Literature summary for 3.4.23.16 extracted from

Short, G.F., 3rd; Laikhter, A.L.; Lodder, M.; Shayo, Y.; Arslan, T.; Hecht, S.M.
Probing the S1/S1' substrate binding pocket geometry of HIV-1 protease with modified aspartic acid analogues (2000), Biochemistry, 39, 8768-8781.

Search for more literature for 3.4.23.16

Protein Variants

Protein Variants	Comment	Organism
additional information	proteases with modified aspartic acid analogues at Asp25 or Asp125. Introduction of the beta-methyl moiety alters the protease function to varying extents depending upon ist orientation. While a beta-methyl group in the erythro orientation is the least deleterious to the specific activity of the protease, a beta-methyl group in the threo orientation, present in the modified proteins containing threo-beta-methylaspartate and beta,beta-dimethylaspartate, results in specific activities between 0 and 45% of that of the wild-type depending upon the substrate and the substituted active site position	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-(4-(dimethylamino)phenylazo)benzoyl-SQNYPIVQ-5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid + H2O	-	Human immunodeficiency virus 1	?	-	?
Abz-KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O	-	Human immunodeficiency virus 1	Abz-KARV-Nle + Phe(NO2)-EA-Nle-NH2	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)