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Literature summary extracted from

  • Wu, W.; Clem, R.J.; Rohrmann, G.F.; Passarelli, A.L.
    The baculovirus sulfhydryl oxidase Ac92 (P33) interacts with the Spodoptera frugiperda P53 protein and oxidizes it in vitro (2013), Virology, 447, 197-207 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.2 additional information construction of a mutant ac92-knockout virus Autographa californica nucleopolyhedrovirus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Autographa californica nucleopolyhedrovirus P41480 AcMNPV
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.2 additional information recombinant baculovirus in Spodoptera frugiperda SF9 insect cells Autographa californica nucleopolyhedrovirus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 dithiothreitol + O2
-
 Autographa californica nucleopolyhedrovirus dithiothreitol disulfide + H2O2
-
 r
1.8.3.2 protein SfP53 + O2
-
 Autographa californica nucleopolyhedrovirus protein SfP53 disulfide + H2O2
-
 ?
1.8.3.2 reduced thioredoxin + O2
-
 Autographa californica nucleopolyhedrovirus thioredoxin disulfide + H2O2
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 Ac92
-
 Autographa californica nucleopolyhedrovirus
1.8.3.2 FAD-linked sulfhydryl oxidase UniProt Autographa californica nucleopolyhedrovirus
1.8.3.2 P33
-
 Autographa californica nucleopolyhedrovirus
1.8.3.2 sulfhydryl oxidase
-
 Autographa californica nucleopolyhedrovirus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 FAD
-
 Autographa californica nucleopolyhedrovirus

General Information

EC Number General Information Comment Organism
1.8.3.2 malfunction silencing Sfp53 expression does not rescue the ability of an ac92-knockout virus to produce infectious virus. Similarly, ac92 expression does not affect SfP53-stimulated caspase activity or the localization of SfP53. Although Ac92 binds to SfP53 during AcMNPV replication and oxidizes SfP53 in vitro, no effects of this interaction on AcMNPV replication in cultured cells can be detected. Overexpression or silencing of Ac92 during virus infection does not affect SfP53 accumulation Autographa californica nucleopolyhedrovirus
1.8.3.2 physiological function the Autographa californica M nucleopolyhedrovirus (AcMNPV) sulfhydryl oxidase Ac92 is essential for production of infectious virions. Ac92 also interacts with human protein p53 and enhances human p53-induced apoptosis in insect cell. Enzyme Ac92 interacts with protein SfP53 from Spodoptera frugiperda in infected Sf9 cells and oxidizes SfP53 in vitro. Ac92 does not affect the cellular localization of SfP53 and partially co-localizes with SfP53 in Sf9 cells. Ac92 does not interact with or oxidize a mutant of SfP53 predicted to lack DNA binding. Ac92 possibly prevents DNA binding of SfP53. Ac92 expression does not stimulate significant caspase activity on its own, nor does it stimulate HA-SfP53-mediated caspase activation above levels induced by SfP53 alone or with an empty vector in transfected Sf9 cells Autographa californica nucleopolyhedrovirus