Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Compound: pyridoxal 5'-phosphate

Abbrev Name: PLP

Synonyms: PLP, pyridoxal phosphate, pyridoxal-5P, pyridoxal 5-phosphate, pyridoxal-P, vitamin B6

Superclasses: a vitamin a vitamin B6

Summary from MetaCyc:
Pyridoxal-5'-phosphate (PLP, vitamin B6) is an essential cofactor in all living systems [John95]. It plays an important role in amino acid and carbohydrate metabolism and has recently been implicated in singlet oxygen resistance [Daub00].

Most bacteria, archaebacteria, fungi, and plants synthesize PLP in a single reaction, as described in pyridoxal 5'-phosphate biosynthesis II. Some anaerobic bacteria use a longer, more complex pathway (see pyridoxal 5'-phosphate biosynthesis I).

Chemical Formula: C8H8NO6P

Molecular Weight: 245.13 Daltons

Monoisotopic Molecular Weight: 247.0245735688 Daltons

SMILES: CC1(N=CC(=C(C=1O)C=O)COP(=O)([O-])[O-])

InChI: InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)/p-2

InChIKey: InChIKey=NGVDGCNFYWLIFO-UHFFFAOYSA-L

Unification Links: CAS:54-47-7 , ChEBI:597326 , ChemSpider:559203 , HMDB:HMDB01491 , IAF1260:33526 , KEGG:C00018 , MetaboLights:MTBLC597326 , PubChem:644168

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -294.53

Reactions known to consume the compound:

Not in pathways:
pyridoxal 5'-phosphate + H2O → pyridoxal + phosphate

Reactions known to produce the compound:

pyridoxal 5'-phosphate biosynthesis I :
pyridoxine 5'-phosphate + oxygen → hydrogen peroxide + pyridoxal 5'-phosphate

pyridoxal 5'-phosphate salvage I :
ATP + pyridoxal → ADP + pyridoxal 5'-phosphate + H+
pyridoxine 5'-phosphate + oxygen → hydrogen peroxide + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + oxygen + H2O → ammonium + hydrogen peroxide + pyridoxal 5'-phosphate

Reactions known to both consume and produce the compound:

Not in pathways:
pyridoxamine 5'-phosphate + a deaminated amino group acceptor ↔ pyridoxal 5'-phosphate + an aminated amino group acceptor
D-alanine + pyridoxal 5'-phosphate ↔ pyruvate + pyridoxamine 5'-phosphate

Enzymes activated by pyridoxal 5'-phosphate, sorted by the type of activation, are:

Activator (Mechanism unknown) of: glucose-1-phosphate adenylyltransferase [Gardiol90, Figueroa11]

Enzymes inhibited by pyridoxal 5'-phosphate, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: pyridoxine 5'-phosphate oxidase [Zhao95a, Comment 1] , L-glutamine:D-fructose-6-phosphate aminotransferase [GolinelliPimpan91, Comment 2] , pyridoxamine 5'-phosphate oxidase [Comment 1]

Inhibitor (Mechanism unknown) of: erythrose 4-phosphate dehydrogenase [Comment 3] , L-glutamine:D-fructose-6-phosphate aminotransferase [GolinelliPimpan91, Comment 4] , 3-phosphoshikimate-1-carboxyvinyltransferase , pyridoxamine-oxaloacetate transaminase [WADA62] , hydroxymethylbilane synthase [Miller89] , pyridoxal kinase [White70, Comment 5]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: L-cysteine desulfurase , cysteine sulfinate desulfinase , dTDP-4-dehydro-6-deoxy-D-glucose transaminase , aminodeoxychorismate lyase , 5,10-methenyltetrahydrofolate hydrolase , 5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase , allothreonine acetaldehyde-lyase (glycine-forming) , valine-pyruvate aminotransferase , tyrosine aminotransferase , tryptophanase , threonine synthase , threonine deaminase , threonine dehydratase , succinylornithine transaminase , N-succinyldiaminopimelate aminotransferase , putrescine aminotransferase , phosphohydroxythreonine aminotransferase , 3-phosphoserine aminotransferase , phenylalanine aminotransferase , ornithine decarboxylase , ornithine decarboxylase , O-succinylhomoserine(thiol)-lyase , maltodextrin phosphorylase , lysine decarboxylase , L-allo-threonine aldolase , leucine aminotransferase , lysine decarboxylase , glutamate-1-semialdehyde aminotransferase , glycogen phosphorylase , glutamate decarboxylase B , glutamate decarboxylase A , glycine decarboxylase , 4-aminobutyrate transaminase , 4-hydroxy-L-threonine aldolase , methionine-oxo-acid transaminase , serine deaminase , phenylalanine transaminase , kynurenine-oxoglutarate transaminase , phenylserine aldolase , threonine aldolase , alanine racemase , 4-aminobutyrate aminotransferase , cystathionine β-lyase , UDP-L-Ara4O C-4" transaminase , 2,3-diaminopropionate ammonia-lyase , selenocysteine synthase , D-serine ammonia-lyase , diamine transaminase , D-cysteine desulfhydrase, PLP-dependent , 7,8-diaminopelargonic acid synthase , cystathionine-β-lyase , valine transaminase , leucine transaminase , isoleucine transaminase , aspartate transaminase , arginine decarboxylase, degradative , arginine decarboxylase, biosynthetic , 2-amino-3-ketobutyrate CoA ligase , cysteine synthase , O-acetylserine sulfhydrylase , acetylornithine transaminase , acetylornithine aminotransferase , 8-amino-7-oxononanoate synthase , tryptophan synthase , tryptophan synthase , lysine 2,3-aminomutase , L-cysteine:[protein cysteine] sulfurtransferase , selenocysteine lyase , cysteine sulfinate desulfinase , diaminopimelate decarboxylase


References

Daub00: Daub ME, Ehrenshaft M (2000). "THE PHOTOACTIVATED CERCOSPORA TOXIN CERCOSPORIN: Contributions to Plant Disease and Fundamental Biology." Annu Rev Phytopathol 38;461-490. PMID: 11701851

Figueroa11: Figueroa CM, Esper MC, Bertolo A, Demonte AM, Aleanzi M, Iglesias AA, Ballicora MA (2011). "Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli." Biochimie 93(10);1816-23. PMID: 21741429

Gardiol90: Gardiol A, Preiss J (1990). "Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzyme." Arch Biochem Biophys 280(1);175-80. PMID: 2162151

GolinelliPimpan91: Golinelli-Pimpaneau B, Badet B (1991). "Possible involvement of Lys603 from Escherichia coli glucosamine-6-phosphate synthase in the binding of its substrate fructose 6-phosphate." Eur J Biochem 1991;201(1);175-82. PMID: 1915361

John95: John RA (1995). "Pyridoxal phosphate-dependent enzymes." Biochim Biophys Acta 1248(2);81-96. PMID: 7748903

Miller89: Miller AD, Packman LC, Hart GJ, Alefounder PR, Abell C, Battersby AR (1989). "Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase)." Biochem J 1989;262(1);119-24. PMID: 2510713

WADA62: WADA H, SNELL EE (1962). "Enzymatic transamination of pyridoxamine. I. With oxaloacetate and alpha-ketoglutarate." J Biol Chem 237;127-32. PMID: 14004226

White70: White RS, Dempsey WB (1970). "Purification and properties of vitamin B6 kinase from Escherichia coli B." Biochemistry 1970;9(21);4057-64. PMID: 4917899

Zhao95: Zhao G, Pease AJ, Bharani N, Winkler ME (1995). "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;177(10);2804-12. PMID: 7751290

Zhao95a: Zhao G, Winkler ME (1995). "Kinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12." J Bacteriol 1995;177(4);883-91. PMID: 7860596


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, biocyc13.