, W B Dempsey

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Citations

Aug 4, 1999·Proceedings of the National Academy of Sciences of the United States of America·M EhrenshaftM E Daub
Feb 15, 2002·Journal of Bacteriology·Andrew J PeaseMalcolm E Winkler
Jun 14, 2016·ACS Chemical Biology·Jennifer J ThiavilleValérie de Crécy-Lagard
Dec 2, 2010·Molecular Systems Biology·Juhan KimShelley D Copley
Sep 8, 2007·The Biochemical Journal·Teresa B FitzpatrickThomas Raschle

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