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

From WikiPathways

Revision as of 11:41, 12 February 2014 by Andra (Talk | contribs)
Jump to: navigation, search
D-erythrose-4-phosphate Pyridoxal 5'-phosphate (PLP) is the biochemically active formof pyridoxine 5'-phosphate (PNP)or vitamin B6. PLP is an essential cofactor of numerous metabolic enzymes, predominantly in amino acid metabolism1.2.1.72 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 1-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

No description

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

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Tomschy A, Glockshuber R, Jaenicke R; ''Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli. Authenticity and kinetic properties of the recombinant enzyme.''; Eur J Biochem, 1993 PubMed Europe PMC Scholia
  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
  4. Haghighi B, Flynn TG, Levy HR; ''Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Isolation and sequence of a peptide containing an essential lysine.''; Biochemistry, 1982 PubMed Europe PMC Scholia
  5. Jankowski MD, Henry CS, Broadbelt LJ, Hatzimanikatis V; ''Group contribution method for thermodynamic analysis of complex metabolic networks.''; Biophys J, 2008 PubMed Europe PMC Scholia
  6. Herz S, Wungsintaweekul J, Schuhr CA, Hecht S, Luttgen H, Sagner S, Fellermeier M, Eisenreich W, Zenk MH, Bacher A, Rohdich F; ''Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate.''; Proc Natl Acad Sci U S A, 2000 PubMed Europe PMC Scholia
  7. Mizote T, Nakayama H; ''Purification and properties of hydroxymethylpyrimidine kinase from Escherichia coli.''; Biochim Biophys Acta, 1989 PubMed Europe PMC Scholia
  8. John RA; ''Pyridoxal phosphate-dependent enzymes.''; Biochim Biophys Acta, 1995 PubMed Europe PMC Scholia
  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
  13. Yamada RH, Tsuji T, Nose Y; ''Uptake and utilization of vitamin B6 and its phosphate esters by Escherichia coli.''; J Nutr Sci Vitaminol (Tokyo), 1977 PubMed Europe PMC Scholia
  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
  15. Van Heyningen S, Shemin D; ''Inhibition of delta-aminolaevulate dehydratase by pyridoxal derivatives and by cyanide.''; Biochem J, 1971 PubMed Europe PMC Scholia
  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
  17. Braun M, L��nsdorf H, B��ckmann AF; ''12 alpha-hydroxysteroid dehydrogenase from Clostridium group P, strain C 48-50. Production, purification and characterization.''; Eur J Biochem, 1991 PubMed Europe PMC Scholia
  18. Aisaka K, Masuda T, Chikamune T, Kamitori K; ''Purification and characterization of trehalose phosphorylase from Catellatospora ferruginea.''; Biosci Biotechnol Biochem, 1998 PubMed Europe PMC Scholia
  19. Kaminskas E, Kimhi Y, Magasanik B; ''Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway.''; J Biol Chem, 1970 PubMed Europe PMC Scholia
  20. Emes AV, Hassall H; ''The degradation of L-histidine in the rat. The formation of imidazolylpyruvate, imidazolyl-lactate and imidazolylpropionate.''; Biochem J, 1973 PubMed Europe PMC Scholia
  21. Uyeda K, Rabinowitz JC; ''Enzymes of the clostridial purine fermentation. Serine hydroxymethyltransferase.''; Arch Biochem Biophys, 1968 PubMed Europe PMC Scholia
  22. Schryvers A, Lohmeier E, Weiner JH; ''Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli.''; J Biol Chem, 1978 PubMed Europe PMC Scholia
  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
  26. White RS, Dempsey WB; ''Purification and properties of vitamin B6 kinase from Escherichia coli B.''; Biochemistry, 1970 PubMed Europe PMC Scholia
  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
  31. Crow VL, Wittenberger CL; ''Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from Streptococcus mutans.''; J Biol Chem, 1979 PubMed Europe PMC Scholia
  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)
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
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
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP2631"
Personal tools