Literature summary for 6.3.1.19 extracted from

Ofer, N.; Forer, N.; Korman, M.; Vishkautzan, M.; Khalaila, I.; Gur, E.
Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase (2013), J. Biol. Chem., 288, 11287-11293.

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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	key enzyme in the Pup tagging (i.e. pupylation) system. Protein pupylation can be regulated at the enzyme level via an allosteric mechanism	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	key enzyme in the Pup tagging (i.e. pupylation) system. Protein pupylation can be regulated at the enzyme level via an allosteric mechanism	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	P9WNU7	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein PanB]-L-lysine	a pupylation product with a molecular mass approximately 7 kDa heavier than PanB suggests that each PanB monomer is singly pupylated by PafA. PanB is pupylated primarily on either one of two lysines, namely Lys34 or Lys36. Pupylation on Lys137 is also detected, although less frequently	Mycobacterium tuberculosis	ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein PanB]-L-lysine	-	?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein PanB]-L-lysine	a pupylation product with a molecular mass approximately 7 kDa heavier than PanB suggests that each PanB monomer is singly pupylated by PafA. PanB is pupylated primarily on either one of two lysines, namely Lys34 or Lys36. Pupylation on Lys137 is also detected, although less frequently	Mycobacterium tuberculosis ATCC 25618	ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein PanB]-L-lysine	-	?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine	key enzyme in the Pup tagging (i.e. pupylation) system. Protein pupylation can be regulated at the enzyme level via an allosteric mechanism	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	PafA is an allosteric enzyme that binds its target substrates cooperatively. In contrast, binding of deamidated Pup (Pup-L-glutamate) by PafA follows simple kinetics and is, therefore, not involved in the allosteric transitions of PafA. Pup and target substrate binding by PafA are independent events	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	key enzyme in the Pup tagging (i.e. pupylation) system. Protein pupylation can be regulated at the enzyme level via an allosteric mechanism	Mycobacterium tuberculosis ATCC 25618	ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine	-	?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine	PafA is an allosteric enzyme that binds its target substrates cooperatively. In contrast, binding of deamidated Pup (Pup-L-glutamate) by PafA follows simple kinetics and is, therefore, not involved in the allosteric transitions of PafA. Pup and target substrate binding by PafA are independent events	Mycobacterium tuberculosis ATCC 25618	ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Mycobacterium tuberculosis

Synonyms

Synonyms	Comment	Organism
PafA	ambiguous	Mycobacterium tuberculosis
Pup ligase	-	Mycobacterium tuberculosis
ubiquitin-like protein ligase	-	Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0023	-	[prokaryotic ubiquitin-like protein]-L-glutamate	pH 8.0, 30°C	Mycobacterium tuberculosis
0.023	-	[protein PanB]-L-lysine	pH 8,0, 30°C	Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Mycobacterium tuberculosis

General Information

General Information	Comment	Organism
physiological function	in Mycobacterium tuberculosis Pup tagging is important for virulence	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)