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525472

Sigma-Aldrich

D-Phenylalanine methyl ester hydrochloride

98%

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About This Item

Linear Formula:
C6H5CH2CH(NH2)CO2CH3 · HCL
CAS Number:
Molecular Weight:
215.68
MDL number:
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.22

Assay

98%

reaction suitability

reaction type: solution phase peptide synthesis

mp

159-163 °C (lit.)

application(s)

peptide synthesis

storage temp.

2-8°C

SMILES string

Cl[H].COC(=O)[C@H](N)Cc1ccccc1

InChI

1S/C10H13NO2.ClH/c1-13-10(12)9(11)7-8-5-3-2-4-6-8;/h2-6,9H,7,11H2,1H3;1H/t9-;/m1./s1

InChI key

SWVMLNPDTIFDDY-SBSPUUFOSA-N

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Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Ikuo Kira et al.
Journal of bioscience and bioengineering, 108(3), 190-193 (2009-08-12)
Screening was carried out for microorganisms able to produce N-(l-alpha-l-aspartyl)-l-phenylalanine methyl ester [APM] from l-isoasparagine and l-phenylalanine methyl ester hydrochloride. Of the 422 strains examined, 44 strains belonging to the family Enterobacteriaceae were found to produce APM. The enzyme catalyzing
Shotaro Tsuchiyama et al.
Biotechnology progress, 23(4), 820-823 (2007-05-08)
The PST-01 protease is a metalloprotease that has zinc ion at the active center and is very stable in the presence of water-soluble organic solvents. The reaction rates and the equilibrium yields of the aspartame precursor N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester (Cbz-Asp-Phe-OMe)
Robert Rennert et al.
Biochimica et biophysica acta, 1758(3), 347-354 (2005-12-29)
Many promising therapeutics are currently awaiting their clinical application. Due to their low capability of cell membrane crossing, these compounds do not reach their site of action. One way to overcome this problem might be the fusion of these agents
Andrew J Quinn et al.
Biotechnology progress, 27(6), 1554-1560 (2012-01-12)
The direct one-step synthesis of L-phenylalanine methyl ester in an organic-aqueous biphasic system using phenylalanine ammonia lyase (E.C.4.3.1.5, PAL) containing Rhodotorula glutinis yeast whole cells was reported earlier. We report here further optimization of this biotransformation using isolated PAL, when
S Reissmann et al.
Journal of medicinal chemistry, 39(4), 929-936 (1996-02-16)
For further studies on the structural and conformational requirements of positions 2,3, and 7 in the bradykinin sequence, we replaced the proline residues by the more hydrophobic and conformationally restricted N-methyl-L- and D-phenylalanine (NMF). The biological activities of the new

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