All Photos(2)
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
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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
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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)
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
J S Shin et al.
Biotechnology and bioengineering, 69(5), 577-583 (2000-07-18)
We recently demonstrated (J Am Chem Soc 121:3334-3340, 1999) that enzymatic enantioselectivity in organic solvents can be markedly enhanced by temporarily enlarging the substrate via salt formation. In the present study, this approach was expanded by finding that, in addition
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
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
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