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Identification
YMDB IDYMDB00304
NameL-Phenylalanine
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionPhenylalanine (abbreviated as Phe or F) is an alpha-amino acid. The L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. It is classified as a nonpolar, aromatic amino acid, because of the hydrophobic nature of the benzyl side chain. L-Phenylalanine (LPA) is an electrically neutral amino acid. It is used in the manufacture of food and drink products and sold as a nutritional supplement for its reputed analgesic and antidepressant effects. Biosynthesis of phenylalanine, tyrosine, and tryptophan proceeds via a common pathway to chorismate, at which point the pathway branches. One branch proceeds to phenylalanine and tyrosine, and the other to tryptophan. The phenylalanine and tyrosine branch has one reaction in common, rearrangement of chorismate to prephenate, at which point, the pathway branches again to either phenylalanine or tyrosine. S. cerevisiae, similar to E. coli, synthesizes phenylalanine and tyrosine via the intermediate 4-hydroxyphenylpyruvate and phenylpyruvate, respectively. Aromatic amino acid biosynthesis in S. cerevisiae is controlled by a combination of feedback inhibition, activation of enzyme activity, and regulation of enzyme synthesis. The carbon flow through the pathways is regulated primarily at the initial step and the branching points by the terminal end-products. The initial step of chorismate biosynthesis can be catalyzed by two isoenzymes Aro3p or Aro4p, whereby Aro3p is inhibited by phenylalanine, and Aro4p by tyrosine. The first step in the phenylalanine-tyrosine branch is feedback inhibited by tyrosine and activated by tryptophan. Phenylalanine normally has only three metabolic fates: incorporation into polypeptide chains, production of tyrosine via the tetrahydrobiopterin-requiring phenylalanine hydroxylase and conversion to a fusel alcohol. S. cerevisiae degrade the aromatic amino acids (tryptophan, phenylalanine, and tyrosine) and the branched-chain amino acids (valine, leucine, and iso-leucine) via the Ehrlich pathway. This pathway consists of 3 steps: 1) deamination of the amino acid to the corresponding alpha-keto acid; 2) decarboxylation of the resulting alpha-keto acid to the respective aldehyde; and, 3) reduction of the aldehyde to form the corresponding long chain or complex alcohol, known as a fusel alcohol or fusel oil. Fusel alcohols are important flavor and aroma compounds in yeast-fermented food products and beverages.
Structure
Thumb
Synonyms
  • (-)-beta-Phenylalanine
  • (L)-Phenylalanine
  • (S)-(-)-Phenylalanine
  • (S)-2-amino-3-phenylpropanoate
  • (S)-2-amino-3-phenylpropanoic acid
  • (S)-2-Amino-3-phenylpropionate
  • (S)-2-Amino-3-phenylpropionic acid
  • (S)-alpha-Amino-benzenepropanoate
  • (S)-alpha-Amino-benzenepropanoic acid
  • (S)-alpha-Amino-beta-phenylpropionate
  • (S)-alpha-Amino-beta-phenylpropionic acid
  • (S)-alpha-Aminobenzenepropanoate
  • (S)-alpha-Aminobenzenepropanoic acid
  • (S)-alpha-Aminohydrocinnamate
  • (S)-alpha-Aminohydrocinnamic acid
  • (S)-Phenylalanine
  • 3-Phenyl-L-alanine
  • alpha-Aminohydrocinnamate
  • alpha-Aminohydrocinnamic acid
  • beta-Phenyl-alpha-alanine
  • beta-Phenyl-L-alanine
  • beta-Phenylalanine
  • L-2-Amino-3-phenylpropionate
  • L-2-Amino-3-phenylpropionic acid
  • Phe
  • phenyl-Alanine
  • Phenylalamine
  • Phenylalanine
  • F
  • (S)-a-Amino-b-phenylpropionate
  • (S)-a-Amino-b-phenylpropionic acid
  • (S)-Α-amino-β-phenylpropionate
  • (S)-Α-amino-β-phenylpropionic acid
  • b-Phenyl-L-alanine
  • Β-phenyl-L-alanine
  • L-Isomer phenylalanine
  • Phenylalanine, L isomer
  • Phenylalanine, L-isomer
  • Endorphenyl
CAS number63-91-2
WeightAverage: 165.1891
Monoisotopic: 165.078978601
InChI KeyCOLNVLDHVKWLRT-QMMMGPOBSA-N
InChIInChI=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
IUPAC Name(2S)-2-amino-3-phenylpropanoic acid
Traditional IUPAC NameL-phenylalanine
Chemical FormulaC9H11NO2
SMILES[H]OC(=O)[C@@]([H])(N([H])[H])C([H])([H])C1=C([H])C([H])=C([H])C([H])=C1[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as phenylalanine and derivatives. Phenylalanine and derivatives are compounds containing phenylalanine or a derivative thereof resulting from reaction of phenylalanine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentPhenylalanine and derivatives
Alternative Parents
Substituents
  • Phenylalanine or derivatives
  • 3-phenylpropanoic-acid
  • Alpha-amino acid
  • Amphetamine or derivatives
  • L-alpha-amino acid
  • Aralkylamine
  • Monocyclic benzene moiety
  • Benzenoid
  • Amino acid
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Organic nitrogen compound
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Hydrocarbon derivative
  • Primary aliphatic amine
  • Organic oxide
  • Carbonyl group
  • Organopnictogen compound
  • Organic oxygen compound
  • Amine
  • Aromatic homomonocyclic compound
Molecular FrameworkAromatic homomonocyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point283 °C
Experimental Properties
PropertyValueReference
Water Solubility26.9 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)]PhysProp
LogP-1.38 [AVDEEF,A (1997)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility4.14 g/LALOGPS
logP-1.4ALOGPS
logP-1.2ChemAxon
logS-1.6ALOGPS
pKa (Strongest Acidic)2.47ChemAxon
pKa (Strongest Basic)9.45ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area63.32 ŲChemAxon
Rotatable Bond Count3ChemAxon
Refractivity45.12 m³·mol⁻¹ChemAxon
Polarizability17.03 ųChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic Properties
Flavour/OdourSource
BitterFDB013245
OdorlessFDB013245
SMPDB Pathways
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
Phenylalanine metabolismPW002437 ThumbThumb?image type=greyscaleThumb?image type=simple
Tryptophan metabolismPW002442 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Phenylalanine metabolismec00360 Map00360
Phenylalanine, tyrosine and tryptophan biosynthesisec00400 Map00400
Tryptophan metabolismec00380 Map00380
SMPDB Reactions
4-Methylthio-2-oxobutanoate + L-PhenylalanineL-Methionine + 2-Ketobutyric acid
keto-phenylpyruvic acid + L-AlaninePyruvic acid + L-Phenylalanine
L-Tryptophan + keto-phenylpyruvic acid3-(indol-3-yl)pyruvate + L-Phenylalanine
keto-phenylpyruvic acid + L-Glutamic acidL-Phenylalanine + Oxoglutaric acid
KEGG Reactions
Oxoglutaric acid + L-PhenylalanineL-Glutamic acid + keto-phenylpyruvic acid
tRNA(Phe) + Adenosine triphosphate + L-PhenylalanineAdenosine monophosphate + Pyrophosphate + Phe-tRNA(Phe)
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
1428 ± 29 µM YPD mediaaerobicBaker's yeastPMID: 7654310
1180 ± 23 µM YPG mediaaerobicBaker's yeastPMID: 7654310
311 ± 6 µM SD mediaaerobicBaker's yeastPMID: 7654310
186 ± 4 µM SG mediaaerobicBaker's yeastPMID: 7654310
683 ± 14 µM M (molasses)aerobicBaker's yeastPMID: 7654310
2794 ± 56 µM MA (molasses)aerobicBaker's yeastPMID: 7654310
993 ± 20 µM MB (molasses)aerobicBaker's yeastPMID: 7654310
3042 ± 61 µM MAB (molasses)aerobicBaker's yeastPMID: 7654310
1415 ± 71 µM YEB media with 0.5 mM glucoseaerobicBaker's yeastExperimentally Determined
Not Available
540 ± 64 µM Synthetic medium with 20 g/L glucoseaerobicBaker's yeastPMID: 12584756
Conversion Details Here
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • Martinez-Force, E., Benitez, T. (1995). "Effects of varying media, temperature, and growth rates on the intracellular concentrations of yeast amino acids." Biotechnol Prog 11:386-392.7654310
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Vuralhan, Z., Morais, M. A., Tai, S. L., Piper, M. D., Pronk, J. T. (2003). "Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Appl Environ Microbiol 69:4534-4541.12902239
  • Vaseghi, S., Baumeister, A., Rizzi, M., Reuss, M. (1999). "In vivo dynamics of the pentose phosphate pathway in Saccharomyces cerevisiae." Metab Eng 1:128-140.10935926
  • Hans, M. A., Heinzle, E., Wittmann, C. (2003). "Free intracellular amino acid pools during autonomous oscillations in Saccharomyces cerevisiae." Biotechnol Bioeng 82:143-151.12584756
  • Nookaew, I., Jewett, M. C., Meechai, A., Thammarongtham, C., Laoteng, K., Cheevadhanarak, S., Nielsen, J., Bhumiratana, S. (2008). "The genome-scale metabolic model iIN800 of Saccharomyces cerevisiae and its validation: a scaffold to query lipid metabolism." BMC Syst Biol 2:71.18687109
  • Iraqui, I., Vissers, S., Cartiaux, M., Urrestarazu, A. (1998). "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily." Mol Gen Genet 257:238-248.9491083
  • Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). "Growth control of the eukaryote cell: a systems biology study in yeast." J Biol 6:4.17439666
Synthesis Reference:Zhou, Hua; Zhong, Yao; Sun, Guanghai; Wei, Ping. Preparation of L-phenylalanine by an aqueous two-phase system. Huaxue Fanying Gongcheng Yu Gongyi (2006), 22(2), 146-150.
External Links:
ResourceLink
CHEBI ID17295
HMDB IDHMDB00159
Pubchem Compound ID6140
Kegg IDC00079
ChemSpider ID5910
FOODB IDFDB013245
WikipediaPhenylalanine
BioCyc IDPHE

Enzymes

General function:
Involved in nucleotide binding
Specific function:
Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins
Gene Name:
MSF1
Uniprot ID:
P08425
Molecular weight:
54828.39844
Reactions
ATP + L-phenylalanine + tRNA(Phe) → AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
General function:
Involved in RNA binding
Specific function:
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Gene Name:
FRS1
Uniprot ID:
P15624
Molecular weight:
67364.29688
Reactions
ATP + L-phenylalanine + tRNA(Phe) → AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
General function:
Involved in nucleotide binding
Specific function:
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Gene Name:
FRS2
Uniprot ID:
P15625
Molecular weight:
57511.0
Reactions
ATP + L-phenylalanine + tRNA(Phe) → AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Has aromatic amino acid transaminase activity and kynurenine aminotransferase activity
Gene Name:
ARO9
Uniprot ID:
P38840
Molecular weight:
58527.0
Reactions
An aromatic amino acid + 2-oxoglutarate → an aromatic oxo acid + L-glutamate.
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Has aromatic amino acid transaminase activity. Also active with methionine, alpha-aminoadipate and leucine when phenylpyruvate is the amino acceptor
Gene Name:
ARO8
Uniprot ID:
P53090
Molecular weight:
56177.30078
Reactions
An aromatic amino acid + 2-oxoglutarate → an aromatic oxo acid + L-glutamate.
L-2-aminoadipate + 2-oxoglutarate → 2-oxoadipate + L-glutamate

Transporters

General function:
Involved in transport
Specific function:
Permease for various amino acids as well as for GABA. Can also transport L-cysteine and beta-alanine
Gene Name:
GAP1
Uniprot ID:
P19145
Molecular weight:
65654.89844
General function:
Involved in transport
Specific function:
Required for high-affinity tryptophan transport. Also transports cysteine, phenyalanine and tyrosine
Gene Name:
TAT2
Uniprot ID:
P38967
Molecular weight:
65403.80078
General function:
Involved in transport
Specific function:
Permease for leucine, valine and isoleucine. Also transports cysteine, methionine, phenyalanine, tyrosine and tryptophan
Gene Name:
BAP2
Uniprot ID:
P38084
Molecular weight:
67669.60156
General function:
Involved in transport
Specific function:
Involved in transport of isoleucine, leucine, valine, cysteine, methionine, phenylalanine, tyrosine and tryptophan
Gene Name:
BAP3
Uniprot ID:
P41815
Molecular weight:
67364.39844
General function:
Involved in transport
Specific function:
Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source
Gene Name:
AGP1
Uniprot ID:
P25376
Molecular weight:
69670.70313