C1877
Z-Ile-Leu
Synonym(s):
N-CBZ-Ile-Ieu
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About This Item
Empirical Formula (Hill Notation):
C20H30N2O5
CAS Number:
Molecular Weight:
378.46
UNSPSC Code:
12352200
PubChem Substance ID:
MDL number:
InChI
1S/C20H30N2O5/c1-5-14(4)17(18(23)21-16(19(24)25)11-13(2)3)22-20(26)27-12-15-9-7-6-8-10-15/h6-10,13-14,16-17H,5,11-12H2,1-4H3,(H,21,23)(H,22,26)(H,24,25)
SMILES string
CCC(C)C(NC(=O)OCc1ccccc1)C(=O)NC(CC(C)C)C(O)=O
InChI key
BSRAGXJNZJMFMY-UHFFFAOYSA-N
storage temp.
−20°C
Biochem/physiol Actions
N-CBZ-Ile-Ieu (Z-Ile-Ieu) (CBZ-isoleucylleucine) is an N-terminal protected Cbz-dipeptide substrate used to differentiate, characterize and kinetically analyze various carboxypeptidase(s).
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Joji Mima et al.
European journal of biochemistry, 269(13), 3220-3225 (2002-06-27)
Cys341 of carboxypeptidase Y, which constitutes one side of the solvent-accessible surface of the S1 binding pocket, was replaced with Gly, Ser, Asp, Val, Phe or His by site-directed mutagenesis. Kinetic analysis, using Cbz-dipeptide substrates, revealed that polar amino acids
Long-Liu Lin et al.
Journal of biotechnology, 128(2), 322-334 (2006-11-30)
The gene encoding a Deinococcus radiodurans R1 bifunctional aminoacylase/carboxypeptidase (DR_ACY/CP) was amplified by polymerase chain reaction and cloned into pQE-30 to generate pQE-DRAC. The cloned gene consists of an open reading frame of 1197 bp encoding a protein with a
H Ostrowska
Platelets, 8(5), 355-360 (2006-06-24)
Human platelets were investigated for activity of the acidic carboxypeptidases: cathepsin A, lysosomal carboxypeptidase B and prolyl-carboxypeptidase. It was found that the main acidic carboxypeptidase in human platelets had cathepsin A activity. No activity of lysosomal carboxypeptidase B and prolyl-carboxypeptidase
Li Li et al.
Journal of industrial microbiology & biotechnology, 35(1), 41-47 (2007-10-19)
Effects of the enzymes in Actinomucor elegans extract and the enzyme Alcalase 2.4L on debittering the soybean protein hydrolysates were investigated. When the protein was treated only with the latter, a strong bitterness formed; but it decreased if the protein
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