Asparaginyl-phenylalanine

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Asparaginyl-phenylalanine
Category Others
Catalog number BBF-05076
CAS 22849-01-0
Molecular Weight 279.29
Molecular Formula C13H17N3O4

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Description

Asparaginyl-Phenylalanine is a dipeptide composed of asparagine and phenylalanine.

Specification

Synonyms L-Asparaginyl-L-phenylalanine; Asn-Phe
Sequence H-Asn-Phe-OH
IUPAC Name (2S)-2-[[(2S)-2,4-diamino-4-oxobutanoyl]amino]-3-phenylpropanoic acid
Canonical SMILES C1=CC=C(C=C1)CC(C(=O)O)NC(=O)C(CC(=O)N)N
InChI InChI=1S/C13H17N3O4/c14-9(7-11(15)17)12(18)16-10(13(19)20)6-8-4-2-1-3-5-8/h1-5,9-10H,6-7,14H2,(H2,15,17)(H,16,18)(H,19,20)/t9-,10-/m0/s1
InChI Key OMSMPWHEGLNQOD-UWVGGRQHSA-N

Properties

Boiling Point 645.8±55.0°C at 760 mmHg
Density 1.3±0.1 g/cm3

Reference Reading

1. Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide
Z Y Zhang, R A Poorman, L L Maggiora, R L Heinrikson, F J Kézdy J Biol Chem. 1991 Aug 25;266(24):15591-4.
Human immunodeficiency virus 1 (HIV-1) protease is an aspartyl protease composed of two identical protomers linked by a four-stranded antiparallel beta-sheet consisting of the NH2- and COOH-terminal segments (Weber, I.T. (1990) J. Biol. Chem. 265, 10492-10496). Kinetic analysis of the HIV-1 protease-catalyzed hydrolysis of a fluorogenic substrate demonstrates that the enzyme is an obligatory dimer. At pH = 5.0, 0.1 M sodium acetate, 1 M NaCl, 1 mM EDTA buffer, 37 degrees C, the equilibrium dissociation constant, Kd = 3.6 +/- 1.9 nM. We found that the tetrapeptide Ac-Thr-Leu-Asn-Phe-COOH, corresponding to the COOH-terminal segment of the enzyme, is an excellent inhibitor of the enzyme. Kinetic analysis shows that the inhibitor binds to the inactive protomers and prevents their association into the active dimer (dissociative inhibition). The dissociative nature of this inhibition is consistent with the results obtained from sedimentation equilibrium experiments in which the apparent molecular weight of the enzyme was observed to be 20,800 +/- 1,500 and 12,100 +/- 300, in the absence and presence of the COOH-terminal tetrapeptide, respectively. The dissociation constant of the protomer-inhibitor complex is Ki = 45.1 +/- 1.8 microM. This is the first kinetic analysis and direct experimental demonstration of noncovalent dissociative inhibition.

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