Phenylalanine (symbol Phe or F) is an essential α-amino acid with the formula C9H11NO2. It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine. This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain. The L-isomer is used to biochemically form proteins coded for by DNA. Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the biological pigment melanin. It is encoded by the messenger RNA codons UUU and UUC.
Phenylalanine is found naturally in the milk of mammals. It is used in the manufacture of food and drink products and sold as a nutritional supplement as it is a direct precursor to the neuromodulator phenethylamine. As an essential amino acid, phenylalanine is not synthesized de novo in humans and other animals, who must ingest phenylalanine or phenylalanine-containing proteins.
The one-letter symbol F was assigned to phenylalanine for its phonetic similarity. |
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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 |
COLNVLDHVKWLRT-QMMMGPOBSA-N |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Chlamydomonas reinhardtii
(NCBI:txid3055)
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See:
PubMed
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Saccharomyces cerevisiae
(NCBI:txid4932)
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See:
PubMed
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Saccharomyces cerevisiae
(NCBI:txid4932)
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Source: yeast.sf.net
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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Homo sapiens
(NCBI:txid9606)
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Found in
blood serum
(BTO:0000133).
See:
MetaboLights Study
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Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
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plant metabolite
Any eukaryotic metabolite produced during a metabolic reaction in plants, the kingdom that include flowering plants, conifers and other gymnosperms.
Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
algal metabolite
Any eukaryotic metabolite produced during a metabolic reaction in algae including unicellular organisms like chlorella and diatoms to multicellular organisms like giant kelps and brown algae.
human xenobiotic metabolite
Any human metabolite produced by metabolism of a xenobiotic compound in humans.
EC 3.1.3.1 (alkaline phosphatase) inhibitor
An EC 3.1.3.* (phosphoric monoester hydrolase) inhibitor that interferes with the action of alkaline phosphatase (EC 3.1.3.1).
Saccharomyces cerevisiae metabolite
Any fungal metabolite produced during a metabolic reaction in Baker's yeast (Saccharomyces cerevisiae ).
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
micronutrient
Any nutrient required in small quantities by organisms throughout their life in order to orchestrate a range of physiological functions.
Daphnia magna metabolite
A Daphnia metabolite produced by the species Daphnia magna.
(via phenylalanine )
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nutraceutical
A product in capsule, tablet or liquid form that provide essential nutrients, such as a vitamin, an essential mineral, a protein, an herb, or similar nutritional substance.
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View more via ChEBI Ontology
(2S)-2-amino-3-phenylpropanoic acid
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L-phenylalanine
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(S)-2-Amino-3-phenylpropionic acid
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HMDB
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(S)-alpha-Amino-beta-phenylpropionic acid
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KEGG COMPOUND
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3-phenyl-L-alanine
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NIST Chemistry WebBook
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β-phenyl-L-alanine
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NIST Chemistry WebBook
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F
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ChEBI
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L-Phenylalanine
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KEGG COMPOUND
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Phe
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ChEBI
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PHENYLALANINE
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PDBeChem
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2144
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DrugCentral
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C00001386
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KNApSAcK
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C00079
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KEGG COMPOUND
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D00021
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KEGG DRUG
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DB00120
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DrugBank
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ECMDB00159
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ECMDB
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HMDB0000159
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HMDB
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PHE
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PDBeChem
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PHE
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MetaCyc
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Phenylalanine
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Wikipedia
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YMDB00304
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YMDB
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View more database links |
1910408
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Reaxys Registry Number
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Reaxys
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50837
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Gmelin Registry Number
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Gmelin
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63-91-2
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CAS Registry Number
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KEGG COMPOUND
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63-91-2
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CAS Registry Number
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ChemIDplus
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63-91-2
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CAS Registry Number
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NIST Chemistry WebBook
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Romagnoli G, Knijnenburg TA, Liti G, Louis EJ, Pronk JT, Daran JM (2015) Deletion of the Saccharomyces cerevisiae ARO8 gene, encoding an aromatic amino acid transaminase, enhances phenylethanol production from glucose. Yeast (Chichester, England) 32, 29-45 [PubMed:24733517] [show Abstract] Phenylethanol has a characteristic rose-like aroma that makes it a popular ingredient in foods, beverages and cosmetics. Microbial production of phenylethanol currently relies on whole-cell bioconversion of phenylalanine with yeasts that harbour an Ehrlich pathway for phenylalanine catabolism. Complete biosynthesis of phenylethanol from a cheap carbon source, such as glucose, provides an economically attractive alternative for phenylalanine bioconversion. In this study, synthetic genetic array (SGA) screening was applied to identify genes involved in regulation of phenylethanol synthesis in Saccharomyces cerevisiae. The screen focused on transcriptional regulation of ARO10, which encodes the major decarboxylase involved in conversion of phenylpyruvate to phenylethanol. A deletion in ARO8, which encodes an aromatic amino acid transaminase, was found to underlie the transcriptional upregulation of ARO10 during growth, with ammonium sulphate as the sole nitrogen source. Physiological characterization revealed that the aro8Δ mutation led to substantial changes in the absolute and relative intracellular concentrations of amino acids. Moreover, deletion of ARO8 led to de novo production of phenylethanol during growth on a glucose synthetic medium with ammonium as the sole nitrogen source. The aro8Δ mutation also stimulated phenylethanol production when combined with other, previously documented, mutations that deregulate aromatic amino acid biosynthesis in S. cerevisiae. The resulting engineered S. cerevisiae strain produced >3 mm phenylethanol from glucose during growth on a simple synthetic medium. The strong impact of a transaminase deletion on intracellular amino acid concentrations opens new possibilities for yeast-based production of amino acid-derived products. | Kim B, Cho BR, Hahn JS (2014) Metabolic engineering of Saccharomyces cerevisiae for the production of 2-phenylethanol via Ehrlich pathway. Biotechnology and bioengineering 111, 115-124 [PubMed:23836015] [show Abstract] 2-Phenylethanol (2-PE), a fragrance compound with a rose-like odor, is widely used in perfumery and cosmetics. Here, we report the first metabolic engineering approach for 2-PE production in Saccharomyces cerevisiae. 2-PE can be produced from the catabolism of L-phenylalanine via Ehrlich pathway, consisting of transamination to phenylpyruvate by Aro9, decarboxylation to phenylacetaldehyde by Aro10, and reduction to 2-PE by alcohol dehydrogenases. We demonstrated that Ald3 is mainly responsible for phenylacetaldehyde oxidation, competing with 2-PE production. ALD3 deletion strain overexpressing ARO9 and ARO10 both by episomal overexpression and by induction of the endogenous genes through overexpression of Aro80 transcription factor, produced 4.8 g/L 2-PE in a medium containing 10 g/L L-phenylalanine as a sole nitrogen source. Considering the cytotoxicity of 2-PE, this production titer is almost the upper limit that can be reached in batch cultures, suggesting the great potential of this yeast strain for 2-PE production. 2-PE production was further increased by applying two-phase fermentation method with polypropylene glycol 1200 as an extractant, reaching 6.1 g/L 2-PE in organic phase with the molar yield of 82.5%, which is about ninefold increase compared with wild type. | Ding R, Liu L, Chen X, Cui Z, Zhang A, Ren D, Zhang L (2014) Introduction of two mutations into AroG increases phenylalanine production in Escherichia coli. Biotechnology letters 36, 2103-2108 [PubMed:24966042] [show Abstract] L-Phenylalanine is an important amino acid commercially, and therefore optimization of its manufacture is of interest. We constructed a range of mutant alleles of AroG, the enzyme involved in the first step of phenylalanine biosynthesis. Three single-site mutant alleles were constructed (aroG8, aroG15, and aroG29), which were then combined to generate three double-site aroG (fbr) mutant alleles (aroG8/15, aroG8/29, and aroG15/29). Enzymatic activity, feedback inhibition, and fermentation were analyzed in all of the mutants. All double-site mutants, except AroG15/29, showed higher enzymatic activity and greater resistance to feedback inhibition than their respective single-site mutants. The E. coli strain carrying the aroG8/15 allele produced a phenylalanine titer of 26.78 g/l, a 116 % improvement over the control phenylalanine overproducing strain (12.41 g/l). Our findings provide an effective method for modifying phenylalanine biosynthetic genes, which may be applied to optimize the commercial manufacture of phenylalanine. | Singh V, Rai RK, Arora A, Sinha N, Thakur AK (2014) Therapeutic implication of L-phenylalanine aggregation mechanism and its modulation by D-phenylalanine in phenylketonuria. Scientific reports 4, 3875 [PubMed:24464217] [show Abstract] Self-assembly of phenylalanine is linked to amyloid formation toxicity in phenylketonuria disease. We are demonstrating that L-phenylalanine self-assembles to amyloid fibrils at varying experimental conditions and transforms to a gel state at saturated concentration. Biophysical methods including nuclear magnetic resonance, resistance by alpha-phenylglycine to fibril formation and preference of protected phenylalanine to self-assemble show that this behaviour of L-phenylalanine is governed mainly by hydrophobic interactions. Interestingly, D-phenylalanine arrests the fibre formation by L-phenylalanine and gives rise to flakes. These flakes do not propagate further and prevent fibre formation by L-phenylalanine. This suggests the use of D-phenylalanine as modulator of L-phenylalanine amyloid formation and may qualify as a therapeutic molecule in phenylketonuria. | Mallakpour S, Barati A (2012) Preparation and characterization of novel optically active poly(vinyl alcohol-co-vinyl ester) in nonaqueous medium using L-phenylalanine as a chiral material. Amino acids 42, 1287-1295 [PubMed:21203787] [show Abstract] In this investigation, poly(vinyl alcohol) was chemically modified by the introduction of different amounts of N-phthaloyl-L-phenylalanine. The modification was carried out by the reaction of PVA hydroxyl groups with (2S)-3-phenyl-2-phthalimidylpropanoyl chloride using N,N-dimethyl acetamide/lithium chloride as a reaction media. The novel copolymers obtained were characterized by spectroscopic techniques, elemental analysis, X-ray diffraction and thermal methods. Optical rotation and viscosities were also measured. The degree of esterification was determined by (1)H-NMR. The influence of reagent molar ratio on the degree of modification was also evaluated. The vinyl(3-phenyl-2-phthalimidopropanoate) content in the copolymer was attained up to 52%. Thermal stability of the copolymers was checked by thermogravimetric analysis and differential thermogravimetric analysis. All copolymers displayed improved thermal stability compared to the parent polymer. | Herrera MC, Daddaoua A, Fernández-Escamilla A, Ramos JL (2012) Involvement of the global Crp regulator in cyclic AMP-dependent utilization of aromatic amino acids by Pseudomonas putida. Journal of bacteriology 194, 406-412 [PubMed:22081386] [show Abstract] The phhAB operon encodes a phenylalanine hydroxylase involved in the conversion of L-phenylalanine into L-tyrosine in Pseudomonas putida. The phhAB promoter is transcribed by RNA polymerase sigma-70 and is unusual in that the specific regulator PhhR acts as an enhancer protein that binds to two distant upstream sites (-75 to -92 and -132 to -149). There is an integration host factor (IHF) binding site that overlaps the proximal PhhR box, and, consequently, IHF acts as an inhibitor of transcription. Use of L-phenylalanine is compromised in a crp-deficient background due to reduced expression from the phhAB promoter. Electrophoretic mobility shift assays and DNase I footprinting assays reveal that Crp binds at a site centered at -109 only in the presence of cyclic AMP (cAMP). We show, using circular permutation analysis, that the simultaneous binding of Crp/cAMP and PhhR bends DNA to bring positive regulators and RNA polymerase into close proximity. This nucleoprotein complex promotes transcription from phhA only in response to L-phenylalanine. | Purushotham U, Vijay D, Narahari Sastry G (2012) A computational investigation and the conformational analysis of dimers, anions, cations, and zwitterions of L-phenylalanine. Journal of computational chemistry 33, 44-59 [PubMed:21956539] [show Abstract] The structure and stability of various conformations of L-phenylalanine (PheN) and its zwitterions (PheZ), along with their ionized counterparts, cation (PheC) and anion (PheA), generated by adding and removing a proton respectively, have been investigated using first principle calculations in vacuum and in solution. This is followed by an extensive study on various possible dimer (PheD) conformations, which are noncovalently bound units without a peptide bond. This study results in 52, 31, 12, 9, and 11 minimum energy structures on the potential energy surfaces of PheD, PheN, PheC, PheA, and PheZ, respectively. Several important nonbonded interactions such as hydrogen bonds, NH-π, CH-π, OH-π, and π-π interactions, which impart stability to the monomeric and dimeric units, have been analyzed. The capability and strength of the nonbonded interactions drastically changing the conformational orientations of monomeric units has been illustrated. | Dong F, Yang Z, Baldermann S, Kajitani Y, Ota S, Kasuga H, Imazeki Y, Ohnishi T, Watanabe N (2012) Characterization of L-phenylalanine metabolism to acetophenone and 1-phenylethanol in the flowers of Camellia sinensis using stable isotope labeling. Journal of plant physiology 169, 217-225 [PubMed:22209218] [show Abstract] Acetophenone (AP) and 1-phenylethanol (1PE) are the two major endogenous volatile compounds in flowers of Camellia sinensis var. Yabukita. Until now no information has been available on the biosynthesis of AP and 1PE in plants. Here we propose that AP and 1PE are derived from L-phenylalanine (L-Phe), based on feeding experiments using stable isotope-labeled precursors L-[(2)H(8)]Phe and L-[(13)C(9)]Phe. The subacid conditions in the flowers result in more hydrogenation than dehydrogenation in the transformation between AP and 1PE. Due to the action of some enzyme(s) responsible for the formation of (R)-1PE from AP in the flowers, (R)-1PE is the dominant endogenous steroisomer of 1PE. The modification of 1PE into nonvolatile glycosidic forms is one of the reasons for why only a little 1PE is released from the flowers. The levels of AP, 1PE, and glycosides of 1PE increase during floral development, whereas the level of L-Phe decreases. These metabolites occur mostly in the anthers. | Prasuna ML, Mujahid M, Sasikala Ch, Ramana ChV (2012) L-Phenylalanine catabolism and L-phenyllactic acid production by a phototrophic bacterium, Rubrivivax benzoatilyticus JA2. Microbiological research 167, 526-531 [PubMed:22494897] [show Abstract] A phototrophic bacterium (Rubrivivax benzoatilyticus JA2) grows at the expense of L-phenylalanine as sole source of nitrogen but not as carbon source. Near stoichiometric yields of L-phenylpyruvic acid (0.4 mM) and L-phenyllactate (0.4 mM) were observed from L-phenylalanine (0.9 mM consumed). Aminotransfarase and dehydrogenase activities involved in the formation of L-phenylpyruvic acid and L-phenyllactate were demonstrated unequivocally in Rubrivivax benzoatilyticus JA2. Growth conditions and carbon sources had an influence on L-phenyllactate production. The process yielded a maximum of 0.92 mM L-phenyllactate from L-phenylalanine (1 mM) when fructose served as carbon source for R. benzoatilyticus JA2. | King MD, Blanton TN, Korter TM (2012) Revealing the true crystal structure of L-phenylalanine using solid-state density functional theory. Physical chemistry chemical physics : PCCP 14, 1113-1116 [PubMed:22143120] [show Abstract] Solid-state density functional theory can be used for crystal structure determination from powder X-ray diffraction data of molecular crystals that are too large and complex for conventional refinement methods. | Qiu H, Xi Y, Lu F, Fan L, Luo C (2012) Determination of L-phenylalanine on-line based on molecularly imprinted polymeric microspheres and flow injection chemiluminescence. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy 86, 456-460 [PubMed:22112574] [show Abstract] A novel molecular imprinting-chemiluminescence (MIP-CL) sensor for the determination of L-phenylalanine (Phe) using molecularly imprinted polymer (MIP) as recognition element is reported. The Phe-MIP was synthesized using acrylamide (AM) as functional monomer and ethylene glycol dimethacrylate (EGDMA) as cross-linker, 2,2-azobisisobutyronitrile (AIBN) as initiator and the polymers' properties were characterized. Then the synthesized MIP was employed as recognition element by packing into flow cell to establish a novel flow injection CL sensor. The CL intensity responded linearly to the concentration of Phe in the range 1.3 × 10(-6) to 5.44 × 10(-4) mol/L with a detection limit of 6.23 × 10(-7) mol/L (3σ), which is lower than that of conventional methods. The sensor is reusable and has a great improvement in sensitivity and selectivity for CL analysis. As a result, the new MIP-CL sensor had been successfully applied to the determination of Phe in samples. | Doroshenko V, Airich L, Vitushkina M, Kolokolova A, Livshits V, Mashko S (2007) YddG from Escherichia coli promotes export of aromatic amino acids. FEMS microbiology letters 275, 312-318 [PubMed:17784858] [show Abstract] The inner membrane protein YddG of Escherichia coli is a homologue of the known amino acid exporters RhtA and YdeD. It was found that the yddG gene overexpression conferred resistance upon E. coli cells to the inhibiting concentrations of l-phenylalanine and aromatic amino acid analogues, dl-p-fluorophenylalanine, dl-o-fluorophenylalanine and dl-5-fluorotryptophan. In addition, yddG overexpression enhanced the production of l-phenylalanine, l-tyrosine or l-tryptophan by the respective E. coli-producing strains. On the other hand, the inactivation of yddG decreased the aromatic amino acid accumulation by these strains. The cells of the E. colil-phenylalanine-producing strain containing overexpressed yddG accumulated less l-phenylalanine inside and exported the amino acid at a higher rate than the cells of the isogenic strain containing wild-type yddG. Taken together, these results indicate that YddG functions as an aromatic amino acid exporter. | Smagghe BJ, Kundu S, Hoy JA, Halder P, Weiland TR, Savage A, Venugopal A, Goodman M, Premer S, Hargrove MS (2006) Role of phenylalanine B10 in plant nonsymbiotic hemoglobins. Biochemistry 45, 9735-9745 [PubMed:16893175] [show Abstract] All plants contain an unusual class of hemoglobins that display bis-histidyl coordination yet are able to bind exogenous ligands such as oxygen. Structurally homologous hexacoordinate hemoglobins (hxHbs) are also found in animals (neuroglobin and cytoglobin) and some cyanobacteria, where they are thought to play a role in free radical scavenging or ligand sensing. The plant hxHbs can be distinguished from the others because they are only weakly hexcacoordinate in the ferrous state, yet no structural mechanism for regulating hexacoordination has been articulated to account for this behavior. Plant hxHbs contain a conserved Phe at position B10 (Phe(B10)), which is near the reversibly coordinated distal His(E7). We have investigated the effects of Phe(B10) mutation on kinetic and equilibrium constants for hexacoordination and exogenous ligand binding in the ferrous and ferric oxidation states. Kinetic and equilibrium constants for hexacoordination and ligand binding along with CO-FTIR spectroscopy, midpoint reduction potentials, and the crystal structures of two key mutant proteins (F40W and F40L) reveal that Phe(B10) is an important regulatory element in hexacoordination. We show that Phe at this position is the only amino acid that facilitates stable oxygen binding to the ferrous Hb and the only one that promotes ligand binding in the ferric oxidation states. This work presents a structural mechanism for regulating reversible intramolecular coordination in plant hxHbs. | FISHMAN WH, GREEN S, INGLIS NI (1963) L-phenylalanine: an organ specific, stereospecific inhibitor of human intestinal alkaline phosphatase. Nature 198, 685-686 [PubMed:13945318] |
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