PMID:8595869
| Citation |
Zhao, G and Winkler, ME (1996) 4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12. FEMS Microbiol. Lett. 135:275-80 |
|---|---|
| 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. |
| Links | |
| Keywords |
Acetaldehyde/analogs & derivatives; Acetaldehyde/metabolism; Carbohydrate Dehydrogenases/genetics; Carbohydrate Dehydrogenases/physiology; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Models, Chemical; Organophosphates/metabolism; Phosphotransferases (Alcohol Group Acceptor)/genetics; Phosphotransferases (Alcohol Group Acceptor)/physiology; Pyridoxal Phosphate/analogs & derivatives; Pyridoxal Phosphate/biosynthesis; Pyridoxal Phosphate/metabolism; Threonine/analogs & derivatives; Threonine/metabolism |
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