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Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase and Organism(s) Escherichia coli and UniProt Accession P0AC84

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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:
Escherichia coli
UNIPROT: P0AC84
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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
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Germ cell specific protein
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GLO II
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glyoxalase II
hydrolase, acetoacetylglutathione
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hydrolase, hydroxyacylglutathione
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hydroxyacylglutathione hydrolase
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Round spermatid protein RSP29
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S-2-hydroxylacylglutathione hydrolase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
S-(2-hydroxyacyl)glutathione hydrolase
Also hydrolyses S-acetoacetylglutathione, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-90-5
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9025-92-7
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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-lactate + glutathione
show the reaction diagram
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-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
-
second step in the glyoxalase system, detoxification of methylglyoxal
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-
?
additional information
?
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the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
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?
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
D-lactate + glutathione
show the reaction diagram
-
second step in the glyoxalase system, detoxification of methylglyoxal
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-
?
additional information
?
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the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
binuclear zinc-dependent metalloenzyme
Co2+
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glxII apoenzyme activity is regained
Mn2+
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glxII apoenzyme activity is regained
Ni2+
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no activity of glxII, re-addition of Zn2+ results in a further inhibition of the residual enzyme activity of the incompletely demetalled apo-GlxII
Zn2+
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glxII is a binuclear metalloenzyme with Zn2+ as the probable active site metal ion, glxII is isolated with approximately two mol of Zn2+ bound per mole of glxII
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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a DELTAgloB mutant is as tolerant of methylglyoxal as the parent, despite having the same degree of inhibition of MG detoxification as a DELTAgloA strain. The DgloB mutant grows at a similar rate to the parent in K0.2 minimal medium and exhibits no obvious growth phenotype. Addition of 0.7 mM MG to both parent andmutant strains, in early exponential phase, causes immediate growth inhibition without recovery over the course of the experiment. Mehtylglyoxal disappeares from the medium in a linear fashion and the rate is greatly reduced in DELTAgloB cultures. Increased expression of GlxII from a multicopyplasmid sensitizes Escherichia coli to methylglyoxal. S-lactoylglutathione pools, KefGB potassium efflux system activity and cytoplasmic pH are linked and very sensitive to changes in the activity of GlxI and GlxII
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Manually annotated by BRENDA team
OYoung, J.; Sukdeo, N.; Honek, J.F.
Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme
Arch. Biochem. Biophys.
459
20-26
2007
Escherichia coli (P0AC84), Escherichia coli
Manually annotated by BRENDA team
Sukdeo, N.; Honek, J.F.
Microbial glyoxalase enzymes: metalloenzymes controlling cellular levels of methylglyoxal
Drug Metabol. Drug Interact.
23
29-50
2008
Arabidopsis thaliana, Escherichia coli
Manually annotated by BRENDA team
Ozyamak, E.; Black, S.S.; Walker, C.A.; Maclean, M.J.; Bartlett, W.; Miller, S.; Booth, I.R.
The critical role of S-lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli
Mol. Microbiol.
78
1577-1590
2010
Escherichia coli
Manually annotated by BRENDA team