Literature summary for 3.4.23.B5 extracted from

Matsunaga, S.; Sawasaki, T.; Ode, H.; Morishita, R.; Furukawa, A.; Sakuma, R.; Sugiura, W.; Sato, H.; Katahira, M.; Takaori-Kondo, A.; Yamamoto, N.; Ryo, A.
Molecular and enzymatic characterization of XMRV protease by a cell-free proteolytic analysis (2012), J. Proteomics, 75, 4863-4873.

Search for more literature for 3.4.23.B5

Application

Application	Comment	Organism
analysis	development of an in vitro enzymatic assay system to characterize XMRV protease-mediated cleavage of host-cell proteins	Xenotropic MuLV-related virus VP62

Cloned(Commentary)

Cloned (Comment)	Organism
expression in wheat-germ cell-free system	Xenotropic MuLV-related virus VP62

Crystallization (Commentary)

Crystallization (Comment)	Organism
homology modeling of protease in complex with amprenavir. The amino acids at the active site of HIV-1, HTLV proteases and those likely to be at the active site of XMRV protease are comparatively conserved. Amprenavir interacts with residue Asp32 of the catalytic domain, and also contacts the residues Val39, Lys61, Tyr90, and Leu92. A water molecule would intermediate interactions between amprenavir and Ala57	Xenotropic MuLV-related virus VP62

Crystallization (Comment)

Organism

homology modeling of protease in complex with amprenavir. The amino acids at the active site of HIV-1, HTLV proteases and those likely to be at the active site of XMRV protease are comparatively conserved. Amprenavir interacts with residue Asp32 of the catalytic domain, and also contacts the residues Val39, Lys61, Tyr90, and Leu92. A water molecule would intermediate interactions between amprenavir and Ala57

Xenotropic MuLV-related virus VP62

Protein Variants

Protein Variants	Comment	Organism
A57V	99.7% of wild-type activity, 26.6% residual activity in presence of 1 microM amprenavir	Xenotropic MuLV-related virus VP62
K61L	10.3% of wild-type activity, 95% residual activity in presence of 1 microM amprenavir	Xenotropic MuLV-related virus VP62
V39I	23.5% of wild-type activity, 53% residual activity in presence of 1 microM amprenavir	Xenotropic MuLV-related virus VP62
V39I/A57V	27% of wild-type activity, no residual activity in presence of 1 microM amprenavir	Xenotropic MuLV-related virus VP62
Y90A/L92V	15.6% of wild-type activity, 81.7% residual activity in presence of 1 microM amprenavir	Xenotropic MuLV-related virus VP62

Inhibitors

Inhibitors	Comment	Organism	Structure
amprenavir	catalytic activity of XMRV protease is selectively blocked by the HIV protease inhibitor, amprenavir, 13.9% residual activity at 1 microM	Xenotropic MuLV-related virus VP62

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
14000	-	x * 17000 and x * 14000, SDS-PAGE, corresponding to the expected mobility of the full-length protease and the truncated form by auto-cleavage of the flanking 20 amino acids at both ends	Xenotropic MuLV-related virus VP62
17000	-	x * 17000 and x * 14000, SDS-PAGE, corresponding to the expected mobility of the full-length protease and the truncated form by auto-cleavage of the flanking 20 amino acids at both ends	Xenotropic MuLV-related virus VP62

Organism

Organism	UniProt	Comment	Textmining
Xenotropic MuLV-related virus VP62	A1Z651	GAG-POL protein	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
FLAG-pr55Gag + H2O	-	Xenotropic MuLV-related virus VP62	?	-	?
human tumor suppressor protein ARL11 + H2O	-	Xenotropic MuLV-related virus VP62	?	-	?
human tumor suppressor protein BAX + H2O	-	Xenotropic MuLV-related virus VP62	?	-	?
human tumor suppressor protein DKK3 + H2O	-	Xenotropic MuLV-related virus VP62	?	-	?
human tumor suppressor protein PTEN + H2O	-	Xenotropic MuLV-related virus VP62	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 17000 and x * 14000, SDS-PAGE, corresponding to the expected mobility of the full-length protease and the truncated form by auto-cleavage of the flanking 20 amino acids at both ends	Xenotropic MuLV-related virus VP62