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Literature summary for 3.4.23.16 extracted from

  • Yamazaki, T.; Nicholson, L.K.; Torchia, D.A.; Wingfield, P.; Stahl, S.J.; Kaufman, J.D.; Eyerman, C.J.; Hodge, C.N.; Lam, P.Y.S.; Ru, Y.; Jadhav, P.K.; Chang, C.H.; Weber, P.C.
    NMR and X-Ray evidence that the HIV protease catalytic aspartyl groups have an essential role in the complex formed by the protease and a non-peptide cyclic urea-based inhibitor (1994), J. Am. Chem. Soc., 116, 10791-10792.
No PubMed abstract available

Application

Application Comment Organism
medicine the enzyme is an attractive target for antiviral drugs of HIV-1 Human immunodeficiency virus 1

Cloned(Commentary)

Cloned (Comment) Organism
the enzyme is cloned in pMAL-cRI and expressed as a MBP-pol fusion protein in Escherichia coli XL1-blue Human immunodeficiency virus 1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0098
-
His-Lys-Ala-Arg-Val-Leu-(4-nitro)Phe-Glu-Ala-Nle-Ser-amide
-
Human immunodeficiency virus 1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Human immunodeficiency virus 1 the enzyme is essential for the replication of the virus ?
-
?

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Human immunodeficiency virus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
His-Lys-Ala-Arg-Val-Leu-(4-nitro)Phe-Glu-Ala-Nle-Ser-amide + H2O
-
Human immunodeficiency virus 1 His-Lys-Ala-Arg-Val-Leu + (4-nitro)Phe-Glu-Ala-Nle-Ser-amide
-
?
additional information the enzyme exhibits autoprocessing Human immunodeficiency virus 1 ?
-
?
additional information the enzyme is essential for the replication of the virus Human immunodeficiency virus 1 ?
-
?