Literature summary for 3.4.23.B10 extracted from

Schatz, G.W.; Reinking, J.; Zippin, J.; Nicholson, L.K.; Vogt, V.M.
Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function (2001), J. Virol., 75, 4761-4770.

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Protein Variants

Protein Variants	Comment	Organism
additional information	mutations at the N-terminus: deletions of one or three residues, addition of one residue or substitution of Alan for the N-terminal Leu reduces enzymatic activity on peptide and protein substrates 100fold to 1000fold. The purified mutant enzymes remain monomeric up to a concentration of about 2 mg/ml. The three-dimensional structure of the monomeric mutant protein lacking the three N-terminal residues, DELTALAM, is significantly different from that of the wild-type enzyme	Rous sarcoma virus

Organism

Organism	UniProt	Comment	Textmining
Rous sarcoma virus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
mutant and wild-type enzymes	Rous sarcoma virus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
PAVSLAMT + H2O	-	Rous sarcoma virus	PAVS + LAMT	-	?
PFQAYPLREA + H2O	-	Rous sarcoma virus	PFQAY + PLREA	-	?

Subunits

Subunits	Comment	Organism
dimer	all retrovirus proteases are homodimers and dimerization is essential for enzymatic function	Rous sarcoma virus

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Release 2023.1 (January 2023)