HIV Protease Substrate IV
HIV Protease Substrate IV structure
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Common Name | HIV Protease Substrate IV | ||
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| CAS Number | 128340-47-6 | Molecular Weight | 1090.28000 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C49H83N15O13 | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease.
J. Gen. Virol. 87(Pt 5) , 1321-30, (2006) The protease (PR) of Murine leukemia virus (MLV) was expressed in Escherichia coli, purified to homogeneity and characterized by using various assay methods, including HPLC-based, photometric and fluorometric activity measurements. The specificity of the bact... |
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Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.
FEBS J. 272(20) , 5265-77, (2005) HIV-1 protease (PR) and two drug-resistant variants--PR with the V82A mutation (PR(V82A)) and PR with the I84V mutation (PR(I84V))--were studied using reduced peptide analogs of five natural cleavage sites (CA-p2, p2-NC, p6pol-PR, p1-p6 and NC-p1) to understa... |
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Interactions of a novel inhibitor from an extremophilic Bacillus sp. with HIV-1 protease: implications for the mechanism of inactivation.
J. Biol. Chem. 276(4) , 2487-93, (2001) The active site cleft of the HIV-1 protease (PR) is bound by two identical conformationally mobile loops known as flaps, which are important for substrate binding and catalysis. The present article reports, for the first time, an HIV-1 PR inhibitor, ATBI, fro... |
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Sensitive, soluble chromogenic substrates for HIV-1 proteinase.
J. Biol. Chem. 265 , 7733, (1990) By replacement of the P1' residue in a capsid/nucleocapsid cleavage site mimic with 4-NO2-phenylalanine (Nph), an excellent chromogenic substrate, Lys-Ala-Arg-Val-Leu*Nph-Glu-Ala-Met, for HIV-1 proteinase (kappa cat = 20 s-1, Km = 22 microM) has been prepared... |
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Hydrolysis of synthetic chromogenic substrates by HIV-1 and HIV-2 proteinases.
Biochem. Biophys. Res. Commun. 171 , 439, (1990) Kinetic constants (Km,Kcat) are derived for the hydrolysis of a number of chromogenic peptide substrates by the aspartic proteinase from HIV-2. The effect of systematic replacement of the P2 residue on substrate hydrolysis by HIV-1 and HIV-2 proteinases is ex... |