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Information on EC 3.5.1.124 - protein deglycase and Organism(s) Pyrococcus furiosus and UniProt Accession Q51732

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.124 protein deglycase
IUBMB Comments
The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].
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Pyrococcus furiosus
UNIPROT: Q51732
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Word Map
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine
+
H2O
=
a [protein]-L-arginine
+
lactate
an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine
+
=
+
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine
+
H2O
=
a [protein]-L-lysine
+
lactate
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine
+
=
a [protein]-L-lysine
+
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine
+
H2O
=
a [protein]-L-cysteine
+
(R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine
+
=
a [protein]-L-cysteine
+
Synonyms
glyoxalase, park7, dj-1 protein, deglycase, protein deglycase, parkinsonism-associated protein dj-1, dj-1 deglycase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Maillard deglycase
-
DJ-1 protein
-
-
-
-
PARK7
-
-
-
-
yajL
-
-
-
-
yhbO
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming]
The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
assay at, deglycase activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme PfpI belongs to the PfpI/Hsp31/DJ-1 superfamily
physiological function
the enzyme prevents acrylamide formation in vivo, acrylamide formation in the glyoxal/asparagine mixture is reduced by 72% by PfpI
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Richarme, G.; Marguet, E.; Forterre, P.; Ishino, S.; Ishino, Y.
DJ-1 family Maillard deglycases prevent acrylamide formation
Biochem. Biophys. Res. Commun.
478
1111-1116
2016
Escherichia coli (P45470), Pyrococcus furiosus (Q51732), Pyrococcus furiosus, Homo sapiens (Q99497)
Manually annotated by BRENDA team