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Information on EC 3.5.1.124 - protein deglycase and Organism(s) Escherichia coli and UniProt Accession Q46948
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EC Tree
3.5.1.124 protein deglycaseIUBMB 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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Word Map
- 3.5.1.124
- methylglyoxal
- gsh
-
detoxify
- neurodegenerative
- d-lactate
-
dicarbonyls
- ascorbate
- dismutase
- seedlings
-
dopaminergic
- chlorophyll
-
neuroprotective
-
non-enzymatic
- alzheimer
-
early-onset
- mellitus
- malondialdehyde
-
substantia
-
mg-induced
- dehydroascorbate
- pink1
-
endproducts
- lipoxygenase
- rage
- monodehydroascorbate
-
ascorbate-glutathione
-
d-lactic
- mdhar
-
glutathione-dependent
- hemithioacetal
- s-d-lactoylglutathione
-
sh-sy5y
-
pd-related
- properdin
- phytochelatins
-
atp13a2
- diagnostics
- alpha-synuclein
-
pd-associated
-
anti-glycation
-
gsh-dependent
-
asa-gsh
- trypanothione
- drug development
- aminoguanidine
-
methylglyoxal-induced
-
deglycation
-
hyperglycaemia
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine
+
=
+
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine
+
=
a [protein]-L-lysine
+
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DJ-1 protein
-
-
-
-
PARK7
-
-
-
-
yajL
-
-
-
-
yhbO
additional information
yhbO
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate
reaction mechanism via spontaneous aminocarbinol formation, H migration catalyzed by deglycase, and amidolysis by deglycase. The mechnaism is similar for L-cysteine and L-arginine deglycation
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate
reaction mechanism via spontaneous aminocarbinol formation, H migration catalyzed by deglycase, and amidolysis by deglycase. The mechnaism is similar for L-cysteine and L-arginine deglycation
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-amino acid + H2O
a [bovine serum albumin]-L-amino acid + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YajL efficiently deglycates FBP as glycation occurs
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YajL efficiently deglycates FBP as glycation occurs
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O
a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
glyceraldehyde-3-phosphate dehydrogenase activity decreases to 40% in absence of a deglycase, while in the presence of YajL, glyceraldehyde-3-phosphate dehydrogenase remains 100% active, suggesting that YajL deglycates GAPDH as glycation occurs
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-arginine + H2O
a [aspartate aminotransferase]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O
a [aspartate aminotransferase]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-amino acid + H2O
a [bovine serum albumin]-L-amino acid + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-lysine + H2O
a [bovine serum albumin]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O
a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
glyceraldehyde-3-phosphate dehydrogenase activity decreases to 40% in absence of a deglycase, while in the presence of YhbO, glyceraldehyde-3-phosphate dehydrogenase decreases only to 80% of its initial activity, suggesting that YhbO deglycates GAPDH as glycation occurs
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
N-acetyl-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YhbO efficiently deglycates FBP as glycation occurs
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YhbO efficiently deglycates FBP as glycation occurs
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
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 + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
additional information
?
-
the enzyme also shows GSH-independent activity of glyoxylase III, EC 4.2.1.130. The apparent glyoxalase activity of YhbO, EC 4.2.1.130, reflects its deglycase activity
-
-
?
additional information
?
-
the enzyme also shows GSH-independent activity of glyoxylase III, EC 4.2.1.130. The apparent glyoxalase activity of YhbO, EC 4.2.1.130, reflects its deglycase activity
-
-
?
additional information
?
-
-
the enzyme also shows GSH-independent activity of glyoxylase III, EC 4.2.1.130. The apparent glyoxalase activity of YhbO, EC 4.2.1.130, reflects its deglycase activity
-
-
?
additional information
?
-
the enzyme also shows GSH-independent activity of glyoxylase III, EC 4.2.1.130. The apparent glyoxalase activity of YhbO, EC 4.2.1.130, reflects its deglycase activity
-
-
?
additional information
?
-
the enzyme also shows GSH-independent activity of glyoxylase III, EC 4.2.1.130. The apparent glyoxalase activity of YhbO, EC 4.2.1.130, reflects its deglycase activity
-
-
?
additional information
?
-
-
the enzyme also shows GSH-independent activity of glyoxylase III, EC 4.2.1.130. The apparent glyoxalase activity of YhbO, EC 4.2.1.130, reflects its deglycase activity
-
-
?
additional information
?
-
the enzyme DJ-1 also shows glyoxalase III activity, cf. EC 4.2.1.130, which is representative of its deglycase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
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 + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55 - 95
enzyme activity is reduced by 72% for YhbO 70°C, YhbO is inactive at 95°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
enzyme YajL belongs to the PfpI/Hsp31/DJ-1 superfamily
malfunction
bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. yajL mutants display decreased viability in methylglyoxal- or glucose-containing media
physiological function
the enzyme is involved in protection against environmental stresses, it protect scells against protein glycation. It repairs glyoxal- and methylglyoxal-glycated proteins. YajL repairs glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase
evolution
malfunction
physiological function
evolution
enzyme YhbO belongs to the PfpI/Hsp31/DJ-1 superfamily
evolution
Hsp31 is a member of the PfpI/Hsp31/DJ-1 superfamily whose members possess a conserved exposed cysteine involved in environmental stress resistance
malfunction
bacterial extracts from a hchA mutant display increased glycation levels and the apparent glyoxylase activity of Hsp31 reflects its deglycase activity
malfunction
bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. yhbO mutants display decreased viability in methylglyoxal- or glucose-containing media
physiological function
Hsp31 is reported to function as a chaperone, an aminopeptidase, and a glutathione-independent glyoxylase. Enzyme Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal, it repairs glycated serum albumin, glyceraldehyde-3-phosphate dehydrogenase, fructose biphosphate aldolase, and aspartate aminotransferase. Since glycation with methylglyoxal and glyoxal inactivates the enzymes partially or completely, the protein deglycase HSp31 functionally protects the enzymes. To execute its deglycase activity, Hsp31 recruits its previously reported functions: 1. chaperone activity to interact with nonnative glycated proteins and gain access to partially buried glycated sites, 2. glyoxalase 1 activity to interact with glycated substrates and convert hemithioacetals into thioesters, and aminocarbinols into amides, 3. reactive cysteine 185 to attack carbonyl groups of thioesters and amides, 4. glyoxalase 2 activity to cut thioesters for cysteine deglycation, and 5. amidase/peptidase activity to cut amide bonds for lysine/arginine deglycation. The requirement of these apparently disparate functions of Hsp31 for deglycation strongly suggests that deglycation is its primary function
physiological function
the enzyme is involved in protection against environmental stresses, it protects cells against protein glycation. It repairs glyoxal- and methylglyoxal-glycated proteins. YhbO repairs glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Overexpression of YhbO (from the pBAD-yhbO plasmid) in a wild-type strain overexpressing the YeaG kinase (from pET-21ayeaG) decreases protein aggregation from 7% to 2%, and decreases protein glycation by approximately 60%
physiological function
the enzyme prevents acrylamide formation in vivo, acrylamide formation in the glyoxal/asparagine mixture is reduced by 78% by YhbO
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
additional information
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
additional information
-
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
additional information
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
additional information
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
additional information
-
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mihoub, M.; Abdallah, J.; Gontero, B.; Dairou, J.; Richarme, G.
The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal
Biochem. Biophys. Res. Commun.
463
1305-1310
2015
Escherichia coli (P31658)
Abdallah, J.; Mihoub, M.; Gautier, V.; Richarme, G.
The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal
Biochem. Biophys. Res. Commun.
470
282-286
2016
Escherichia coli (P45470), Escherichia coli (Q46948), Escherichia coli
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