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Literature summary 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 PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.19 recombinant expression of His6-tagged enzyme in Escherichia coli Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.19 Mg2+ required Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine Mycolicibacterium smegmatis
-
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine Mycolicibacterium smegmatis ATCC 700084 / mc2155
-
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.119 Mycolicibacterium smegmatis A0QZ49
-
-
3.5.1.119 Mycolicibacterium smegmatis ATCC 700084 A0QZ49
-
-
6.3.1.19 Mycolicibacterium smegmatis A0QZ42
-
-
6.3.1.19 Mycolicibacterium smegmatis ATCC 700084 / mc2155 A0QZ42
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.19 recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chormatography Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [IdeR]-L-lysine
-
Mycolicibacterium smegmatis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[IdeR]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [IdeR]-L-lysine
-
Mycolicibacterium smegmatis ATCC 700084 / mc2155 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[IdeR]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB]-L-lysine
-
Mycolicibacterium smegmatis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[PanB]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB]-L-lysine
-
Mycolicibacterium smegmatis ATCC 700084 / mc2155 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[PanB]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
-
Mycolicibacterium smegmatis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine the Pup product of the Dop reaction presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA Mycolicibacterium smegmatis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
-
Mycolicibacterium smegmatis ATCC 700084 / mc2155 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
?
6.3.1.19 ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine the Pup product of the Dop reaction presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA Mycolicibacterium smegmatis ATCC 700084 / mc2155 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.119 deamidase of Pup
-
Mycolicibacterium smegmatis
3.5.1.119 Dop
-
Mycolicibacterium smegmatis
6.3.1.19 PafA
-
Mycolicibacterium smegmatis
6.3.1.19 Pup ligase
-
Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.1.19 ATP
-
Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
3.5.1.119 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
6.3.1.19 metabolism posttranslational regulation of coordinated enzyme activities in the prokaryotic ubiquitin-like protein (Pup)-proteasome system (PPS), overview. Pup, a ubiquitin analogue, is conjugated to proteins through the activities of two enzymes, Dop (deamidase of Pup) and PafA (proteasome accessory factor A), the Pup ligase. The depupylase activity of Dop counteracts the actions of PafA. tight Pup binding and the limited degree of Dop interaction with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by enzyme Dop. Dop is depleted in the absence of Pup in stationary-phase cells. Pup-PanB and Pup-IdeR act as tight-binding competitors versus Pup binding by Dop. Pup binding stabilizes Dop and prevents its depletion. PafA and Dop generate a high-molecular-weight pupylome Mycolicibacterium smegmatis
6.3.1.19 physiological function Pup, a ubiquitin analogue, is conjugated to proteins through the activities of two enzymes, Dop (deamidase of Pup) and PafA (proteasome accessory factor A), the Pup ligase. Dop also catalyzes depupylation. Pupylation is a reversible process, with pupylated proteins being rescued from degradation following depupylation by Dop (deamidase of Pup). PafA (proteasome accessory factor A) and Dop are homologous enzymes, both binding Pup through interaction with its extended C-terminal region Mycolicibacterium smegmatis