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 vitamina 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

pyridoxal 5'-phosphate compound structure

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


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 donor ↔ pyridoxal 5'-phosphate + an aminated amino group donor
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: alanine racemase, N-succinyldiaminopimelate aminotransferase, N-acetylornithine aminotransferase, 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, N-acetylornithine aminotransferase, N-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

This compound has been characterized as an alternative substrate of the following enzymes: phosphoglycolate phosphatase, alkaline phosphatase


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

Sivaraman03: Sivaraman J, Li Y, Banks J, Cane DE, Matte A, Cygler M (2003). "Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway." J Biol Chem 278(44);43682-90. PMID: 12896974

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

Yang98: Yang Y, Zhao G, Man TK, Winkler ME (1998). "Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12." J Bacteriol 1998;180(16);4294-9. PMID: 9696782

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

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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