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Literature summary extracted from

  • Imkamp, F.; Rosenberger, T.; Striebel, F.; Keller, P.M.; Amstutz, B.; Sander, P.; Weber-Ban, E.
    Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo (2010), Mol. Microbiol., 75, 744-754.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.119 E10A mutation abolishes Dop activity both in vivo and in vitro Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.119 Mycolicibacterium smegmatis A0QZ49
-
-
3.5.1.119 Mycolicibacterium smegmatis ATCC 700084 A0QZ49
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.119 [prokaryotic ubiquitin-like protein]-L-glutamine + H2O
-
 Mycolicibacterium smegmatis [prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
 ?
3.5.1.119 [prokaryotic ubiquitin-like protein]-L-glutamine + H2O
-
 Mycolicibacterium smegmatis ATCC 700084 [prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
 ?

General Information

EC Number General Information Comment Organism
3.5.1.119 malfunction generation of a dop deletion mutant in Mycobacterium smegmatis. In the Ddop strain, pupylation is severely impaired and the steady-state levels of proteasomal substrate proteins is drastically increased Mycolicibacterium smegmatis
3.5.1.119 metabolism the enzyme is involved in targeted proteasomal degradation Mycolicibacterium smegmatis