Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase

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

EC NUMBER
COMMENTARY hide
3.1.2.6
-
RECOMMENDED NAME
GeneOntology No.
hydroxyacylglutathione hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
hydrolysis of thioester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methylglyoxal degradation I
-
-
methylglyoxal degradation
-
-
Pyruvate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
S-(2-hydroxyacyl)glutathione hydrolase
Also hydrolyses S-acetoacetylglutathione, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-90-5
-
9025-92-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
upregulated by NaCl, Zn, and ABA
Swissprot
Manually annotated by BRENDA team
cv. BINA sharisha 3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
IFO 0895
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
gene gloB
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
ectopic expression of OsGLYII-2 in Escherichia coli and tobacco provides improved tolerance against salinity and dicarbonyl stress indicating towards its role in abiotic stress tolerance; OsGLYII-2 is able to functionally complement a yeast GLY II mutant
metabolism
-
drought stress slightly decreases activity, selenium-pretreated seedlings maintain higher activity at either level of drought
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
bis-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
show the reaction diagram
-
-
-
?
bis-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
show the reaction diagram
preferred substrate
trypathione is bis(glutathionyl)spermidine
?
D-lactoyltrypanothione + H2O
D-lactate + trypanothione
show the reaction diagram
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
show the reaction diagram
mono-(lactoyl)trypanothione + H2O
trypanothione + D-lactate
show the reaction diagram
preferred substrate
trypathione is bis(glutathionyl)spermidine
?
N,S-bisfluorenylmethoxycarbonylglutathione + H2O
9-fluorenylmethoxycarboxylate + glutathione
show the reaction diagram
-
-
-
-
?
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
show the reaction diagram
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione + H2O
beta-ethoxy-alpha-D-hydroxybutyrate + glutathione
show the reaction diagram
-
-
-
-
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
?
show the reaction diagram
-
slow model substrate for computational study, the substrate does not coordinate to any of the zinc ions in the Michaelis complex. The hydroxyl group forms a hydrogen bond to the Asp58 residue.
-
-
?
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O
N-hydroxy-N-bromophenylcarbamate + glutathione
show the reaction diagram
-
weak substrate
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
show the reaction diagram
S-acetylglutathione + H2O
acetate + glutathione
show the reaction diagram
S-acetyltrypanothione + H2O
acetate + trypanothione
show the reaction diagram
-
-
-
?
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
show the reaction diagram
-
-
-
?
S-D-lactoylglutathione
D-lactate + glutathione
show the reaction diagram
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
S-D-lactoylglutathione + H2O
D-lactic acid + glutathione
show the reaction diagram
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
show the reaction diagram
S-D-lactoylglutathione + H2O
glutathione + D-lactic acid
show the reaction diagram
-
-
-
-
r
S-D-lactoyltrypanothione + H2O
D-lactate + trypanothione
show the reaction diagram
-
additionally S-D-lactoylglutathione used by mutant Y291R/C294K
-
-
?
S-D-mandeloylglutathione + H2O
? + glutathione
show the reaction diagram
-
-
-
?
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
show the reaction diagram
S-formylglutathione + H2O
formate + glutathione
show the reaction diagram
S-glycerylglutathione + H2O
glycerate + glutathione
show the reaction diagram
S-glycoloylglutathione + H2O
glycolate + glutathione
show the reaction diagram
S-glycolylglutathione + H2O
? + glutathione
show the reaction diagram
hydrolysis at about half the rate of S-lactoylglutathione
-
-
?
S-glycolyltrypanothione + H2O
glycolate + trypanothione
show the reaction diagram
-
-
-
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
show the reaction diagram
-
-
-
?
S-lactonylglutathione + H2O
? + glutathione
show the reaction diagram
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
S-lactoylglutathione + H2O
GSH + D-lactate
show the reaction diagram
-
-
-
-
?
S-lactoylglutathionylspermidine + H2O
?
show the reaction diagram
-
-
-
?
S-m-nitrobenzyloxycarbonylglutathione + H2O
m-nitrobenzyloxycarboxylate + glutathione
show the reaction diagram
-
-
-
-
?
S-mandeloylglutathione + H2O
mandelate + glutathione
show the reaction diagram
S-mandeloylglutathione + H2O
mandelic acid + glutathione
show the reaction diagram
hydrolysis about 10fold lower than of S-lactoylglutathione
-
-
?
S-methyl hydroxy(phenyl)ethanethioate + H2O
methanethiol + hydroxy(phenyl)acetic acid
show the reaction diagram
S-o-nitrobenzyloxycarbonylglutathione + H2O
o-nitrobenzyloxycarboxylate + glutathione
show the reaction diagram
-
-
-
-
?
S-p-nitrobenzyloxycarbonylglutathione + H2O
p-nitrobenzyloxycarboxylate + glutathione
show the reaction diagram
-
-
-
-
?
S-propionylglutathione + H2O
propionate + glutathione
show the reaction diagram
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
show the reaction diagram
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
show the reaction diagram
trypanothione hemithioacetal + H2O
?
show the reaction diagram
-
-
-
-
ir
additional information
?
-
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
lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
-
reaction is rate-limiting, methylglyoxal bypass of glycolysis
-
-
r
S-(2-hydroxyacyl)glutathione + H2O
glutathione + a 2-hydroxycarboxylate anion
show the reaction diagram
S-acetyltrypanothione + H2O
acetate + trypanothione
show the reaction diagram
Q581U6
-
-
-
?
S-bis-lactoyltrypanothione + 2 H2O
2 D-lactate + trypanothione
show the reaction diagram
Q581U6
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
S-D-lactoylglutathione + H2O
glutathione + D-lactate
show the reaction diagram
S-D-lactoylglutathione + H2O
glutathione + D-lactic acid
show the reaction diagram
-
-
-
-
r
S-glycolyltrypanothione + H2O
glycolate + trypanothione
show the reaction diagram
Q581U6
-
-
-
?
S-hydroxyglutaryltrypanothione + H2O
hydroxyglutarate + trypanothione + 2 H+
show the reaction diagram
Q581U6
-
-
-
?
S-lactoylglutathionylspermidine + H2O
?
show the reaction diagram
Q581U6
-
-
-
?
S-propionyltrypanothione + H2O
propionate + trypanothione + H+
show the reaction diagram
Q581U6
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
glxII apoenzyme activity is regained
Cobalt
0.6 mol per mol of protein
Ni2+
-
no activity of glxII, re-addition of Zn2+ results in a further inhibition of the residual enzyme activity of the incompletely demetalled apo-GlxII
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12-O-tetradecanoylphorbol-13-acetate
-
-
2,4,6-Trinitrobenzenesulfonate
2-aminopyridine
-
-
acidic phospholipids
-
noncompetitive inhibition, lower thermal stability of the enzyme, inhibit protein intermolecular interactions/aggregation by thermal denaturation, small changes in the secondary structure are caused
-
adenine
-
-
adenosine
-
-
aniline
-
-
Anionic phospholipids
-
noncompetitive inhibition, cytosolic isozyme
-
AsO2-
-
-
benzimidazole
-
-
Caffeine
-
-
cardiolipin
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
CdCl2
-
-
copper acetate
-
above 15 mM
cytidine
-
-
D-lactate
diethyldicarbonate
dioleoyl phosphatidic acid
-
i.e. DOPA, negatively charged phospholipid, strongly inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
dipalmitoylphosphatidylserine
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
diphosphate
-
25 mM, 50% inhibition
DTT
-
1.25 mM, 60% inhibition
EDTA
-
-
Fe2+
addition to the medium slightly reduces the activity in vivo
fructose
-
inactivation of the glyoxalase system (glyoxalase I and II) in fructose fed mice
glutathione
glutathione ethyl ester
-
carboxylate group of the glycine-moiety is modified, non-competitive inhibition
Guanidine-HCl
-
below 1 M, inactivation occurs without loss of the secondary structure
guanine
-
-
guanosine
-
-
hemithioacetal
-
-
-
hexyl-S-glutathione
-
-
iodoacetate
KCl
-
above 15 mM
methylene blue
-
photoinactivation
methylglyoxal
methylglyoxal-glutathione hemimercaptal
-
Mn2+
addition to the medium reduces the activity in vivo
N,S-(dicarbobenzoxy)glutathione
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione
-
N,S-bis-(phenylmethoxycarbonyl)glutathione
-
N,S-bis-carbobenzoxy-glutathione
-
-
N,S-bis-FMOC-glutathione
-
-
N,S-bisfluorenylmethoxycarbonylglutathione
-
-
-
N-(9-fluorenylmethoxycarbonyl)-S-phenylmethoxycarbonylglutathione
-
N-(9-fluorenylmethoxycarbonyl)glutathione
-
N-acetyl-S-(p-bromobenzyl)glutathione
N-benzoyl-S-(p-bromobenzyl)glutathione
-
-
N-benzyloxycarbonyl-S-(p-bromobenzyl)glutathione
-
-
N-phenylmethoxycarbonyl-S-(9-fluorenylmethoxycarbonyl)glutathione
-
N-phenylmethoxycarbonylglutathione
-
NaCl
-
above 15 mM
NH4Cl
-
above 15 mM
octyl-S-glutathione
-
-
oxalate
-
20 mM, 38% inhibition
p-hydroxymercuribenzoate
-
-
p-nitrobenzyl-S-glutathione
-
very weak
Phenylglyoxal
phosphate
-
67 mM, 35% inhibition
phosphatidylserine
-
negatively charged phospholipid, inhibits the cytosolic isozyme noncompetitively, specific ionic and probably also hydrophobic interaction
propyl-S-glutathione
-
-
pyridoxal
-
-
pyridoxamine
-
-
S,N-blocked glutathiones
-
-
-
S-(9-fluorenylmethoxycarbonyl)glutathione
-
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione
50% inhibition at 0.002 mM; 50% inhibition at 0.03 mM
S-(N-hydroxy-N-phenylcarbamoyl)glutathione
50% inhibition at 0.006 mM; 50% inhibition at 0.185 mM
S-(p-Azidophenacyl)-glutathione
S-(p-azidophenacyl)glutathione
-
S-(p-bromobenzyl)glutathione
-
-
S-(p-chlorophenacyl)glutathione
S-benzyloxycarbonylglutathione
S-blocked glutathiones
-
-
-
S-fluorenylmethyloxycarbonylglutathione
S-hexylglutathione
-
S-m-nitrobenzyloxycarbonylglutathione
S-o-nitrobenzyloxycarbonylglutathione
S-p-nitrobenzyloxycarbonylglutathione
S-phenylmethoxycarbonylglutathione
-
S-propylglutathione
-
Theobromine
-
-
theophylline
-
-
thymine
-
-
transcription factor p63
-
upregulation of glyoxalase II
-
transcription factor p73
-
upregulation of glyoxalase II
-
Trinitrobenzenesulfonate
-
-
Uracil
-
-
uridine
-
-
xanthine
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
auxin
-
enhances activity of both gly I and II
Zn2+
2fold activation; 2fold activation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.086
bis-(lactoyl)trypanothione
pH 7.2, 25°C; recombinant enzyme, pH 7.2, 25°C
3
lactoylglutathione
or above, pH 7.2, 25°C
0.039 - 0.108
mono-(lactoyl)trypanothione
0.152 - 0.283
S-(2-hydroxyacyl)glutathione
0.044 - 0.703
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
0.054 - 0.841
S-Acetoacetylglutathione
0.034 - 0.83
S-acetylglutathione
0.144
S-acetyltrypanothione
-
0.164
S-bis-lactoyltrypanothione
-
0.06 - 5.782
S-D-lactoylglutathione
0.32
S-D-lactoylgutathione
-
pH 6.5, 30°C, substrate concentration 1.5-3 mM
0.092 - 0.15
S-D-lactoyltrypanothione
0.009 - 0.0365
S-D-mandeloylglutathione
0.153 - 0.213
S-formylglutathione
0.109
S-glyceroylglutathione
0.07 - 1.16
S-glycolylglutathione
0.265
S-glycolyltrypanothione
-
0.133
S-hydroxyglutaryltrypanothione
-
0.0966
S-L-glyceroylglutathione
-
-
0.0007 - 0.6
S-Lactoylglutathione
0.195
S-lactoylglutathionylspermidine
-
0.19
S-lactylglutathione
0.014 - 0.0164
S-mandeloylglutathione
0.213 - 1.2
S-propionylglutathione
0.109
S-propionyltrypanothione
-
0.134 - 0.535
S-succinylglutathione
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
82
S-Acetoacetylglutathione
-
-
10.6 - 6780
S-D-lactoylglutathione
16 - 241
S-D-lactoyltrypanothione
25.8 - 183
S-D-mandeloylglutathione
1740
S-glycoloylglutathione
-
-
1490
S-L-glyceroylglutathione
-
-
64.3 - 780
S-Lactoylglutathione
188 - 755
S-mandeloylglutathione
68
S-succinylglutathione
-
-
additional information
additional information
-
turnover-numver is pH-independent in the range pH 6-9.3
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11 - 10000
S-D-lactoylglutathione
180 - 1600
S-D-lactoyltrypanothione
710 - 2200
S-D-mandeloylglutathione
2000
S-Lactoylglutathione
-
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
cardiolipin
-
cytosolic isozyme, pH 7.2, 25°C
0.000031
D-lactate
-
inhibitor binding to the free enzyme, at 25°C, pH 6.8
2.3
di-carbobenzoxyglutahione
-
-
-
0.0002
dioleoyl phosphatidic acid
-
cytosolic isozyme, pH 7.2, 25°C
0.0022
dipalmitoylphosphatidylserine
-
cytosolic isozyme, pH 7.2, 25°C
25
diphosphate
-
-
3.5 - 13
glutathione
14 - 49
glutathione ethyl ester
0.00089 - 0.0028
N,S-bis-(9-fluorenylmethoxycarbonyl)glutathione
0.0023
N,S-bis-(phenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.89
N,S-bis-FMOC-glutathione
-
-
0.0017
N-(9-fluorenylmethoxycarbonyl)-S-phenylmethoxycarbonylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.015
N-(9-fluorenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.002
N-phenylmethoxycarbonyl-S-(9-fluorenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.0056
N-phenylmethoxycarbonylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.055
phosphatidylserine
-
cytosolic isozyme, pH 7.2, 25°C
0.014
S-(9-fluorenylmethoxycarbonyl)glutathione
recombinant wild-type enzyme, pH 7.2, 25°C
0.0005 - 0.035
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
0.0007 - 0.05
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione
0.006
S-(N-hydroxy-N-phenylcarbamoyl)glutathione
25°C
1.3
S-(p-azidophenacyl)glutathione
25°C
1.5
S-hexylglutathione
25°C
0.0049
S-phenylmethoxycarbonylglutathione
recombinant wild-type enzyme, pH 7.2, 25°C
1.9
S-propylglutathione
25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
glutathione
Salmonella enterica subsp. enterica serovar Typhimurium
-
Mn-GloB, in 10 mM MOPS buffer, 0.2 M NaCl, pH 7.2, at 30 °C
additional information
additional information
Salmonella enterica subsp. enterica serovar Typhimurium
-
Fe- and Zn-GloB is inhibited at submillimolar concentrations of glutathione, in 10 mM MOPS buffer, 0.2 M NaCl, pH 7.2, at 30 °C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
clone B2 (pHD678/GLXII) plus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.05
clone B4 (p2T7/GLXII) plus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.21
wild-type minus tetracycine, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.22
clone B4 (p2T7/GLXII) minus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference; clone K3 (pHD678) minus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.23
clone K3 (pHD678) plus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
0.27
clone B2 (pHD678/GLXII) minus tetracycline, GLX II activity in bloodstream Trypanosoma brucei subject to RNA interference
2.35
-
enzyme from intermembrane space
4
-
mitochondrial enzyme
24.3
-
cytosolic enzyme
63
S-hydroxyglutaryltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
65
-
-
73
S-glycolyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
92
S-bis-lactoyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
96
S-propionyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
115
S-lactoylglutathionylspermidine as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
117
S-acetyltrypanothione as substrate, kinetic parameters of recombinant enzyme are determined in 100 mM MOPS
134.6
-
-
169
-
matrix enzyme
536.4
-
-
2007
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
saturation kinetic behavior for the phosphate diester hydrolysis reaction
6.5 - 9
-
mitochondrial enzyme
7.1
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
-
6.3 - 7.7
pH 6.3: aout 65% of maximal activity, pH 7.7: about 80% of maximal activity
7 - 9
-
saturation kinetic behavior for the thioester hydrolysis reaction. At pH 9.0 ligand exchange at the zinc center via deprotonation of the alpha-hydroxy group of the thioester to give an equilibrium amount of a zinc alkoxide species
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 55
-
25°C: about 60% of maximal activity, 55°C: about 70% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
calculated
6
calculated from protein sequence
7.25
calculated, N-terminally truncated active form
8.08
calculated from sequence
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
culture-adapted bloodstream and procyclic Trypanosoma brucei of cell line 449, descendants of the strain Lister 427, stably transfected with pHD449 encoding the tetracycline repressor
Manually annotated by BRENDA team
-
human breast cancer cell, estrogen-receptor negative
Manually annotated by BRENDA team
for RNA interference experiments a cell line (427 1313 514) is employed that encodes a second tetracycline repressor and constitutively expresses a T7-polymerase
Manually annotated by BRENDA team
-
fibroadenoma mammae cells
Manually annotated by BRENDA team
-
activity decreases after a two-week exposure to a sublethal concentration (1.6 mM) of Cu2+ compared to untreated control specimens in marine water
Manually annotated by BRENDA team
-
activity is unchanged after a two-week exposure to a sublethal concentration (1.6 mM) of Cu2+ compared to untreated control specimens in marine water
Manually annotated by BRENDA team
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glioblastoma multiform cells
Manually annotated by BRENDA team
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transcription of glyoxalase II is about threefold increased in cancerous tissue comared to noncancerous tissue. Glyoxalase II activity is significantly lower in pathological tissues than in normal ones
Manually annotated by BRENDA team
in the lung of diabetic rats, the increase in GLO I activity is not associated to a concomitant increase in GLO II activity. This finding could result in a defective methylglyoxal detoxification
Manually annotated by BRENDA team
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increase of enzyme activity upon starvation, and decrease of level of D-lactate and related metabolites
Manually annotated by BRENDA team
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human breast cancer cell, estrogen-receptor positive
Manually annotated by BRENDA team
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outer green rind
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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increase of enzyme activity upon starvation, and decrease of level of D-lactate and related metabolites
Manually annotated by BRENDA team