Organism | UniProt | Comment | Textmining |
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Bacillus subtilis | - |
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Purification (Comment) | Organism |
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Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine | mechanistic studies. Pdx2 has glutaminase activity and channels ammonia to the active site of the PLP synthase subunit, Pdx1, where ribose-5-phosphate, glyceraldehyde-3-phosphate, and ammonia are condensed in a complex series of reactions. Under pre-steady-state conditions, a chromophoric intermediate is observed that accumulates upon addition of only two of the substrates, D-ribose 5-phosphate and glutamine. The intermediate is covalently bound to the protein. The phosphate unit of R5P is eliminated rather than hydrolyzed in route to intermediate formation | Bacillus subtilis | pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate | - |
? | |
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine | the synthase subunit of this enzyme, Pdx1, operates in concert with the glutaminase subunit, Pdx2, to catalyze the complex condensation of ribose 5-phosphate, glutamine and glyceraldehyde 3-phosphate to form pyridoxal 5'-phosphate. Many if not all of the reaction intermediates are covalently bound to the synthase subunit, thus making them difficult to isolate and characterize. By denaturing the enzyme at points along the reaction coordinate, the structures of three covalently bound intermediates are solved. Thes analysis reveals a 1,5 migration of the lysine amine linking the intermediate to the enzyme during the conversion of ribose 5-phosphate to pyridoxal 5'-phosphate | Bacillus subtilis | pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate | - |
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Synonyms | Comment | Organism |
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Pdx1 | pyridoxal 5'-phosphate synthase subunit | Bacillus subtilis |
PDX2 | glutaminase subunit | Bacillus subtilis |