Literature summary for 3.4.23.16 extracted from

Kona, J.
Theoretical study on the mechanism of a ring-opening reaction of oxirane by the active-site aspartic dyad of HIV-1 protease (2008), Org. Biomol. Chem., 6, 359-365.

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Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	two possible mechanisms of the irreversible inhibition of HIV-1 protease by epoxide inhibitors are investigated on an enzymatic model using ab initio (MP2) and density functional theory methods (B3LYP, MPW1K and M05-2X). The calculations predict the inhibition as a general acid-catalyzed nucleophilic substitution reaction proceeding by a concerted SN2 mechanism with a reaction barrier of ca. 1521 kcal/mol. The irreversible nature of the inhibition is characterized by a large negative reaction energy of ca. -17-(-24) kcal/mol. A mechanism with a direct proton transfer from an aspartic acid residue of the active site onto the epoxide ring has been shown to be preferred compared to one with the proton transfer from the acid catalyst facilitated by a bridging catalytic water molecule	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

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Release 2023.1 (January 2023)