Literature summary for 3.4.23.B6 extracted from

Veverka, V.; Bauerova, H.; Zabransky, A.; Lang, J.; Ruml, T.; Pichova, I.; Hrabal, R.
Three-dimensional structure of a monomeric form of a retroviral protease (2003), J. Mol. Biol., 333, 771-780.

Search for more literature for 3.4.23.B6

Crystallization (Commentary)

Crystallization (Comment)	Organism
NMR structure of a fully folded monomer of a 12000 Da M-PMV protease and of a C7A/D26N/C106A mutant	Mason-Pfizer monkey virus

Protein Variants

Protein Variants	Comment	Organism
C7A/C106A	the midpoint of the urea unfolding curve for 12000 Da truncated enzyme is at 1.9 M urea, the denaturation curve for the C7A/C106A mutant is no longer sigmoidal in character, confirming that this mutant is very unstable	Mason-Pfizer monkey virus
C7A/D26N/C106A	triple mutant of the 12000 Da truncated enzyme form shows significantly decreased capacity to dimerize	Mason-Pfizer monkey virus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.158	-	ATPQVYF(NO2)VRKA	13000 Da mutant enzyme C7A/106A	Mason-Pfizer monkey virus
0.386	-	ATPQVYF(NO2)VRKA	13000 Da enzyme form	Mason-Pfizer monkey virus
0.58	-	ATPQVYF(NO2)VRKA	12000 Da truncated mutant enzyme C7A/C106A	Mason-Pfizer monkey virus
1.7	-	ATPQVYF(NO2)VRKA	12000 Da truncated enzyme form	Mason-Pfizer monkey virus

Organic Solvent Stability

Organic Solvent	Comment	Organism
urea	the 13000 Da wild-type enzyme (which exhibits higher catalytic activity) loses 50% activity at 3.4 M urea, the midpoint of the urea unfolding curve of the 12000 Da truncated enzyme is at 1.9 M urea, the denaturation curve for the C7A/C106A mutant is no longer sigmoidal in character, confirming that this mutant is very unstable	Mason-Pfizer monkey virus

Organism

Organism	UniProt	Comment	Textmining
Mason-Pfizer monkey virus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the first M-PMV protease sequence that excises autocatalytically from the precursor at the N terminus of the protease domain, is a 17000 Da protein, which undergoes further self-processing at the C terminus yielding a 13000 Da protease. These proteases are identified in virions. In vitro, wild-type 13000 Da protease cleaves off another stretch of seven amino acid residues from the C terminus resulting in the shortest 12000 Da form protease. The truncation of the protease decreases its proteolytic activity, however the activity of wild-type 12000 Da protease is sufficient for processing of Gag-polyproteins in vivo	Mason-Pfizer monkey virus

Purification (Commentary)

Purification (Comment)	Organism
-	Mason-Pfizer monkey virus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATPQVYF(NO2)VRKA + H2O	-	Mason-Pfizer monkey virus	ATPQVY + F(NO2)VRKA	-	?

Synonyms

Synonyms	Comment	Organism
M-PMV protease	-	Mason-Pfizer monkey virus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.1	-	ATPQVYF(NO2)VRKA	12000 Da truncated mutant enzyme C7A/C106A	Mason-Pfizer monkey virus
0.51	-	ATPQVYF(NO2)VRKA	13000 Da mutant enzyme C7A/106A	Mason-Pfizer monkey virus
0.81	-	ATPQVYF(NO2)VRKA	12000 Da truncated enzyme form	Mason-Pfizer monkey virus
3.16	-	ATPQVYF(NO2)VRKA	13000 Da enzyme form	Mason-Pfizer monkey virus

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Release 2023.1 (January 2023)