Superpathway of pyridoxal 5'-phosphate biosynthesis and salvage (Solanum lycopersicum)

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1-5D-erythrose-4-phosphate 1.2.1.72 erythronate-4-phosphate 2-oxo-3-hydroxy-4-phosphobutanoate 4-(phosphonooxy)-threonine (2S)-2-amino-3-oxo-4-phosphonooxybutanoate1-amino-propan-2-one-3-phosphate D-glyceraldehyde-3-phosphate 6-91-deoxy-D-xylulose 5-phosphate pyridoxine-5'-phosphate pyridoxal 5'-phosphate pyridoxal pyridoxine pyridoxamine pyridoxamine 5'-phosphate 2.6.1.52 1.1.1.262spontaneous2.2.1.7 1.1.1.290 2.6.99.2 2.7.1.- 2.7.1.35 1.4.3.5 1.4.3.5 2.7.1.35


Description

Pyridoxal 5'-phosphate (PLP) is the biochemically active form of pyridoxine 5'-phosphate (PNP)or vitamin B6. PLP is an essential cofactor of numerous metabolic enzymes, predominantly in amino acid metabolism

Comments

 
Synonyms: vitamin B6 biosynthesis and salvage / This superpathway shows the various ways that E. coli can obtain pyridoxal 5'-phosphate, a coenzyme for many enzymes that participate in amino acid and glycogen metabolism.
 
This pathway has been manually created based on Lycocyc content: Lyco: PWY0-845

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Ontology Terms

 

Bibliography

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  2. Gardiol A, Preiss J; ''Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzyme.''; Arch Biochem Biophys, 1990 PubMed Europe PMC Scholia
  3. Daub ME, Ehrenshaft M; ''THE PHOTOACTIVATED CERCOSPORA TOXIN CERCOSPORIN: Contributions to Plant Disease and Fundamental Biology.''; Annu Rev Phytopathol, 2000 PubMed Europe PMC Scholia
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  7. Mizote T, Nakayama H; ''Purification and properties of hydroxymethylpyrimidine kinase from Escherichia coli.''; Biochim Biophys Acta, 1989 PubMed Europe PMC Scholia
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  9. Blumenthal KM, Smith EL; ''Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora. I. Isolation, subunits, amino acid composition, sulfhydryl groups, and identification of a lysine residue reactive with pyridoxal phosphate and N-ethylmaleimide.''; J Biol Chem, 1973 PubMed Europe PMC Scholia
  10. Sivaraman J, Li Y, Banks J, Cane DE, Matte A, Cygler M; ''Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway.''; J Biol Chem, 2003 PubMed Europe PMC Scholia
  11. Yang Y, Zhao G, Winkler ME; ''Identification of the pdxK gene that encodes pyridoxine (vitamin B6) kinase in Escherichia coli K-12.''; FEMS Microbiol Lett, 1996 PubMed Europe PMC Scholia
  12. Furukawa Y, Yamada R, Iwashima A; ''Inactivation of microbial pyridoxal kinase by pyridoxal.''; Acta Vitaminol Enzymol, 1981 PubMed Europe PMC Scholia
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  14. Breton J, Avanzi N, Magagnin S, Covini N, Magistrelli G, Cozzi L, Isacchi A; ''Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase.''; Eur J Biochem, 2000 PubMed Europe PMC Scholia
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  16. Yang Y, Tsui HC, Man TK, Winkler ME; ''Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12.''; J Bacteriol, 1998 PubMed Europe PMC Scholia
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  23. Zhao G, Winkler ME; ''Kinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12.''; J Bacteriol, 1995 PubMed Europe PMC Scholia
  24. Miller AD, Packman LC, Hart GJ, Alefounder PR, Abell C, Battersby AR; ''Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase).''; Biochem J, 1989 PubMed Europe PMC Scholia
  25. Takahashi S, Abbe K, Yamada T; ''Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties.''; J Bacteriol, 1982 PubMed Europe PMC Scholia
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  27. Golinelli-Pimpaneau B, Badet B; ''Possible involvement of Lys603 from Escherichia coli glucosamine-6-phosphate synthase in the binding of its substrate fructose 6-phosphate.''; Eur J Biochem, 1991 PubMed Europe PMC Scholia
  28. van der Meijden P, te Br��mmelstroet BW, Poirot CM, van der Drift C, Vogels GD; ''Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri.''; J Bacteriol, 1984 PubMed Europe PMC Scholia
  29. Yang Y, Zhao G, Man TK, Winkler ME; ''Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12.''; J Bacteriol, 1998 PubMed Europe PMC Scholia
  30. Figueroa CM, Esper MC, Bertolo A, Demonte AM, Aleanzi M, Iglesias AA, Ballicora MA; ''Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli.''; Biochimie, 2011 PubMed Europe PMC Scholia
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  32. Zhao G, Pease AJ, Bharani N, Winkler ME; ''Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis.''; J Bacteriol, 1995 PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
107271view14:36, 17 September 2019MaintBotChEBI identifier normalization
87608view08:54, 25 July 2016MirellaKalafatiOntology Term : 'classic metabolic pathway' added !
73656view17:41, 12 February 2014AndraChanged the layout to reflect the source
73655view16:41, 12 February 2014AndraAdded literature
73653view11:46, 12 February 2014AndraModified description
73652view11:41, 12 February 2014Andra
73648view23:48, 11 February 2014LarsEijssenNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
(2S)-2-amino-3-oxo-4-phosphonooxybutanoateMetabolite441260 (PubChem-compound)
1-amino-propan-2-one-3-phosphate Metabolite1449 (ChEBI)
1-deoxy-D-xylulose 5-phosphate Metabolite16493 (ChEBI)
1.1.1.262GeneProduct1.1.1.262 (Enzyme Nomenclature)
1.1.1.290 GeneProduct1.1.1.290 (Enzyme Nomenclature)
1.2.1.72 GeneProduct1.2.1.72 (Enzyme Nomenclature)
1.4.3.5 GeneProduct1.4.3.5 (Enzyme Nomenclature)
2-oxo-3-hydroxy-4-phosphobutanoate Metabolite27951 (ChEBI)
2.2.1.7 GeneProduct2.2.1.7 (Enzyme Nomenclature)
2.6.1.52 GeneProduct2.6.1.52 (Enzyme Nomenclature)
2.6.99.2 GeneProduct2.6.99.2 (Enzyme Nomenclature)
2.7.1.- GeneProduct2.7.1.- (Enzyme Nomenclature)
2.7.1.35 GeneProduct2.7.1.35 (Enzyme Nomenclature)
4-(phosphonooxy)-threonine Metabolite18336 (ChEBI)
D-erythrose-4-phosphate Metabolite48153 (ChEBI)
D-glyceraldehyde-3-phosphate Metabolite17138 (ChEBI)
erythronate-4-phosphate Metabolite49003 (ChEBI)
pyridoxal Metabolite17310 (ChEBI)
pyridoxal 5'-phosphate Metabolite18405 (ChEBI)
pyridoxamine Metabolite16410 (ChEBI)
pyridoxamine 5'-phosphate Metabolite18335 (ChEBI)
pyridoxine Metabolite16709 (ChEBI)
pyridoxine-5'-phosphate Metabolite28803 (ChEBI)
spontaneousGeneProduct

Annotated Interactions

No annotated interactions
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