Literature summary for 3.4.21.97 extracted from

Snyder, S.W.; Edalji, R.P.; Lindh, F.G.; Walter, K.A.; Solomon, L.; Pratt, S.; Steffy, K.; Holzman, T.F.
Initial characterization of autoprocessing and active-center mutants of CMV proteinase (1996), J. Protein Chem., 15, 763-774.

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Protein Variants

Protein Variants	Comment	Organism
A133V	I-site mutant	Human betaherpesvirus 5
S132A	active-site mutant	Human betaherpesvirus 5

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
27000	-	2 * 27000, I-site mutant A134V, sedimentation equilibrium centrifugation of diluted enzyme solution	Human betaherpesvirus 5
54000	56000	I-site mutant A143V, sedimentation equilibrium centrifugation, the value is concentration-dependent	Human betaherpesvirus 5

Organism

Organism	UniProt	Comment	Textmining
Human betaherpesvirus 5	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	expressed in virus-infected cells as a 709-residue precursor that undergoes two autocatalytic cleavages to generate the mature enzyme form	Human betaherpesvirus 5

Subunits

Subunits	Comment	Organism
dimer	2 * 27000, I-site mutant A134V, sedimentation equilibrium centrifugation of diluted enzyme solution	Human betaherpesvirus 5

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
52	55	melting temperature of I-site mutant A143V	Human betaherpesvirus 5

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Release 2023.1 (January 2023)