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Literature summary for 3.4.21.97 extracted from

  • Hall, M.R.T.; Gibson, W.
    Cytomegalovirus assemblin: the amino and carboxy domains of the proteinase form active enzyme when separately cloned and coexpressed in eukaryotic cells (1996), J. Virol., 70, 5395-5404.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
assembly protein precursor of cytomegalovirus + H2O Human betaherpesvirus 5 the enzyme is essential for virus replication and functions during capsid assembly from pAP, i.e. assembly protein precursor ?
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Organism

Organism UniProt Comment Textmining
Human betaherpesvirus 5
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the proteinase is synthesized as an enzymatiacally active precursor that undergoes several autoproteolytic cleavages. Two of these are common in all herpes group viruses, one occurs toward the carboxyl end of the precursor, i.e. M-site, and the other near the middle at the R-site. The R-site cleavage divides the precusor into assemblin and a nonproteolytic carboxyl half. CMV proteinase undergoes a third autoproteolytic cleavage that divides assemblin into approximately equal-size An and Ac subunits. None of these cleavages is absolutely necessary for enzyme activity Human betaherpesvirus 5

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
assembly protein precursor of cytomegalovirus + H2O the enzyme is essential for virus replication and functions during capsid assembly from pAP, i.e. assembly protein precursor Human betaherpesvirus 5 ?
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 ?