Literature summary for 3.4.23.16 extracted from

Louis, J.M.; Ishima, R.; Nesheiwat, I.; Pannell, L.K.; Lynch, S.M.; Torchia, D.A.; Gronenborn, A.M.
Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties (2003), J. Biol. Chem., 278, 6085-6092.

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Protein Variants

Protein Variants	Comment	Organism
additional information	enzyme PR mutant with mutations Q7K/L33I/L63I/C67A/C95A and the additional mutation D25N/C2-S-S-C97, in which the terminal beta-strand is linked through a disulfide bridge, is less prone to aggregation, even at a relatively high protein concentration of about 1 mM	Human immunodeficiency virus 1
Q7K/D29N/L33I/L63I/C67A/C95A	920fold less active than with Q7K/L33I/L63I/C67A/C95A, poor catalytic activity arises both from the destabilization of the dimer as well as changes in the active site environment	Human immunodeficiency virus 1
Q7K/L33I/L63I/C67A/R87K/C95A	4600fold less active than with Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
Q7K/T26A/L33I/L63I/C67A/C95A	mutant enzyme with restricted autoproteolysis, mutation T26A destabilizes the dimer, exhibits a monomer fold and is prone to aggregation	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	P04585	-	-

Purification (Commentary)

Purification (Comment)	Organism
mutant enzymes Q7K/T26A/L33I/L63IC67A/C95A and Q7K/D29N/L33I/L63IC67A/C95A	Human immunodeficiency virus 1

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O	-	Human immunodeficiency virus 1	KARV-Nle + Phe(NO2)-EA-Nle-NH2	-	?

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Release 2023.1 (January 2023)