Information on EC 3.5.1.124 - protein deglycase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.5.1.124
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RECOMMENDED NAME
GeneOntology No.
protein deglycase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + (R)-lactate
show the reaction diagram
an Nomgega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + (R)-lactate
show the reaction diagram
(1)
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-
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an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + (R)-lactate
show the reaction diagram
(3)
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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 (R)-lactate, depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-arginine + H2O
a [aspartate aminotransferase]-L-arginine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O
a [aspartate aminotransferase]-L-lysine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-amino acid + H2O
a [bovine serum albumin]-L-amino acid + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-lysine + H2O
a [bovine serum albumin]-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O
a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
show the reaction diagram
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
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
show the reaction diagram
-
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
show the reaction diagram
-
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-arginine + H2O
N-acetyl-L-arginine + (R)-lactate
show the reaction diagram
-
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
N-acetyl-L-cysteine + (R)-lactate
show the reaction diagram
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-lysine + H2O
N-acetyl-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-N-acetyl-L-cysteine + H2O
[bovine serum albumin]-L-cysteine + (R)-lactate
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
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
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-arginine
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pH 7.0, 22C
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0.32
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine
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pH 7.0, 22C
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0.35
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-lysine
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pH 7.0, 22C
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additional information
additional information
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biphasic kinetics for aminocarbinol degradation, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-arginine
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pH 7.0, 22C
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0.42
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine
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pH 7.0, 22C
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0.28
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-lysine
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pH 7.0, 22C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 95
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant soluble and active enzyme from Escherichia coli by anion exchange and hydroxy apatite chromatography followed by dialysis
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression in Escherichia coli from pET21a-DJ-1 plasmid
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C106S
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site-directed mutagenesis, inactive mutant
C46S
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
C53S
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
additional information
Show AA Sequence (264 entries)
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