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Literature summary for 3.5.1.119 extracted from

  • Elharar, Y.; Roth, Z.; Hecht, N.; Rotkopf, R.; Khalaila, I.; Gur, E.
    Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system (2016), Proc. Natl. Acad. Sci. USA, 113, E1605-E1614.
    View publication on PubMed
Search for more literature for 3.5.1.119

Organism

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

Synonyms Comment Organism
deamidase of Pup
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 Mycolicibacterium smegmatis
Dop
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 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
metabolism tight Pup binding and the limited degree of interaction of the enzyme (Dop) with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by this enzyme. Under starvation conditions, when accelerated protein pupylation is required, this bias is intensified by depletion of free Dop molecules, thereby minimizing the chance of depupylation. In contrast to Dop (deamidase of Pup), PafA (proteasome accessory factor A), presents a distinct preference for highmolecular-weight protein substrates. As such, PafA and Dop act in concert, rather than canceling each other's activity, to generate a high-molecular-weight pupylome. This bias in pupylome molecular weight distribution is consistent with the proposed nutritional role of the Pup-proteasome system (PPS) under starvation conditions Mycolicibacterium smegmatis