Information on EC 3.5.1.119 - Pup amidohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.119
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RECOMMENDED NAME
GeneOntology No.
Pup amidohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3
show the reaction diagram
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[His6-myo-inositol-1-phosphate synthetase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [His6-myo-inositol-1-phosphate synthetase]-L-lysine
show the reaction diagram
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
show the reaction diagram
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
show the reaction diagram
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme with ATP, protein (Pup) ligase PafA and the depupylase/deamidase Dop are are close structural homologues
structure of full-length Dop, to 2.6 A resolution and to 2.85 A resolution in complex with ATP. The active site is located on the concave surface of the beta-sheet with the nucleotide bound in a deep pocket. A conserved groove leading into the active site could play a role in Pup-binding
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expressed in Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme is highly insoluble when overproduced in Escherichia coli
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the dop gene is cloned with a C-terminal His6-tag, expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
pharmacology