Literature summary for 3.5.1.119 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.

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Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Mycolicibacterium smegmatis	A0QZ49	-	-
Mycolicibacterium smegmatis ATCC 700084	A0QZ49	-	-

Substrates and Products (Substrate)

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

General Information

General Information	Comment	Organism
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
metabolism	the enzyme is involved in targeted proteasomal degradation	Mycolicibacterium smegmatis

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Release 2023.1 (January 2023)