Literature summary for 3.4.23.16 extracted from

Mahalingam, B.; Louis, J.M.; Reed, C.C.; Adomat, J.M.; Krouse, J.; Wang, Y.F.; Harrison, R.W.; Weber, I.T.
Structural and kinetic analysis of drug resistant mutants of HIV-1 protease (1999), Eur. J. Biochem., 263, 238-245.

Search for more literature for 3.4.23.16

Cloned(Commentary)

Cloned (Comment)	Organism
HIV-1 protease clone for expression in Escherichia coli is constructed with the substitutions Q7K/L33I/L63I/C67A/C95A. The expressed enzyme is purified from inclusion bodies	Human immunodeficiency virus 1

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant enzymes R8Q, K45I and L90M are crystallized with the inhibitor RVL-(reduced peptide bond)-FEA-Nle-NH2	Human immunodeficiency virus 1

Protein Variants

Protein Variants	Comment	Organism
D30N	similar to wild-type enzyme in stability towards urea denaturation. The kcat/Km ratio for the substrate KARVLAEAMS is 113% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
G48V	the kcat/Km ratio for the substrate KARVLAEAMS is 55% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
G48V	half maximal activity at 0.7 M urea compared to 1.8 M for the wild-type enzyme	Human immunodeficiency virus 1
K45I	mutant with significantly increased stability with half-maximal activity at 3.3 mM urea compared to 1.8 M urea for the wild-type enzyme. The kcat/Km ratio for the substrate KARVLAEAMS is 106% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
L90M	the kcat/Km ratio for the substrate KARVLAEAMS is 44% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A. Half maximal activity at 1.0 M urea compared to 1.8 M for the wild-type enzyme	Human immunodeficiency virus 1
M46L	the kcat/Km ratio for the substrate KARVLAEAMS is 63% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
N88D	mutant with significantly increased stability with half-maximal activity at 3.1 mM urea compared to 1.8 M urea for the wild-type enzyme. The kcat/Km ratio for the substrate KARVLAEAMS is 39% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
Q7K/L33I/L63I/C67A/C95A	the kinetic parameters are nearly identical to those of the native enzyme. Half maximal activity at 1.9 M urea compared to 1.8 M for the wild-type enzyme	Human immunodeficiency virus 1
Q7K/L33I/L63I/C67A/C95A	mutant enzyme with restricted autoproteolysis, self-degradation	Human immunodeficiency virus 1
R8Q	half maximal activity at 1.3 M urea compared to 1.8 M for the wild-type enzyme. The kcat/Km ratio for the substrate KARVLAEAMS is 15% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
V82S	similar to wild-type enzyme in stability towards urea denaturation. The kcat/Km ratio for the substrate KARVLAEAMS is 24% of that for the autoproteolysis resistant variant Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	RVL-(reduced peptide bond)-FEA-Nle-NH2 and Ac-TI-Nle-(reduced peptide bond)-Nle-QR-NH2	Human immunodeficiency virus 1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.06	-	KARV-Nle-Phe(NO2)-EA-Nle	pH 5.0, wild-type enzyme	Human immunodeficiency virus 1
0.075	-	KARV-Nle-Phe(NO2)-EA-Nle	pH 5.0, mutant enzyme Q7K/L33I/L63I/C67A/C95A	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.
KARV-Nle-Phe(NO2)-EA-Nle + H2O	-	Human immunodeficiency virus 1	KARV-Nle + Phe(NO2)-EA-Nle	-	?
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O	-	Human immunodeficiency virus 1	KARV-Nle + Phe(NO2)-EA-Nle-NH2	-	?
KARVLAEAMS + H2O	-	Human immunodeficiency virus 1	KARVL + AEAMS	-	?
TLNFPISPKK + H2O	-	Human immunodeficiency virus 1	TLNF + PISPKK	-	?
VSFNFPQITKK + H2O	-	Human immunodeficiency virus 1	VSFNF + PQITKK	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.767	-	KARV-Nle-Phe(NO2)-EA-Nle	pH 5.0, mutant enzyme Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
1.23	-	KARV-Nle-Phe(NO2)-EA-Nle	pH 5.0, wild-type enzyme	Human immunodeficiency virus 1

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Release 2023.1 (January 2023)