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Literature summary for 6.3.1.19 extracted from

  • Barandun, J.; Damberger, F.F.; Delley, C.L.; Laederach, J.; Allain, F.H.; Weber-Ban, E.
    Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins (2017), BMC Struct. Biol., 17, doi: 10.1186/s12900-017-0072-1 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.1.19

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium tuberculosis

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 Mycobacterium tuberculosis
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 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine Mycobacterium tuberculosis ATCC 25618 / H37Rv
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 ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNU7
-
-
Mycobacterium tuberculosis ATCC 25618 / H37Rv P9WNU7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB]-L-lysine PanB from Mycobacterium tuberculosis is pupylated at a single lysine residue, K212, formation of a covalent MtbPup-MtbPanB conjugate Mycobacterium tuberculosis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[PanB]-L-lysine
-
 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB]-L-lysine PanB from Mycobacterium tuberculosis is pupylated at a single lysine residue, K212, formation of a covalent MtbPup-MtbPanB conjugate Mycobacterium tuberculosis ATCC 25618 / H37Rv ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[PanB]-L-lysine
-
 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
-
 Mycobacterium tuberculosis ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
 ?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
-
 Mycobacterium tuberculosis ATCC 25618 / H37Rv ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
-
 ?
additional information the prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins. When linked to the proteasomal substrates FabD and PanB, Pup is unstructured and retains the ability to interact with its different binding partners. This suggests that it is not the conformation of Pup attached to these two substrates which determines their delivery to the proteasome, but the availability of the degradation complex and the depupylase. Structure analysis of Pup coupled to the PanB decamer, overview Mycobacterium tuberculosis ?
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 ?
additional information the prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins. When linked to the proteasomal substrates FabD and PanB, Pup is unstructured and retains the ability to interact with its different binding partners. This suggests that it is not the conformation of Pup attached to these two substrates which determines their delivery to the proteasome, but the availability of the degradation complex and the depupylase. Structure analysis of Pup coupled to the PanB decamer, overview Mycobacterium tuberculosis ATCC 25618 / H37Rv ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycobacterium tuberculosis