525472
D-苯丙氨酸甲酯 盐酸盐
98%
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线性分子式:
C6H5CH2CH(NH2)CO2CH3 · HCL
化学文摘社编号:
分子量:
215.68
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.22
MDL number:
产品名称
D-苯丙氨酸甲酯 盐酸盐, 98%
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
assay
98%
reaction suitability
reaction type: solution phase peptide synthesis
mp
159-163 °C (lit.)
application(s)
peptide synthesis
storage temp.
2-8°C
Quality Level
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存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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
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
Y Watanabe et al.
Biochimica et biophysica acta, 1337(1), 40-46 (1997-01-04)
A newly isolated actinomycete belonging to Saccharothrix sp. was found to produce a unique enzyme catalyzing D-amino acid transfer. The enzyme, which was tentatively named D-amino acid transferase, was purified 2600-fold to electrophoretic homogeneity and the molecular mass was 41
L Ye et al.
Journal of molecular recognition : JMR, 11(1-6), 75-78 (1999-03-17)
We have studied the possibility of shifting a thermodynamically unfavourable enzymatic equilibrium towards product formation via the addition of a highly specific adsorbent. The commercially interesting enzymatic condensation of Z-L-aspartic acid with L-phenylalanine methyl ester to the sweetener aspartame was
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