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Literature summary for 6.3.1.19 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
Search for more literature for 6.3.1.19

Cloned(Commentary)

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QZ42
-
-
Mycolicibacterium smegmatis ATCC 700084 / mc2155 A0QZ42
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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

Synonyms Comment Organism
PafA
-
 Mycolicibacterium smegmatis
Pup ligase
-
 Mycolicibacterium smegmatis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
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
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