4.3.3.6: pyridoxal 5'-phosphate synthase (glutamine hydrolysing)
This is an abbreviated version!
For detailed information about pyridoxal 5'-phosphate synthase (glutamine hydrolysing), go to the full flat file.
Word Map on EC 4.3.3.6
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4.3.3.6
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glutaminase
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ammonia
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amidotransferase
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heteromeric
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deoxyxylulose
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vitamer
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pentose
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falciparum
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ribulose
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malaria
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eubacteria
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dodecameric
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imine
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oxyanion
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l-glutamine
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triose
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plasmodial
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hexameric
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drug development
- 4.3.3.6
- glutaminase
- ammonia
-
amidotransferase
-
heteromeric
- deoxyxylulose
-
vitamer
- pentose
- falciparum
- ribulose
- malaria
- eubacteria
-
dodecameric
- imine
-
oxyanion
- l-glutamine
- triose
-
plasmodial
-
hexameric
- drug development
Reaction
Synonyms
Pdx1, PDX2, PdxS, Ph1355, PLP synthase, PLP-synthase complex, PLPS, pyridoxal 5'-phosphate synthase, pyridoxal 5-phosphate synthase, pyridoxal 5-phosphate synthase Snz1, pyridoxal biosynthesis lyase, pyridoxal biosynthesis lyase PdxS, Rv2606c, Snz1
ECTree
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Activating Compound
Activating Compound on EC 4.3.3.6 - pyridoxal 5'-phosphate synthase (glutamine hydrolysing)
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PdxR
PdxR is a direct activator of the pdxST operon, has a regulatory function in de novo synthesis of pyridoxal 5'-phosphate, encoded by gene pdxR, PdxR is a member of the MocR/GabR subfamily with an N-terminal putative DNA-binding domain and a C-terminal aminotransferase-like domain. PdxR is also a negative autoregulator, and its ability to repress is increased by pyridoxal 5'-phosphate. PdxR-like proteins, for which PLP plays just a signalling role, form a separate functional group among the MocR/GabRtype proteins. Mutational analysis of the PdxR binding site, overview
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