Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.1.19 extracted from

  • Delley, C.L.; Striebel, F.; Heydenreich, F.M.; ึzcelik, D.; Weber-Ban, E.
    Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation (2012), J. Biol. Chem., 287, 7907-7914.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.1.19

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine Mycobacterium tuberculosis pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
-
 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine Mycobacterium tuberculosis ATCC 25618 pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNU7
-
-
Mycobacterium tuberculosis ATCC 25618 P9WNU7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive Mycobacterium tuberculosis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
-
 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly at Lys591 Mycobacterium tuberculosis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
-
 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive Mycobacterium tuberculosis ATCC 25618 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
-
 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly at Lys591 Mycobacterium tuberculosis ATCC 25618 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
-
 ?

Synonyms

Synonyms Comment Organism
PafA ambiguous Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism pupylation is a bacterial post-translational modification of target proteins on lysine residues with prokaryotic ubiquitinlike protein (Pup). Pup-tagged substrates are recognized by a proteasome-interacting ATPase (Mpa) in Mycobacterium tuberculosis. Mpa unfolds pupylated substrates and threads them into the proteasome core particle for degradation Mycobacterium tuberculosis