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Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase and Organism(s) Rattus norvegicus and UniProt Accession O35952
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3.1.2.6 hydroxyacylglutathione hydrolaseIUBMB Comments
Also hydrolyses S-acetoacetylglutathione, but more slowly.
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Word Map
- 3.1.2.6
- methylglyoxal
- gsh
- s-d-lactoylglutathione
-
glyoxalases
- d-lactate
-
glycation
-
glutathione-dependent
- dehydroascorbate
- monodehydroascorbate
- hemithioacetal
-
d-lactic
- mdhar
-
dicarbonyls
- trypanothione
- 2-oxoaldehydes
-
4.4.1.5
- lactoylglutathione
- metallo-beta-lactamase
- drug development
- biotechnology
- pharmacology
- medicine
- agriculture
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glyoxalase ii, glyoxalase 2, gly ii, glyii, glxii, glx2-2, gloii, hydroxyacylglutathione hydrolase, cgloii, glo ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetoacetylglutathione hydrolase
-
-
-
-
Germ cell specific protein
-
-
-
-
GLO II
-
-
-
-
glyoxalase II
hydrolase, acetoacetylglutathione
-
-
-
-
hydrolase, hydroxyacylglutathione
-
-
-
-
Round spermatid protein RSP29
-
-
-
-
S-2-hydroxylacylglutathione hydrolase
-
-
-
-
glyoxalase II
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-(2-hydroxyacyl)glutathione hydrolase
Also hydrolyses S-acetoacetylglutathione, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY
9025-90-5
-
9025-92-7
-
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
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione + H2O
beta-ethoxy-alpha-D-hydroxybutyrate + glutathione
-
-
-
-
?
S-acetoacetylglutathione + H2O
acetoacetate + glutathione
-
-
-
-
?
S-acetylglutathione + H2O
acetate + glutathione
-
-
-
-
?
S-propionylglutathione + H2O
propionate + glutathione
-
-
-
-
?
S-succinylglutathione + H2O
succinate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
-
reaction is rate-limiting, methylglyoxal bypass of glycolysis
-
-
r
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
lactoylglutathione + H2O
D-lactate + glutathione
-
reaction is rate-limiting, methylglyoxal bypass of glycolysis
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,6-Trinitrobenzenesulfonate
-
N-acetyl-S-(p-bromobenzyl)glutathione protects
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
-
mitochondrial enzyme
0.703
S-(beta-ethoxy-alpha-D-hydroxybutyryl)glutathione
-
mitochondrial enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover-numver is pH-independent in the range pH 6-9.3
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity is determined spectrophotometrically at 240 nm, the hepatic glyoxalase II activity of the 3'-methyl-4-dimethylaminoazobenzene group (10 weeks fed) is almost the same as that of the control group
additional information
-
determined spectrophotometrically at 240 nm, glyoxalase II activities of 2-methyl-4-dimethylaminoazobenzene-fed rats (10 weeks fed) are 1.3 times higher than that of the control rats
additional information
-
determined spectrophotometrically at 240 nm, glyoxalase II activities of 4'-methyl-4-dimethylaminoazobenzene-fed rats (10 weeks fed) are 1.4 times higher than that of the control rats
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
10-15% of the total glyoxalase II activity in liver. 56% of the activity resides in the matrix, 19% in the intermembrane space. 3 isoforms are exclusively mitochondrial
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLO2_RAT
309
0
34109
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
21900
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
vander Jagt, D.L.
The glyoxalase system
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
597-641
1989
Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
-
Van der Jagt, D.L.
Glyoxalase II: molecular characteristics, kinetic and mechanism
Biochem. Soc. Trans.
21
522-527
1993
Homo sapiens, Rattus norvegicus
Ball, J.C.; vander Jagt, D.L.
Purification of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from rat erythrocytes
Anal. Biochem.
98
472-477
1979
Rattus norvegicus
Ball, J.C.; vander Jagt, D.L.
S-2-Hydroxyacylglutathione hydrolase (glyoxalase II): active-site mapping of a nonserine thiolesterase
Biochemistry
20
899-905
1981
Rattus norvegicus
Principato, G.B.; Rosi, G.; Talesa, V.; Giovannini, E.; Uotila, L.
Purification and characterization of two forms of glyoxalase II from the liver and brain of Wistar rats
Biochim. Biophys. Acta
911
349-355
1987
Rattus norvegicus, Rattus norvegicus Wistar
Talesa, V.; Uotila, L.; Koivusalo, M.; Principato, G.; Giovannini, E.; Rosi, G.
Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms
Biochim. Biophys. Acta
955
103-110
1988
Rattus norvegicus
Uotila, L.
Glutathione thiol esterases
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
767-804
1989
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus
-
Talesa, V.; Uotila, L.; Koivusalo, M.; Principato, G.; Giovannini, E.; Rosi, G.
Isolation of glyoxalase II from two different compartments of rat liver mitochondria. Kinetic and immunochemical characterization of the enzymes
Biochim. Biophys. Acta
993
7-11
1989
Rattus norvegicus
Cho, M.Y.; Bae, C.D.; Park, J.B.; Lee, T.H.
Purification and cloning of glyoxalase II from rat liver
Exp. Mol. Med.
30
53-57
1998
Rattus norvegicus
Bonfigli, A.; Colafarina, S.; Falone, S.; Di Giulio, C.; Di Ilio, C.; Amicarelli, F.
High levels of antioxidant enzymatic defence assure good protection against hypoxic stress in spontaneously diabetic rats
Int. J. Biochem. Cell Biol.
38
2196-2208
2006
Rattus norvegicus (O35952)
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