Literature summary for 3.4.23.16 extracted from

Louis, J.M.; Clore, G.M.; Gronenborn, A.M.
Autoprocessing of HIV-1 protease is tightly coupled to protein folding (1999), Nat. Struct. Biol., 6, 868-875.

Search for more literature for 3.4.23.16

Protein Variants

Protein Variants	Comment	Organism
Q7K/L33I/L63I/C67A/C95A	mutant enzyme with restricted autoproteolysis, self-degradation	Human immunodeficiency virus 1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.177	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, mutant enzyme Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
0.225	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, mutant enzyme Q7K/R8Q/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
0.278	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, wild-type enzyme	Human immunodeficiency virus 1
0.66	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, truncated version PR-(5-99) from mutant enzyme Q7K/L33I/L63I/C67A/C95A	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	regulation of the protease in the viral life cycle: transframe region flanking the N-terminus of the protease may function as a negative regulator for protein folding and dimerization. The low dimer stability of the protease precursor relative to that of the mature enzyme is an ideal way of preventing the emergence of enzymatic functions until assembly of the viral particle is complete	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	autoprocessing of the mature protease from the precursor can either occur in two steps at pH values of 4 tp 6 or in a single step above pH 6	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	-	?
additional information	autoprocessing of the mature protease from the precursor can either occur in two steps at pH values of 4 to 6 or in a single step above pH 6	Human immunodeficiency virus 1	?	-	?
additional information	regulation of the protease in the viral life cycle: transframe region flanking the N-terminus of the protease may function as a negative regulator for protein folding and dimerization. The low dimer stability of the protease precursor relative to that of the mature enzyme is an ideal way of preventing the emergence of enzymatic functions until assembly of the viral particle is complete	Human immunodeficiency virus 1	?	-	?

Subunits

Subunits	Comment	Organism
More	autoprocessing of the mature protease from the precursor can either occur in two steps at pH values of 4 tp 6 or in a single step above pH 6. The mature protease forms a dimer through a four-stranded beta-sheet at the interface. Residues 1-4 of the mature protease from each subunit constitute the outer strands of the beta-sheet, and are essential for maintaining the stability of the free protease	Human immunodeficiency virus 1

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.44	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, truncated version PR-(5-99) from mutant enzyme Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
3.74	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, wild-type enzyme	Human immunodeficiency virus 1
5.2	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, mutant enzyme Q7K/R8Q/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1
5.5	-	KARV-Nle-Phe(NO2)-EA-Nle-NH2	pH 5.0, 25°C, mutant enzyme Q7K/L33I/L63I/C67A/C95A	Human immunodeficiency virus 1

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Release 2023.1 (January 2023)