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COO/COA

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C1752

Z-Ile-Ile

Name: Z-Ile-Ile
Brand: SIGMA

Synonym(s):

N-CBZ-Ile-Ile

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About This Item

Empirical Formula (Hill Notation):

C₂₀H₃₀N₂O₅

CAS Number:

42538-01-2

Molecular Weight:

378.46

EC Number:

255-876-9

MDL number:

MFCD00027066

UNSPSC Code:

12352202

PubChem Substance ID:

24892432

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form

solid

storage temp.

−20°C

SMILES string

CC[C@H](C)[C@@H](C(N[C@@H]([C@@H](C)CC)C(O)=O)=O)NC(OCC1=CC=CC=C1)=O

InChI

1S/C20H30N2O5/c1-5-13(3)16(18(23)21-17(19(24)25)14(4)6-2)22-20(26)27-12-15-10-8-7-9-11-15/h7-11,13-14,16-17H,5-6,12H2,1-4H3,(H,21,23)(H,22,26)(H,24,25)/t13?,14?,16?,17-/m0/s1

InChI key

QJJULDSUCQXEDB-DRRRZMAASA-N

Application

N-CBZ-Ile-Ile (Z-Ile-Ile) (CBZ-isoleucylisoleucine) is an N-terminal protected Cbz-dipeptide substrate used to differentiate, characterize and kinetically analyze various carboxypeptidase(s).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number

076H0829

057H0596

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Cathepsin A-like activity is possibly the main acidic carboxypeptidase in human platelets.

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

Characterization of a bifunctional aminoacylase/carboxypeptidase from radioresistant bacterium Deinococcus radiodurans R1.

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

Amphipathic property of free thiol group contributes to an increase in the catalytic efficiency of carboxypeptidase Y.

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

Debittering effect of Actinomucor elegans peptidases on soybean protein hydrolysates.

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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