L-Phenylalanine

CAS# 63-91-2

L-Phenylalanine

Catalog No. BCN3818----Order now to get a substantial discount!

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Quality Control of L-Phenylalanine

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Chemical structure

L-Phenylalanine

3D structure

Chemical Properties of L-Phenylalanine

Cas No. 63-91-2 SDF Download SDF
PubChem ID 6140 Appearance Powder
Formula C9H11NO2 M.Wt 165.19
Type of Compound Alkaloids Storage Desiccate at -20°C
Solubility H2O : 6.67 mg/mL (40.38 mM; Need ultrasonic)
Chemical Name (2S)-2-amino-3-phenylpropanoic acid
SMILES C1=CC=C(C=C1)CC(C(=O)O)N
Standard InChIKey COLNVLDHVKWLRT-QMMMGPOBSA-N
Standard 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
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months.
Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it.
About Packaging 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial.
2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial.
3. Try to avoid loss or contamination during the experiment.
Shipping Condition Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request.

Source of L-Phenylalanine

The seeds of Glycine max (L.) Merr

Biological Activity of L-Phenylalanine

DescriptionL-Phenylalanine has antibacterial activity.
TargetsAntifection
In vitro

Microbial synthesis of deuterium labelled L-phenylalanine with different levels of isotopic enrichment by facultative methylotrophic bacterium Brevibacterium methylicum with RMP assimilation of carbon.[Pubmed: 25249528]

Biomed Khim. 2014 Jul-Aug;60(4):448-61.


METHODS AND RESULTS:
The preparative microbial synthesis of amino acids labelled with stable isotopes, including deuterium ( 2 H), suitable for biomedical applications by methylotrophic bacteria was studied using L-Phenylalanine as example. This amino acid is secreted by Gram-negative aerobic facultative methylotrophic bacteria Brevibacterium methylicum, assimilating methanol via ribulose-5-monophosphate (RMP) cycle of assimilation of carbon, The data on adaptation of L-Phenylalanine secreted by methylotrophic bacterium В. methylicum to the maximal concentration of deuterium in the growth medium with 98% 2 Н 2 O and 2% [ 2 Н]methanol, and biosynthesis of deuterium labelled L-Phenylalanine With different levels of enrichment are presented. The strain was adapted by means of plating initial cells on firm (2% agarose) minimal growth media with an increasing gradient of 2 Н 2 O concentration from 0; 24.5; 49.0; 73.5 up to 98% 2 Н 2 O followed by subsequent selection of separate colonies stable to the action of 2 Н 2 O. These colonies were capable to produce L-Phenylalanine. L-Phenylalanine was extracted from growth medium by extraction with isopropanol with the subsequent crystallization in ethanol (output 0.65 g/l).
CONCLUSIONS:
The developed method of microbial synthesis allows to obtain deuterium labelled L-Phenylalanine with different levels of isotopic enrichment, depending on concentration of 2 Н 2 O in growth media, from 17% (on growth medium with 24,5% 2 Н 2 O) up to 75% (on growth medium with 98% 2 Н 2 O) of deuterium in the molecule that is confirmed with the data of the electron impact (EI) mass- spectrometry analysis of methyl ethers of N-dimethylamino(naphthalene)-5-sulfochloride (dansyl) phenylalanine in these experimental conditions.

In vivo

Improvement of constraint-based flux estimation during L-phenylalanine production with Escherichia coli using targeted knock-out mutants.[Pubmed: 24449451]

Biotechnol Bioeng. 2014 Jul;111(7):1406-16.


METHODS AND RESULTS:
Fed-batch production of the aromatic amino acid L-Phenylalanine was studied with recombinant Escherichia coli strains on a 15 L-scale using glycerol as carbon source. Flux Variability Analysis (FVA) was applied for intracellular flux estimation to obtain an insight into intracellular flux distribution during L-Phenylalanine production. Variability analysis revealed great flux uncertainties in the central carbon metabolism, especially concerning malate consumption. Due to these results two recombinant strains were genetically engineered differing in the ability of malate degradation and anaplerotic reactions (E. coli FUS4.11 ΔmaeA pF81kan and E. coli FUS4.11 ΔmaeA ΔmaeB pF81kan). Applying these malic enzyme knock-out mutants in the standardized L-Phenylalanine production process resulted in almost identical process performances (e.g., L-Phenylalanine concentration, production rate and byproduct formation). This clearly highlighted great redundancies in central metabolism in E. coli.
CONCLUSIONS:
Uncertainties of intracellular flux estimations by constraint-based analyses during fed-batch production of L-Phenylalanine were drastically reduced by application of the malic enzyme knock-out mutants.

Protocol of L-Phenylalanine

Structure Identification
Microbiol Res. 2014 Sep-Oct;169(9-10):675-85.

A study of the antibacterial activity of L-phenylalanine and L-tyrosine esters in relation to their CMCs and their interactions with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, DPPC as model membrane.[Pubmed: 24667307]

Cationic amino acid-based surfactants are known to interact with the lipid bilayer of cell membranes resulting in depolarization, lysis and cell death through a disruption of the membrane topology.
METHODS AND RESULTS:
A range of cationic surfactant analogues derived from L-Phenylalanine (C1-C20) and L-Tyrosine (C8-C14) esters have been synthesized and screened for their antibacterial activity.

L-Phenylalanine Dilution Calculator

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L-Phenylalanine Molarity Calculator

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Preparing Stock Solutions of L-Phenylalanine

1 mg 5 mg 10 mg 20 mg 25 mg
1 mM 6.0536 mL 30.2682 mL 60.5364 mL 121.0727 mL 151.3409 mL
5 mM 1.2107 mL 6.0536 mL 12.1073 mL 24.2145 mL 30.2682 mL
10 mM 0.6054 mL 3.0268 mL 6.0536 mL 12.1073 mL 15.1341 mL
50 mM 0.1211 mL 0.6054 mL 1.2107 mL 2.4215 mL 3.0268 mL
100 mM 0.0605 mL 0.3027 mL 0.6054 mL 1.2107 mL 1.5134 mL
* Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations.

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Background on L-Phenylalanine

H-Phe-OH

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References on L-Phenylalanine

A study of the antibacterial activity of L-phenylalanine and L-tyrosine esters in relation to their CMCs and their interactions with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, DPPC as model membrane.[Pubmed:24667307]

Microbiol Res. 2014 Sep-Oct;169(9-10):675-85.

Cationic amino acid-based surfactants are known to interact with the lipid bilayer of cell membranes resulting in depolarization, lysis and cell death through a disruption of the membrane topology. A range of cationic surfactant analogues derived from L-Phenylalanine (C1-C20) and L-Tyrosine (C8-C14) esters have been synthesized and screened for their antibacterial activity. The esters were more active against gram positive than gram negative bacteria. The activity increased with increasing chain length, exhibiting a cut-off effect at C12 for gram positive and C8/C10 for gram negative bacteria. The cut-off effect for gram negative bacteria was observed at a lower alkyl chain length. The CMC was correlated with the MIC, inferring that micellar activity contribute to the cut-off effect in antibacterial activity. The interaction of the cationic surfactants with the phospholipid vesicles (1,2-dipalmitoyl-sn-glycero-3-phosphocholine, DPPC) in the presence of 1-anilino-8-naphthalene sulfonate (ANS) and 1,6-diphenyl-1,3,5-hexatriene (DPH) as fluorescence probes showed that an increase in ionic interaction causes an increase in antibacterial activity. Increase in hydrophobic interaction increases the antibacterial activity only to a certain chain length, attributing to the cut-off effect. Therefore, both electrostatic and hydrophobic interactions, involving the polar and nonpolar moieties are of paramount importance for the bactericidal properties.

Improvement of constraint-based flux estimation during L-phenylalanine production with Escherichia coli using targeted knock-out mutants.[Pubmed:24449451]

Biotechnol Bioeng. 2014 Jul;111(7):1406-16.

Fed-batch production of the aromatic amino acid L-Phenylalanine was studied with recombinant Escherichia coli strains on a 15 L-scale using glycerol as carbon source. Flux Variability Analysis (FVA) was applied for intracellular flux estimation to obtain an insight into intracellular flux distribution during L-Phenylalanine production. Variability analysis revealed great flux uncertainties in the central carbon metabolism, especially concerning malate consumption. Due to these results two recombinant strains were genetically engineered differing in the ability of malate degradation and anaplerotic reactions (E. coli FUS4.11 DeltamaeA pF81kan and E. coli FUS4.11 DeltamaeA DeltamaeB pF81kan). Applying these malic enzyme knock-out mutants in the standardized L-Phenylalanine production process resulted in almost identical process performances (e.g., L-Phenylalanine concentration, production rate and byproduct formation). This clearly highlighted great redundancies in central metabolism in E. coli. Uncertainties of intracellular flux estimations by constraint-based analyses during fed-batch production of L-Phenylalanine were drastically reduced by application of the malic enzyme knock-out mutants.

[Microbial synthesis of deuterium labelled L-phenylalanine with different levels of isotopic enrichment by facultative methylotrophic bacterium Brevibacterium methylicum with RMP assimilation of carbon].[Pubmed:25249528]

Biomed Khim. 2014 Jul-Aug;60(4):448-61.

The preparative microbial synthesis of amino acids labelled with stable isotopes, including deuterium ( 2 H), suitable for biomedical applications by methylotrophic bacteria was studied using L-Phenylalanine as example. This amino acid is secreted by Gram-negative aerobic facultative methylotrophic bacteria Brevibacterium methylicum, assimilating methanol via ribulose-5-monophosphate (RMP) cycle of assimilation of carbon, The data on adaptation of L-Phenylalanine secreted by methylotrophic bacterium capital VE, Cyrillic. methylicum to the maximal concentration of deuterium in the growth medium with 98% 2 capital EN, Cyrillic 2 O and 2% [ 2 capital EN, Cyrillic]methanol, and biosynthesis of deuterium labelled L-Phenylalanine With different levels of enrichment are presented. The strain was adapted by means of plating initial cells on firm (2% agarose) minimal growth media with an increasing gradient of 2 capital EN, Cyrillic 2 O concentration from 0; 24.5; 49.0; 73.5 up to 98% 2 capital EN, Cyrillic 2 O followed by subsequent selection of separate colonies stable to the action of 2 capital EN, Cyrillic 2 O. These colonies were capable to produce L-Phenylalanine. L-Phenylalanine was extracted from growth medium by extraction with isopropanol with the subsequent crystallization in ethanol (output 0.65 g/l). The developed method of microbial synthesis allows to obtain deuterium labelled L-Phenylalanine with different levels of isotopic enrichment, depending on concentration of 2 capital EN, Cyrillic 2 O in growth media, from 17% (on growth medium with 24,5% 2 capital EN, Cyrillic 2 O) up to 75% (on growth medium with 98% 2 capital EN, Cyrillic 2 O) of deuterium in the molecule that is confirmed with the data of the electron impact (EI) mass- spectrometry analysis of methyl ethers of N-dimethylamino(naphthalene)-5-sulfochloride (dansyl) phenylalanine in these experimental conditions.

Description

L-Phenylalanine ((S)-2-Amino-3-phenylpropionic acid) is an essential amino acid isolated from Escherichia coli. L-Phenylalanine is a α2δ subunit of voltage-dependent Ca+ channels antagonist with a Ki of 980 nM. L-phenylalanine is a competitive antagonist for the glycine- and glutamate-binding sites of N-methyl-D-aspartate receptors (NMDARs) (KB of 573 μM ) and non-NMDARs, respectively. L-Phenylalanine is widely used in the production of food flavors and pharmaceuticals.

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