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Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q12320

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.6 hydroxyacylglutathione hydrolase
IUBMB Comments
Also hydrolyses S-acetoacetylglutathione, but more slowly.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q12320
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetoacetylglutathione hydrolase
Germ cell specific protein
GLO II
glyoxalase II
glyoxylase II
-
-
hydrolase, acetoacetylglutathione
hydrolase, hydroxyacylglutathione
Round spermatid protein RSP29
S-2-hydroxylacylglutathione hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
show the reaction diagram
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-D-lactoylglutathione + H2O
D-lactic acid + glutathione
show the reaction diagram
-
-
-
?
S-D-mandeloylglutathione + H2O
? + glutathione
show the reaction diagram
-
-
-
?
lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
-
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
-
-
-
?
S-D-lactoylglutathione + H2O
glutathione + D-lactate
show the reaction diagram
S-D-mandeloylglutathione + H2O
D-mandelate + glutathione
show the reaction diagram
S-mandeloylglutathione + H2O
mandelate + glutathione
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-D-lactoylglutathione + H2O
glutathione + D-lactate
show the reaction diagram
-
enzyme is involved in the detoxification of methylglyoxal
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
-
1.25 mM, 60% inhibition
glutathione
Hg2+
-
HgCl2, 0.5 mM, complete inhibition
PCMB
-
0.3 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0722
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
0.0365
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
0.112
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
0.32
S-D-lactoylgutathione
-
pH 6.5, 30°C, substrate concentration 1.5-3 mM
0.0166
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
0.0007
S-Lactoylglutathione
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
723
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
25.8
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
605 - 979
S-D-lactoylglutathione
25.8 - 38.1
S-D-mandeloylglutathione
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10000
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
710
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
8700
S-D-lactoylglutathione
pH not specified in the publication, temperature not specified in the publication
2200
S-D-mandeloylglutathione
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
mitochondrial enzyme
7 - 8
-
cytoplasmic enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
-
gel filtration
31153
-
x * 31153, recombinant enzyme from mitochondria, GLO2, MALDI-TOF
31321
-
x * 31321, recombinant enzyme from cytosol, GLO2, MALDI-TOF
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
stable in 0.001 N HCl at 40°C for 15 min
134174
9
-
rapid loss of activity above
134174
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
pH 7.0, 14 min, 50% loss of activity
50
-
pH 7.0, 2 min, 50% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
cytoplasmic gene GLO2 and mitochondrial gene GLO4, expression in Escherichia coli
-
expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expressed only in glycerol medium
Expression occurs both in glucose and in glycerol media
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murata, K.; Inoue, Y.; Watanabe, K.; Fukuda, Y.; Saikusa, T.; Shimosaka, M.; Kimura, A.
Metabolism of alpha-ketoaldehydes in yeast: purification and characterization of glyoxalase II from Saccharomyces cerevisiae
Agric. Biol. Chem.
50
135-142
1986
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Bito, A.; Haider, M.; Briza, P.; Strasser, P.; Breitenbach, M.
Heterologous expression, purification, and kinetic comparison of the cytoplasmic and mitochondrial glyoxalase II enzymes, Glo2p and Glo4p, from Saccharomyces cerevisiae
Protein Expr. Purif.
17
456-464
1999
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Martins, A.M.; Mendes, P.; Cordeiro, C.; Freire, A.P.
In situ kinetic analysis of glyoxalase I and glyoxalase II in Saccharomyces cerevisiae
Eur. J. Biochem.
268
3930-3936
2001
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Inoue, Y.; Maeta, K.; Nomura, W.
Glyoxalase system in yeasts: structure, function, and physiology
Semin. Cell Dev. Biol.
22
278-284
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q12320)
Manually annotated by BRENDA team