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Escherichia coli K-12 substr. MG1655 Compound: L-phenylalanine

Abbrev Name: phe

Synonyms: 2S-α-phenylalanine, F, endophenyl, phenylalanine, phe, L-phe

Superclasses: an acidall carboxy acidsa carboxylatean amino acida non-polar amino acid
an acidall carboxy acidsa carboxylatean amino acidan alpha amino acida standard alpha amino acid
an acidall carboxy acidsa carboxylatean amino acidan aromatic amino acidan aromatic L-amino acid
an acidall carboxy acidsa carboxylatean amino acidan L-amino acidan aromatic L-amino acid
an acidall carboxy acidsa carboxylatean amino acidan L-amino acid
an amino acid or its derivativean amino acida non-polar amino acid
an amino acid or its derivativean amino acidan alpha amino acida standard alpha amino acid
an amino acid or its derivativean amino acidan aromatic amino acidan aromatic L-amino acid
an amino acid or its derivativean amino acidan L-amino acidan aromatic L-amino acid
an amino acid or its derivativean amino acidan L-amino acid


Component of: TyrR-Phenylalanine DNA-binding transcriptional repressor

Chemical Formula: C9H11NO2

Molecular Weight: 165.19 Daltons

Monoisotopic Molecular Weight: 166.0868036346 Daltons

L-phenylalanine compound structure

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

InChI: InChI=1S/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1

InChIKey: InChIKey=COLNVLDHVKWLRT-QMMMGPOBSA-N

Unification Links: CAS:63-91-2, ChEBI:58095, HMDB:HMDB00159, IAF1260:33775, KEGG:C00079, MetaboLights:MTBLC58095, PubChem:6925665

Standard Gibbs Free Energy of Formation (ΔfG in kcal/mol): -49.5

Reactions known to consume the compound:

tRNA charging :
a tRNAphe + L-phenylalanine + ATP + H+ → an L-phenylalanyl-[tRNAphe] + AMP + diphosphate

Reactions known to produce the compound:

Not in pathways:
a peptide with an N-terminal X-L-proline + H2O → a standard α amino acid + a peptide with an N-terminal L-proline + H+
a peptide + H2O → a standard α amino acid + a peptide
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a standard α amino acid + a peptide
β-aspartyl dipeptide + H2O → L-aspartate + a standard α amino acid
a dipetide with an N-terminal L-aspartate + H2O → L-aspartate + a standard α amino acid
a tripeptide + H2O → a dipeptide + a standard α amino acid
a dipeptide with proline at the C-terminal + H2O → L-proline + a standard α amino acid
a dipeptide + H2O → 2 a standard α amino acid

Not in pathways:
a polypeptide + H2O → a polypeptide + an L-amino acid

Not in pathways:
a carboxylic ester + H2O → an alcohol + a carboxylate + H+
an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+
an acyl phosphate + H2O → a carboxylate + phosphate + H+
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+
a 1-acyl 2-lyso-phosphatidylcholine + H2O → a carboxylate + sn-glycero-3-phosphocholine + H+

Reactions known to both consume and produce the compound:

L-phenylalanine biosynthesis I :
2-oxo-3-phenylpropanoate + L-glutamate ↔ L-phenylalanine + 2-oxoglutarate

Not in pathways:
an aromatic amino acid + 2-oxoglutarate ↔ an aromatic oxo-acid + L-glutamate

In Reactions of unknown directionality:

Not in pathways:
TyrR + L-phenylalanine = TyrR-phe

Not in pathways:
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + a standard α amino acid

Not in pathways:
a 5-L-glutamyl-[peptide][periplasm] + an amino acid[periplasm] = a 5-L-glutamyl-amino acid[periplasm] + a peptide[periplasm]

Not in pathways:
a 2-acyl 1-lyso-phosphatidylcholine + H2O = a carboxylate + sn-glycero-3-phosphocholine + H+
an aldehyde[periplasm] + FAD[periplasm] + H2O[periplasm] = a carboxylate[periplasm] + FADH2[periplasm]

In Transport reactions:
L-phenylalanine[periplasm] + H+[periplasm]L-phenylalanine[cytosol] + H+[cytosol],
an aromatic amino acid[cytosol]an aromatic amino acid[periplasm],
an amino acid[periplasm]an amino acid[extracellular space]

Enzymes inhibited by L-phenylalanine, sorted by the type of inhibition, are:

Inhibitor (Allosteric) of: prephenate dehydratase [Baldwin81a, Dopheide72], chorismate mutase [Baldwin81a, Dopheide72] Inhibitor (Mechanism unknown) of: 2-dehydro-3-deoxyphosphoheptonate aldolase [McCandliss78]

This compound has been characterized as an alternative substrate of the following enzymes: methionine-oxo-acid transaminase

In Growth Media: Neidhardt EZ rich defined medium, PMA nitrogen source test + phe, PMA carbon source test + phe

Transcription Units regulated by related protein TyrR-Phenylalanine DNA-binding transcriptional repressor (2 total):

Transcription-unit diagram

Transcription-unit diagram


References

Baldwin81a: Baldwin GS, Davidson BE (1981). "A kinetic and structural comparison of chorismate mutase/prephenate dehydratase from mutant strains of Escherichia coli K 12 defective in the PheA gene." Arch Biochem Biophys 1981;211(1);66-75. PMID: 7030214

Dopheide72: Dopheide TA, Crewther P, Davidson BE (1972). "Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties." J Biol Chem 247(14);4447-52. PMID: 4261395

McCandliss78: McCandliss RJ, Poling MD, Herrmann KM (1978). "3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli." J Biol Chem 1978;253(12);4259-65. PMID: 26682


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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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