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Key Documents

D4512

Sigma-Aldrich

Diazoacetyl-DL-norleucine methyl ester

crystalline

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About This Item

Empirical Formula (Hill Notation):
C9H15N3O3
CAS Number:
Molecular Weight:
213.23
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:

form

crystalline

color

yellow

storage temp.

−20°C

SMILES string

CCCCC(NC(=O)C=[N]=N)C(=O)OC

InChI

1S/C9H16N3O3/c1-3-4-5-7(9(14)15-2)12-8(13)6-11-10/h6-7,10H,3-5H2,1-2H3,(H,12,13)

InChI key

GPWYIOKNPCWZFQ-UHFFFAOYSA-N

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Wataru Nishii et al.
Biochemical and biophysical research communications, 301(4), 1023-1029 (2003-02-19)
Previously, we purified and partially characterized physarolisin, a lysosomal acid proteinase from Physarum polycephalum, which had been suggested to be concerned with the morphological changes of the mold. In this study, a cDNA for the enzyme was cloned and sequenced
Ostrich pepsins I and II: a kinetic and thermodynamic investigation.
B I Pletschke et al.
The international journal of biochemistry & cell biology, 27(12), 1293-1302 (1995-12-01)
G Iliadis et al.
FEBS letters, 352(3), 315-317 (1994-10-03)
Fourier transform (FTIR) difference spectra of pepsin minus diazoacetylnorleucine methyl ester (DAN) or minus diazoacetyl-L-phenylalanine methyl ester (DAP) modified pepsin, respectively, demonstrated that Asp-215 is not deprotonated in pepsin. The FTIR difference spectrum of pepsin minus 1,2-epoxyparanitrophenoxypropane (EPNP) modified pepsin
Senarath B P Athauda et al.
The Biochemical journal, 399(3), 535-542 (2006-07-04)
The wild type Copia Gag precursor protein of Drosophila melanogaster expressed in Escherichia coli was shown to be processed autocatalytically to generate two daughter proteins with molecular masses of 33 and 23 kDa on SDS/PAGE. The active-site motif of aspartic
Senarath B P Athauda et al.
The Biochemical journal, 381(Pt 1), 295-306 (2004-03-24)
Carnivorous plants are known to secrete acid proteinases to digest prey, mainly insects, for nitrogen uptake. In the present study, we have purified, for the first time, to homogeneity two acid proteinases (nepenthesins I and II) from the pitcher fluid

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