Information on EC 4.4.1.5 - lactoylglutathione lyase

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

EC NUMBER
COMMENTARY
4.4.1.5
-
RECOMMENDED NAME
GeneOntology No.
lactoylglutathione lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(R)-S-lactoylglutathione = glutathione + methylglyoxal
show the reaction diagram
intramolecular hydride migration is the rate-determining step
-
(R)-S-lactoylglutathione = glutathione + methylglyoxal
show the reaction diagram
there is a single site for the binding of the hemimercaptal of methylglyoxal and glutathione, for the binding of glutathione, and for the binding of S-substituted derivatives of glutathione. One-substrate reaction mechanism with hemimercaptal being the substrate, but does not rule out the possibility of the alternate branches
-
(R)-S-lactoylglutathione = glutathione + methylglyoxal
show the reaction diagram
-
-
-
-
(R)-S-lactoylglutathione = glutathione + methylglyoxal
show the reaction diagram
investigation of the biological role of GLO I in renal hypoxic diseases by using the rat ischemia/reperfusion (I/R) injury model. I/R induces the reduction of renal GLO I activity associated with morphological changes and renal dysfunction
-
(R)-S-lactoylglutathione = glutathione + methylglyoxal
show the reaction diagram
methylglyoxal and glutathione form an intermediate, the hemithioacetal, which is catalyzed to S-D-lactoylglutathione by GlxI. Subsequently S-D-lactoylglutathione is hydrolyzed to D-lactate and glutathione by GlxII (EC 3.1.2.6)
-
(R)-S-lactoylglutathione = glutathione + methylglyoxal
show the reaction diagram
comparative study of methylgloxal metabolism in trypanosomatids: Trypanosoma brucei, Trypanosoma cruzi und Leishmania major. Trypanosoma brucei lacks GLO1 activity. Overexpression of GLO1 from Trypanosoma cruzi in Trypanosoma brucei results in restoration of the glyoxalase system resulting in an increased resistance to methylglyoxal and increased conversion of methylglyoxal to D-lactate, demonstratong that glyoxalase II (GLO2, EC 3.1.2.6) is functional in vivo
-
(R)-S-lactoylglutathione = glutathione + methylglyoxal
show the reaction diagram
comparative study of methylgloxal metabolism in trypanosomatids: Trypanosoma brucei, Trypanosoma cruzi und Leishmania major. Trypanosoma brucei lacks GLO1 activity. Overexpression of GLO1 from Trypanosoma cruzi in Trypanosoma brucei results in restoration of the glyoxalase system resulting in an increased resistance to methylglyoxal and increased conversion of methylglyoxal to D-lactate, demonstratong that glyoxalase II (GLO2, EC 3.1.2.6) is functional in vivo
Leishmania major Friedlin
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
addition
-
-
addition
P0A0T3
-
addition
Q9HU72, Q9HY85, Q9I5L8
-
addition
Q88GF8
-
addition
-
-
addition
-
gly I
addition
-
-
of RSH
-
isomerization
-
-
PATHWAY
KEGG Link
MetaCyc Link
methylglyoxal degradation I
-
Pyruvate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
(R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing; glutathione-forming)
Also acts on 3-phosphoglycerol-glutathione.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldoketomutase
-
-
-
-
Glb33
Q76E52
-
GLO I
-
-
Glo1
Q2PYM9
-
Glo1
Q68RJ8
-
Glo1
Leishmania major Friedlin
-
-
-
Glo1
Saccharomyces cerevisiae YPH250
-
-
-
Glo1
Schizosaccharomyces pombe PR 109
-
-
-
GloA1
-
-
-
GloA3
-, Q9HU72
-
GloI
Q5XQR1
-
Glx I
-
-
Glx-I
-
-
GLXI
-
-
-
-
GLXI
-
-
GLXI
Q04760
-
GLXI
Q9HU72, Q9HY85, Q9I5L8
-
GLXI
-, Q88GF8
-
glyoalase I
-
-
glyoxalase 1
-
-
glyoxalase I
-
-
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
Aloe vera, Amaranthus sp.
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
-
gene gly I
glyoxalase I
O04885
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
P0AC81
-
glyoxalase I
-
-
glyoxalase I
Q9ZS21
-
glyoxalase I
Q04760
-
glyoxalase I
Q9CJC0
-
glyoxalase I
Lactococcus lactis IL1404
Q9CJC0
-
-
glyoxalase I
-
-
glyoxalase I
Q2PYM9
-
glyoxalase I
-
-
glyoxalase I
Leishmania major Friedlin
-
-
-
glyoxalase I
-
-
glyoxalase I
P0A0T3
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
Q71KM3
-
glyoxalase I
Q9HU72, Q9HY85, Q9I5L8
-
glyoxalase I
-
-
glyoxalase I
Q88GF8
-
glyoxalase I
-
-
glyoxalase I
Saccharomyces cerevisiae YPH250
-
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase-1
-
-
glyoxalase-1
-
-
glyoxalase-1
-
-
glyoxalase-I
-
-
glyoxylase I
-
-
-
-
glyoxylase I
-
-
GmGlyox I
Q9ZS21
-
ketone-aldehyde mutase
-
-
-
-
lactoylglutathione lyase
-
-
lactoylglutathione methylglyoxal lyase
-
-
lyase, lactoylglutathione
-
-
-
-
methylglyoxalase
-
-
-
-
methylglyoxylase
-
-
-
-
PfGlx I
Q71KM3
-
rhGLO I
-
His-tagged GLO I protein
S-D-lactoylglutathione methylglyoxal lyase
-
-
-
-
S-D-lactoylglutathione:methylglyoxal lyase
-
-
S-D-lactoylglutathione:methylglyoxal lyase
-
-
YaiA
Q9CJC0
-
YaiA
Lactococcus lactis IL1404
Q9CJC0
-
-
CAS REGISTRY NUMBER
COMMENTARY
9033-12-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Amaranthus sp.
-
-
-
Manually annotated by BRENDA team
gene gly I coding for glyoxalase I transformed into Vigna mungo L. Hepper using Agrobacterium tumefaciens, controlled by a novel constitutive Cestrum yellow leaf curling viral promotor
-
-
Manually annotated by BRENDA team
glyoxalase I expression is induced during salt stress
SwissProt
Manually annotated by BRENDA team
no isoenzymes
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 5177D mt-
5177D mt-
-
-
Manually annotated by BRENDA team
immature specimen
-
-
Manually annotated by BRENDA team
MG1655/pGL10
UniProt
Manually annotated by BRENDA team
Escherichia coli MG1655/pGL10
MG1655/pGL10
UniProt
Manually annotated by BRENDA team
soybean
SwissProt
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
3 isoenzymes
-
-
Manually annotated by BRENDA team
caucasians
-
-
Manually annotated by BRENDA team
expressed in bovine aortic endothelial cells
-
-
Manually annotated by BRENDA team
isoform glyoxalase I
-
-
Manually annotated by BRENDA team
two isoforms of glyoxalase I showing different electrophoretic properties result from a change in one amino acid residue at psotion 11 (Ala/Gln)
-
-
Manually annotated by BRENDA team
Lactococcus lactis IL1404
IL1404
UniProt
Manually annotated by BRENDA team
recombinant enzyme
SwissProt
Manually annotated by BRENDA team
Friedlin A1 clone
SwissProt
Manually annotated by BRENDA team
Balb/c mice, C57BL6/J female mice
-
-
Manually annotated by BRENDA team
male Balb/cA, 3-4 week old
-
-
Manually annotated by BRENDA team
no activity in Trypanosoma brucei
overexpression of glyoxalase I from Trypanosomas cruzi exhibits enzyme activity in Trypanosomas brucei. The wild-type Trypansoma brucei lacks the GLO1 activity. No apparent GLO1 gene can be identified in the genome
-
-
Manually annotated by BRENDA team
causative agent of onchocerciasis, GloI expression is induced by oxidative stress
-
-
Manually annotated by BRENDA team
cultivar Pokkali
-
-
Manually annotated by BRENDA team
L. Japonica
SwissProt
Manually annotated by BRENDA team
Phaeosphaeria nodorum
strain SN15
SwissProt
Manually annotated by BRENDA team
strain SN15
SwissProt
Manually annotated by BRENDA team
active cytosolic glyoxalase 1, inactive glyoxalase 1-like protein
-
-
Manually annotated by BRENDA team
crayfish, adult, female and male
-
-
Manually annotated by BRENDA team
gloA2; PAO1
UniProt
Manually annotated by BRENDA team
(SPF/VAF)-strain albino rats
-
-
Manually annotated by BRENDA team
male albino rats
-
-
Manually annotated by BRENDA team
permeabilized with 0.01% (w/v) digitonin
-
-
Manually annotated by BRENDA team
strain YPH250
-
-
Manually annotated by BRENDA team
strains BY4741, null mutant DELTAglo1, and overexpressed strain YEpGLO1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae DKD-5D-H
DKD-5D-H
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae YPH250
strain YPH250
-
-
Manually annotated by BRENDA team
strains Pr109, JM544 and KS1366
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe PR 109
PR 109
-
-
Manually annotated by BRENDA team
strain UA159
-
-
Manually annotated by BRENDA team
cultivar Sumai 3
-
-
Manually annotated by BRENDA team
wheat bran
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
nondiabetic GLO1-knockdown mice demonstrate increased 20S methylglyoxal modification resulting in impaired proteasomal activity
malfunction
-
GLO I heterozygous mutants exhibit reduced methylglyoxal detoxification
physiological function
-
glyoxalase I has renoprotective effects in renal hypoxia such as ischemia/reperfusion injury via a reduction in cytotoxic methylglyoxal level in tubular cell
physiological function
-
GLOI plays an important role in the plant abiotic stress response
physiological function
-
Gly-I plays a key role in cellular detoxification
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
-
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
-
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
-
-
-
-
r
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
-
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
Phaeosphaeria nodorum
-, Q696X2
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
-, Q68RJ8
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
show the reaction diagram
Q696X2
-
-
-
?
gamma-glutamylcysteine-methylglyoxal hemithioacetal
?
show the reaction diagram
Q9ZS21
gamma-glutamylcysteine-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
gamma-glutamylcysteine-phenylglyoxal hemithioacetal
?
show the reaction diagram
Q9ZS21
gamma-glutamylcysteine-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione + 2,4-dimethylphenylglyoxal
S-(2,4-dimethyl)mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
show the reaction diagram
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
show the reaction diagram
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
show the reaction diagram
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
show the reaction diagram
-
no activity
-
-
-
glutathione + 4,5-dioxovalerate
?
show the reaction diagram
Chlamydomonas reinhardtii 5177D mt-
-
-
-
-
?
glutathione + bromophenylglyoxal
?
show the reaction diagram
-
-
-
-
?
glutathione + glyoxal
S-glycolylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + glyoxal
S-glycolylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + glyoxal
S-glycolylglutathione
show the reaction diagram
Chlamydomonas reinhardtii 5177D mt-
-
-
-
-
?
glutathione + hydroxypyruvaldehyde
?
show the reaction diagram
-
-
-
-
?
glutathione + kethoxal
?
show the reaction diagram
-
-
-
-
?
glutathione + kethoxal
?
show the reaction diagram
-
-
-
-
?
glutathione + m-methoxyphenylglyoxal
S-(3-methoxy)mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
the hemimercaptal adduct produced nonenzymatically from methylglyoxal and glutathione is the substrate
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
most active with methylglyoxal
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
stereospecifically transfers hydrogen to form S-D-lactoylglutathione from methylglyoxal and glutathione
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
P0AC81
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
Saccharomyces cerevisiae DKD-5D-H
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
show the reaction diagram
Chlamydomonas reinhardtii 5177D mt-
-
most active with methylglyoxal
-
-
-
glutathione + methylglyoxal
?
show the reaction diagram
-
detoxification of methylglyoxal
-
-
-
glutathione + methylglyoxal
?
show the reaction diagram
Saccharomyces cerevisiae DKD-5D-H
-
detoxification of methylglyoxal
-
-
-
glutathione + methylglyoxal
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
show the reaction diagram
Schizosaccharomyces pombe PR 109
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
Q9HU72
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-, Q68RJ8
very poor substrate, specificity constant 280fold lower than of the N1-glutathionylspermidine
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
show the reaction diagram
-
-
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
show the reaction diagram
-
glutathione reacts with methylglyoxal forming a hemithioacetal, and then glyoxlase I catalyses the formation of S-D-lactoylglutathione
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
show the reaction diagram
-
methylglyoxal is a highly reactive carbonyl compound generated by carbohydrate oxidation and glycolysis, is a major precursor of protein glycation and induces cytotoxicitay leading to apoptosis
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
show the reaction diagram
-
methylglyoxal is a reactive dicarbonyl compound mainly produced by metabolic pathways such as glycolysis, binds to proteins or nucelic acids and forms advanced glycation end products
-
-
?
glutathione + methylphenylglyoxal
?
show the reaction diagram
-
-
-
-
?
glutathione + p-chlorophenylglyoxal
S-(4-chloro)mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + p-chlorophenylglyoxal
S-(4-chloro)mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + p-hydroxyphenylglyoxal
S-(4-hydroxy)mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + p-methoxyphenylglyoxal
S-(4-methoxy)mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + p-phenylphenylglyoxal
?
show the reaction diagram
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
-
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
no activity
-
-
-
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
-
no activity detectable
-
-
-
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
Schizosaccharomyces pombe PR 109
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
show the reaction diagram
Chlamydomonas reinhardtii 5177D mt-
-
no activity detectable
-
-
-
glutathione + phenylglyoxal
S-mandoylglutathione
show the reaction diagram
-
-
-
-
?
glutathione-glyoxal hemithioacetal
?
show the reaction diagram
-, Q71KM3
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
Q04760
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
Q9XGF2, -
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
Q9ZS21
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
O04885
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
O04885
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-, Q76E52
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-, Q71KM3
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, Gly-I may play a critical detoxifying role in glycolysis to maintain cellular activity and viability of prostatic cancer cells
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, operates in conjunction with glyoxalase II to convert cytotoxic methylglyoxal to nontoxic D-lactate
-
?
glutathione-phenylglyoxal hemithioacetal
?
show the reaction diagram
Q9ZS21
glutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-phenylglyoxal hemithioacetal
?
show the reaction diagram
-
glutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from phenylglyoxal and glutathione
-
?
glutathionylspermidine + methylglyoxal
?
show the reaction diagram
-
-
-
-
-
glutathionylspermidine + methylglyoxal
?
show the reaction diagram
-
most efficient substrate
-
-
?
glutathionylspermidine + phenylglyoxal
?
show the reaction diagram
-
-
-
-
?
hemithioacetal + glutathione
(S)-D-lactoylglutathione
show the reaction diagram
-
-
-
-
?
hemithioacetal + reduced trypanothione
(S)-D-lactoyltrypanothione
show the reaction diagram
-, Q2PYM9
-
-
-
?
homoglutathione-methylglyoxal hemithioacetal
(R)-S-lactoylhomoglutathione
show the reaction diagram
Q9ZS21
homoglutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
homoglutathione-phenylglyoxal hemithioacetal
?
show the reaction diagram
Q9ZS21
homoglutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
P0A0T3
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-, Q9HU72, Q9HY85, Q9I5L8
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
Q88GF8
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
Saccharomyces cerevisiae YPH250
-
-
-
-
?
methylglyoxal + glutathione
(R)S-lactoylglutathione
show the reaction diagram
Amaranthus sp.
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
-
determined monitoring the increase in absorbance at 240 nm for 5 min at 25C, pH 7.0
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
-
product measured by monitoring the increase of absorbance at 240 nm by formation of S-D-lactoylglutathione, pH 6.6, 37C
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
glyoxalase I is a member of the metallogltathione transferase superfamily and plays a critical role in detoxification of the cytotoxic methylglyoxal to S-D-lactoylglutathione via 1,2-hydrogen transfer
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
liver homogenate, the effects of taurine, ethanol, and iron alone or in combination are analyzed, pH 7.0, 37C
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
P0AC81
methylglyoxal and glutathione form an intermediate, the hemithioacetal, which is catalyzed to S-D-lactoylglutathione by GlxI. Subsequently S-D-lactoylglutathione is hydrolyzed to D-lactate and glutathione by GlxII (EC 3.1.2.6)
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
non-enzymatic formation of hemithioacetal from methylglyoxal and reduced glutathione
enzyme activity is measured spectrophotometrically as a function of thioester formation, S-((R)-lactoyl)glutathione, by measuring the rate of change of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
non-enzymatic formation of hemithioacteal as substrate for gly I
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
non-enzymatic formation of hemithioacteal as substrate for gly I. The active site of gly I has binding affinity for zinc ion and hemithioacetal, and his His residue might be important for its catalytic activity
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
permeabilized cell suspensions, 30C, pH 7.1
formation is monitored by measuring the increase at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
the hemiacetal of methylglyoxal + glutathione is used as substrate, 25C
the formation is measured by monitoring the increase of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
the hemiacetal of methylglyoxal + glutathione is used as substrate, pH 6.8, 20C
the product formation is measured by monitoring the increase of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
the hemiacetal of methylglyoxal + glutathione is used as substrate, pH 7.0, 30C
the formation is measured by monitoring the increase of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
N1-glutathionylspermidine + methylglyoxal
?
show the reaction diagram
-, Q68RJ8
-
-
-
?
N1-glutathionylspermidine + methylglyoxal
?
show the reaction diagram
-
specificity constant of N1-glutathionylspermidine 50fold less than of glutathione
-
-
?
S-D-lactoyltrypanothione
methylglyoxal + reduced trypanothione
show the reaction diagram
-, Q68RJ8
-
-
-
?
S-mandoylglutathione
glutathione + phenylglyoxal
show the reaction diagram
-, Q68RJ8
-
-
-
?
S-mandoyltrypanothione
phenylglyoxal + trypanothione
show the reaction diagram
-, Q68RJ8
-
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-
-
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-
-
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-, Q68RJ8
-
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-, Q5XQR1
-
-
-
r
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-
cell lysate of the recombinant protein, esxpression of GLO1 from Trypanosomas cruzi in Trypanosomas brucei which lacks GLO1 activity, pH 7.0, 25C
the product formation is measured by monitoring at 240 nm
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
Leishmania major, Leishmania major Friedlin
-
cell lysate, pH 7.0, 25C
the formation is measured by monitoring at 240 nm
-
?
trypanothione + phenylglyoxal
S-mandoyltrypanothione
show the reaction diagram
-
-
-
-
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
show the reaction diagram
-
two major intracelluar thiols are used, glutathione and trypanothione, preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
-
-
?
additional information
?
-
P0AC81
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
-
additional information
?
-
-
the enzyme is associated with cell proliferation, the activity is modulated during the proliferation cycle with a maximal activity between day 2 and day 4 of culture growth
-
-
-
additional information
?
-
-
overexpression of the enzyme completely prevents both hyperglycemia-induced advanced glycation products from methylglyoxal and increased macromolecular endocytosis
-
-
-
additional information
?
-
-
alpha-ketoaldehydes may be formed in cells during oxidative processes, glyoxalase I is the main enzyme involved in the detoxification pathway for these highly toxic compounds
-
-
-
additional information
?
-
-
may serve to detoxify methylglyoxal produced from triosephosphates. Increased expression of glyoxalase I may be linked to a higher demand for ATP generation and to enhanced glycolysis in salt-stressed plants
-
-
-
additional information
?
-
-
together with the second enzyme of the glyoxalase system, EC3.1.2.6, EC4.4.1.5 may detoxify the electrophilic 2-oxoaldehydes which can be formed in the cell from endogenous precursors
-
-
-
additional information
?
-
-
disinfected water from two drinking water production plants at the river Po in North Italy markedly perturb the crap liver detoxfifying system, in terms of both induction and inhibition of enzyme activities and glutathione content
-
-
-
additional information
?
-
-
GLO1 is required for osteoclastogenesis
-
-
-
additional information
?
-
-
Glo1 is the major cellular enzyme that catalyzes the metabolism of methylglyoxal and thereby protects against dicarbonyl glycation
-
-
-
additional information
?
-
-
glyoxalase I activity is involved in the detoxification of toxic metabolites produced during lipid peroxidation
-
-
-
additional information
?
-
-
glyoxalase I catalyzes the isomerization reaction of thiohemiacetal, which is formed nonenzymatically from methylglyoxal and glutathione
-
-
-
additional information
?
-
-
glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids, major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis, reaction involves abstraction of a proton from carbon 1 and reinsertion of the proton at carbon 2. Proton transfer takes place with limited proton exchange with the surrounding medium, and a hydride transfer is involved. In the absence of substrate or product, the metal is coordinated with 2 water molecules in addition to the side chains of Gln33 and Glu99 in the same subunit and His126 and Glu172 from the neighbouring subunit. During the catalytic process the water molecule are displaced by the incoming substrate. Glu172 serves as the acid-base in the catalytic mechanism.
-
-
-
additional information
?
-
-
study of the pathophysiological role of glyaylase I as an methylglyxal detoxifier in rat ischemia-reperfusion (I/R) injury
-
-
-
additional information
?
-
-
the glyoxalase system detoxifies methylglyoxal and is composed of two enzymes: glyoxylase I (GLO I), which metabolizes methylglyoxal to S-D-lactoylglutathione, and glyoxalase II (GLO II, EC 3.1.2.6) which converts S-D-lactoylglutathione to D-lactate
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
P0A0T3
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-, Q9HU72, Q9HY85, Q9I5L8
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
Q88GF8
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the Leishmania sp. glxI preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
-
-
-
additional information
?
-
-
knockdown of glyoxalase I by SiRNA transfecetion in rat tubulart cells exacerbates cell-death by hyposia-reoxygenation compared to control cells. Glyoxalase I exerts renoprotective effects in renal ischemia-reperfusion (I/R) injury via the reduction in methylglyoxal accumulation in tubluar cells
-
-
-
additional information
?
-
-
the glyoxalase I activity is measured spectrophotometrically by S-D-lactoylglutathione formation at 240 nm
-
-
-
additional information
?
-
-
the glyxalase-1 homologue CeGly is subcloned into a Green Fluorescent Protein (GFP) vector under control of its native promotor. Enzymatic activity of CeGly in cultures of age-synchronized 1-day-old transgenic Caenorhabditis elegans overexpressing CeGly is ca. 200fold higher than in the wild-type strain. Increased enzymatic activity in transgenic animals results in a significant reduction of both methylglyoxal and methylglyoxal-derived arginine- and lysine-derived adducts. Increased glyxalase-1 activity significantly prolongs lifespan. Mean lifespan increases in transgenic animals from 13.3 days to 17.2 days and maximum lifespan from 28 days to 37 days
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutathione + methylglyoxal
?
show the reaction diagram
-
detoxification of methylglyoxal
-
-
-
glutathione + methylglyoxal
?
show the reaction diagram
Saccharomyces cerevisiae DKD-5D-H
-
detoxification of methylglyoxal
-
-
-
glutathione-glyoxal hemithioacetal
?
show the reaction diagram
-, Q71KM3
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
Q04760
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
Q9XGF2, -
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
Q9ZS21
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
O04885
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
O04885
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-, Q76E52
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-, Q71KM3
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, Gly-I may play a critical detoxifying role in glycolysis to maintain cellular activity and viability of prostatic cancer cells
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
show the reaction diagram
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, operates in conjunction with glyoxalase II to convert cytotoxic methylglyoxal to nontoxic D-lactate
-
?
glutathionylspermidine + methylglyoxal
?
show the reaction diagram
-
-
-
-
-
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
P0A0T3
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
-, Q9HU72, Q9HY85, Q9I5L8
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
Q88GF8
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)S-lactoylglutathione
show the reaction diagram
Amaranthus sp.
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
show the reaction diagram
-
glyoxalase I is a member of the metallogltathione transferase superfamily and plays a critical role in detoxification of the cytotoxic methylglyoxal to S-D-lactoylglutathione via 1,2-hydrogen transfer
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
show the reaction diagram
Saccharomyces cerevisiae YPH250
-
-
-
-
?
additional information
?
-
P0AC81
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
-
additional information
?
-
-
the enzyme is associated with cell proliferation, the activity is modulated during the proliferation cycle with a maximal activity between day 2 and day 4 of culture growth
-
-
-
additional information
?
-
-
overexpression of the enzyme completely prevents both hyperglycemia-induced advanced glycation products from methylglyoxal and increased macromolecular endocytosis
-
-
-
additional information
?
-
-
alpha-ketoaldehydes may be formed in cells during oxidative processes, glyoxalase I is the main enzyme involved in the detoxification pathway for these highly toxic compounds
-
-
-
additional information
?
-
-
may serve to detoxify methylglyoxal produced from triosephosphates. Increased expression of glyoxalase I may be linked to a higher demand for ATP generation and to enhanced glycolysis in salt-stressed plants
-
-
-
additional information
?
-
-
together with the second enzyme of the glyoxalase system, EC3.1.2.6, EC4.4.1.5 may detoxify the electrophilic 2-oxoaldehydes which can be formed in the cell from endogenous precursors
-
-
-
additional information
?
-
-
disinfected water from two drinking water production plants at the river Po in North Italy markedly perturb the crap liver detoxfifying system, in terms of both induction and inhibition of enzyme activities and glutathione content
-
-
-
additional information
?
-
-
GLO1 is required for osteoclastogenesis
-
-
-
additional information
?
-
-
Glo1 is the major cellular enzyme that catalyzes the metabolism of methylglyoxal and thereby protects against dicarbonyl glycation
-
-
-
additional information
?
-
-
glyoxalase I activity is involved in the detoxification of toxic metabolites produced during lipid peroxidation
-
-
-
additional information
?
-
-
glyoxalase I catalyzes the isomerization reaction of thiohemiacetal, which is formed nonenzymatically from methylglyoxal and glutathione
-
-
-
additional information
?
-
-
glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids, major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis, reaction involves abstraction of a proton from carbon 1 and reinsertion of the proton at carbon 2. Proton transfer takes place with limited proton exchange with the surrounding medium, and a hydride transfer is involved. In the absence of substrate or product, the metal is coordinated with 2 water molecules in addition to the side chains of Gln33 and Glu99 in the same subunit and His126 and Glu172 from the neighbouring subunit. During the catalytic process the water molecule are displaced by the incoming substrate. Glu172 serves as the acid-base in the catalytic mechanism.
-
-
-
additional information
?
-
-
study of the pathophysiological role of glyaylase I as an methylglyxal detoxifier in rat ischemia-reperfusion (I/R) injury
-
-
-
additional information
?
-
-
the glyoxalase system detoxifies methylglyoxal and is composed of two enzymes: glyoxylase I (GLO I), which metabolizes methylglyoxal to S-D-lactoylglutathione, and glyoxalase II (GLO II, EC 3.1.2.6) which converts S-D-lactoylglutathione to D-lactate
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
P0A0T3
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-, Q9HU72, Q9HY85, Q9I5L8
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
Q88GF8
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
-
additional information
?
-
-
the Leishmania sp. glxI preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1 mM restores 25% of the activity of the apoenzyme
Ca2+
-
restores activity after EDTA treatment
Ca2+
-
activates apoenzyme
Ca2+
-
activates apoenzyme
Ca2+
-
activates apoenzyme
Ca2+
-
activates apoenzyme
Ca2+
-
2.6fold increase of activity in the presence of 0.025 mM Ca2+
Ca2+
-
20mM, 32.8% reactivation of EDTA-treated enzyme
Cd2+
-
6% of activity with Ni2+
Cd2+
-
reduced activity compared to Ni2+
Cd2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Cd2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Cd2+
Q9HU72
reactivates GloA3 by 87% after treatment with dipicolinic acid
Cd2+
-
activation, Km: 0.0089 mM, Vmax: 0.043 mmol/min/mg, kcat: 21 1/s; activation of gly I
Co2+
-
1 mM, increases activity more than 100%. 1 mM restores 80% of the activity of the apoenzyme
Co2+
-
reactivates apoenzyme
Co2+
-
activates
Co2+
-
66% of activity with Zn2+
Co2+
-
31% of activity with Ni2+
Co2+
-
reduced activity compared to Ni2+
Co2+
-
1mM, 78.6% reactivation of EDTA-treated enzyme
Co2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Co2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Co2+
-, Q68RJ8
reactivation of the apoenzyme
Co2+
-
only marginally less effective than nickel
Co2+
Q9HU72
increases GloA2 activity, hyper-reactivates GloA3 by 115% after treatment with dipicolinic acid
Co2+
-
GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies
Co2+
-
activation, Km: 0.012 mM, Vmax: 0.213 mmol/min/mg, kcat: 106 1/s; activation of gly I
Co2+
-
reactivation of apo gly I
Co2+
P0A0T3
activated by Ni2+ and Co2+; activation of gly I
Co2+
-, Q9HU72, Q9HY85, Q9I5L8
activation of gloA1; activation of gly I; activation of gly I
Co2+
Q88GF8
apo form reactivated; reactivation of apo gly I
Co2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Co2+
-
activated by Ni2+ and Co2+; activation of gly I
CuSO4
-, Q9CJC0
0.2 mM, extracellular, 30fold upregulated protein spot in the 2D-electrophoresis, identified as glyoxalase I, the expression is regulated by the operon yahCD-yaiAB
Fe2+
-
0.5 mM activates 2.4fold
Fe2+
-
activates
Fe2+
-
activates
Fe2+
-
16% of activity with Ni2+
Fe2+
-
at least one iron per enzyme molecule, the second metal is zinc or manganese, apparantly depending on growth conditions
Fe2+
-
1mM, 8.4% reactivation of EDTA-treated enzyme
Fe2+
-
activation, Km: 0.010 mM, Vmax: 0.112 mmol/min/mg, kcat: 56 1/s
Fe3+
-
activation of gly I
methylglyoxal
-
10 mM, enhanced tolerance to toxic stress in transgenic Vigna mungo
Mg2+
-
1 mM restores 60% of the activity of the apoenzyme
Mg2+
-
restores activity after EDTA treatment
Mg2+
-
activates apoenzyme
Mg2+
-
activates apoenzyme
Mg2+
-
activates apoenzyme
Mg2+
-
activates
Mg2+
-
activates apoenzyme
Mg2+
-
potent stimulator, optimal concentration: 16 mM
Mg2+
-
101% of activity with Zn2+
Mg2+
-
required for maximal activity
Mg2+
-
incubation of the Zn2+ depleted apoenzyme with Mg2+ restores 50% of the enzyme activity
Mg2+
-
20mM, 13.7% reactivation of EDTA-treated enzyme
Mg2+
Q9HU72
reactivates GloA3 by 26% after treatment with dipicolinic acid
Mg2+
-
reactivation of gly I
Mg2+
Q88GF8
apo form reactivated; reactivation of gly I
Mn2+
-
1 mM restores 35% of the activity of the apoenzyme
Mn2+
-
activates apoenzyme
Mn2+
-
activates apoenzyme
Mn2+
-
activates apoenzyme
Mn2+
-
activates
Mn2+
-
activates apoenzyme
Mn2+
-
67% of activity with Zn2+
Mn2+
-
18% of activity with Ni2+
Mn2+
-
reduced activity compared to Ni2+
Mn2+
-
can replace Zn2+
Mn2+
-
1mM, 186% reactivation of EDTA-treated enzyme
Mn2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Mn2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Mn2+
-, Q68RJ8
reactivation of the apoenzyme
Mn2+
Q9HU72
hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
NaCl
-
the transgenic and the untransformed plants are exposed to 100 mM NaCl. The transgenic plants survived whereas the untransformed control plants fail to survive
Ni2+
-
activates apoenzyme
Ni2+
-
activates apoenzyme
Ni2+
-
activates
Ni2+
P0AC81
activates
Ni2+
-
required for activity
Ni2+
-
maximal activity in the presence of Ni2+
Ni2+
-, Q71KM3
2.9fold increase in activity at 0.25 mM
Ni2+
-
1mM, 67.9% reactivation of EDTA-treated enzyme
Ni2+
-, Q5XQR1
-
Ni2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Ni2+
-
increased enzyme activity; in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Ni2+
-, Q68RJ8
reactivation of the apoenzyme, largest recovery in activity
Ni2+
-
most effective
Ni2+
Q9HU72
increases GloA2 activity, hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
Ni2+
-, Q68RJ8
-
Ni2+
-
GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies
Ni2+
-
activation of gly I; highest reactivation activity, Km: 0.027 mM, Vmax: 0.676 mmol/min/mg, kcat: 338 1/s
Ni2+
-
reactivation of apo gly I
Ni2+
-
activates
Ni2+
P0A0T3
activated by Ni2+ and Co2+; activation of gly I
Ni2+
-, Q9HU72, Q9HY85, Q9I5L8
activation, Km: 0.021 mM, Vmax: 0.497 mmol/min/mg, kcat: 247 1/s, kcat/Km: 12000000 1/M * s; activation of gloA1; activation of gly I; activation of gly I
Ni2+
Q88GF8
apo form reactivated; reactivation of apo gly I
Ni2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Ni2+
-
activated by Ni2+ and Co2+; activation of gly I
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
metalloenzyme with one Zn2+ per subunit; zinc metalloenzymes
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
metalloenzyme with one Zn2+ per subunit; zinc metalloenzymes
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
apoenzyme is catalytically inactive, but is partially restored by Zn2+; zinc metalloenzymes
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
reactivates apoenzyme
Zn2+
-
activates apoenzyme; contains 1.4 gatom of Zn2+ per mol of enzyme
Zn2+
-
zinc metalloenzymes
Zn2+
Q9ZS21
4fold higher glyoxalase I activity when glyoxalase is isolated from Zn2+-grown bacteria
Zn2+
-
required for activity, no activity with Ni2+, Co2+ and Cd2+
Zn2+
-
required for activity
Zn2+
-
required for activity, 1 Zn2+ per subunit
Zn2+
-, Q71KM3
2.7fold increase in activity at 0.25 mM
Zn2+
-
metal center of the active site zinc complex plays a direct catalytical role by binding the substrate and stabilizing the proposed enediolate reaction intermediate, one Zn2+-ion per active site
Zn2+
-
1 mol Zn2+ per subunit
Zn2+
-
0.5mM, 84.7% reactivation of EDTA-treated enzyme
Zn2+
-
in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Zn2+
-
addition of ZnSO4 during the overexpression results in increased catalytic activity and a decreased Km value
Zn2+
Q9HU72
does not increase GloA2 activity, GloA3 contains Zn2+, reactivates GloA3 by 76% after treatment with dipicolinic acid
Zn2+
-
glyoxalase I is a zinc-binding enzyme that has an outstanding role in the metabolism of the major precursors of advanced glycation end products (AGEs): methylglyoxal and glyoxal
Zn2+
-
two zinc ions per dimer. The zinc is required for structure and function. The monomer contains a single zinc ion
Zn2+
-
essential role in catalytic mechanism
Zn2+
-
activation of glxI
Zn2+
-, Q9HU72, Q9HY85, Q9I5L8
activation of gloA3, metal ion binds tightly to the enzyme so that removal of metall ion requires more forceful conditions; activation, Zn2+ is tightly bound to GloA3, Km: 0.287 mM, Vmax: 1.176 mmol/min/mg, kcat: 787 1/s, kcat/Km: 2800000 1/M * s
Zn2+
Q88GF8
apo form reactivated; reactivation of gly I
Zn2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Zn2+
Aloe vera, Amaranthus sp.
-
binding affinity
Zn2+
-
activates
Mn2+
-
activation, Km: 0.010 mM, Vmax: 0.121 mmol/min/mg, kcat: 60 1/s; activation of gly I
additional information
-
divalent cation required
additional information
-
no activity with Zn2+
additional information
-
no activity in the presence of Zn2+
additional information
-
Mg2+, Ca2+, Zn2+ no increase in enzyme activity
additional information
-, Q68RJ8
no activity with Zn2+
additional information
-
a wide range of bivalent metal ions can substitute for zinc in glyoxalase I from mammalian sources, and several of them afford enzyme activities of similar magnitude to the zinc-containing glyoxalase I
additional information
-
not activated by Zn2+, Zn2+ can bind to the enzyme, but the resulting enzyme is inactive. Mg2+ does not bind to the apoGlxI as determined by isothermal titration calorimetry
additional information
P0A0T3
not activated by Zn2+
additional information
-, Q9HU72, Q9HY85, Q9I5L8
inactive with Zn2+
additional information
-
not activated by Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1E,4Z,6E)-4-(4-hydroxy-3-methoxybenzylidene)-1-(3-hydroxy-4-methoxyphenyl)-7-(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(3-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(4-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(2S)-2-amino-3-[([(2R)-3-[(4-bromobenzyl)sulfanyl]-1-[(carboxymethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoic acid
-
-
(3Z)-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid
-
inhibitor based on binding mode of myricetin, contributuion of the Zn2+-chelating group to inhibitory activity
(S)-4-bromobenzyl glutathione
-
potent Glx-I inhibitor
(S)-4-bromobenzylglutathione cyclopentyl diester
-
competitive inhibitor of GLOI
(Z)-1-[N-(2-aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolate
-
decreases glyoxalase I expression and activity relative to untreated control cells, cells undergo apoptosis, apoptosis increases further on co-incubation with high glucose
1,10-phenanthroline
-
-
1,10-phenanthroline
-
reactivation by Mg2+, Mn2+ or Ca2+
1,10-phenanthroline
-
2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
1,10-phenanthroline
Q9HU72
decreases GloA3 activity
1-chloro-2,4-dinitrobenzene
-
not reduced by dithiothreitol
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
10 mM, 65% inhibition
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
1-Naphthaleneacetic acid
-
activity decreases by approximately 50% during differentiation in Brassica sp. gly I
2,2'-dipyridyl
-
-
2,3-Butanedione
-
time and concentration dependent inactivation
2,3-Dihydroxybenzoic acid
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2,4,6-trinnitrobenzenesulphonic acid
-
2 mM, 60% inhibition
2,6-pyridindicarboxylic acid
-
2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
2-([(4-methoxyphenyl)carbonyl]amino)-1-benzothiophene-3-carboxylic acid
-
inhibitor based on binding mode of myricetin
2-([(4-methoxyphenyl)carbonyl]amino)benzoic acid
-
inhibitor based on binding mode of myricetin
-
2-aminopyridine
-
-
2-Hydroxy-5-nitrobenzyl bromide
-
-
3-hydroxyflavone
-
-
4-[(4E)-5-(3,4-dimethoxyphenyl)-2-[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]-3-oxopenta-1,4-dien-1-yl]benzene-1,2-dicarbaldehyde
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
adenosine
-
-
amino-group reagents
-
-
-
baicalein
-
79% inhibition of rhGLO I at 0.1 mM
Baicalin
-
30% inhibition of rhGLO I at 0.1 mM
benzimidazole
-
-
Benzyladenine
-
activity decreases by approximately 50% during differentiation in Brassica sp. gly I
bisdemethoxycurcumin
-
-
bisdemethoxycurcumin
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Bisdemethoxycurcumin coordinates with the zinc ion
buthionine sulfoximine
-
58% loss in Gly-I activity by 0.05 mM buthionine sulfoximine
Caffeine
-
-
Chelex-100
-
-
-
ClO2
-
study of the influence of chlorine dicloride during the disinfection process in 2 drinking water production plants at the river Po in North Italy. Measuring of the glyoxalase activity at two experimental times, 3 and 6 days. Plant 1-treated carp shows an increased glyoxalase I activity of about 140%, indicating an induced defense ability. Whereas the plant 2-treated specimens show the depletion of enzyme activity of 50%, indicating a compromised capacity to detoxify the peroxidative products formed during the oxidative process due to the inhibited glyoxalase activity
Co2+
-
apo form reactivated
Colchicine
-
decrease of activity of glyoxalase I
coproporphyrin
-
weak
cromoglycate
-
0.1 mM, 50% inhibition
curcumin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, pH 7.0, 30C, more efficient inhibition of GLO1 compared to quercetin, myricetin, kaempferol, luteolin, or rutin as inhibitor, results in a decrease of D-lactate release
curcumin
-
efficient inhibitor
curcumin
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Curcumin coordinates with the zinc ion
cytidine
-
-
D-glucono-delta-lactone
-
weak
dichlorophen
-
0.048 mM, 50% inhibition
diethyl dicarbonate
-
-
diethyldicarbonate
-
2 mM, complete inhibition
dihydroxyfumaric acid
-
-
dipicolinic acid
Q9HU72
greatest loss of GloA3 activity
dithiothreitol
-
slight
EDTA
-
1 mM
EDTA
-
10 mM, no inhibition
EDTA
-
reactivation by Mg2+, Mn2+ or Ca2+
EDTA
-
0.1 mM, approx. 50% inactivation after 50 min, approx. 80% inhibition after 250 min
fenoprofen
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms
FeSO4
-
2.0 mM, 46.5% inhibition
flavone
-, Q5XQR1
IC50 wild type 56 microM, IC50 enzyme overexpressor 69 microM
formaldehyde
-
-
formononetin 7-O-glucoside
-
0.074 mM, 50% inhibition
gerfelin
-
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30C
glutathione thioethers
-
competitive
glycerol
-
64% loss in Gly-I activity by 2.5% (v/v) glycerol, Gly-I inactivation by glycerol is fully prevented or reversed by 0.5 mM N-acetylcysteine
GSH
-
competitive; non-linear inhibition
guanosine
-
-
H2O2
-
2 mM, 2 h, significantly reduces enzyme activity from 0.2 U/single Caenorhabditis elegans (without addition of H2O2) to 0.065 U/single Caenorhabditis elegans
HgCl2
-
67% loss in Gly-I activity by 0.03 mM HgCl2, Gly-I inactivation by HgCl2 is fully prevented or reversed by 0.5 mM N-acetylcysteine
hyperin
-
below 5% inhibition of rhGLO I at 0.1 mM
I-
-
5 mM, complete inhibition
Indomethacin
-
-
Indomethacin
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Indomethacin coordinates with the zinc ion and is able to occupy all four enzyme subsites, both subsites C and D may be occupied simultaneously
iodoacetamide
-
slight
kaempferol
-
60% inhibition of rhGLO I at 0.1 mM
kaempferol
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30C, results in a decrease of D-lactate release
Ketoprofen
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms
L-gamma-glutamyl-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
-
tight-binding carboanalog of hydroxamate
L-gamma-glutamyl-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
-
hydroxamic acid-based transition state inhibitor, unstable toward gamma-glutamyltranspeptidase
Lapachol
-, Q5XQR1
IC50 wild type 93 microM, IC50 enzyme overexpressor 96 microM
luteolin
-
90% inhibition of rhGLO I at 0.1 mM
luteolin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30C, results in a decrease of D-lactate release
meso-tetrasubstituted porphyrines
-
-
-
methyl gerfelin
-
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30C
methyl gerfelin
-
-
methylglutathione
-, Q71KM3
-
methylglyoxal
-
5 mM, 50% inhibition of activity in cell lines
methylglyoxal
-
addition at pH 7.0 results in a modest 28% decrease in the glycolytic rate
methylglyoxal
-
200 mM, 8 h, significantly reduces enzyme activity from 0.2 U/single Caenorhabditis elegans (without addition of methylglyoxal) to 0.12 U/single Caenorhabditis elegans
MS-3
-
inhibitor produced by a mushroom Stereum hirsutum
MS-3
-
inhibitor produced by a mushroom Stereum hirsutum; mechanism of inhibition
myricetin
-
75% inhibition of rhGLO I at 0.1 mM
myricetin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30C, results in a decrease of D-lactate release
myricetin
-
substrate transition-state (Zn2+-bound methylglyoxal-glutathione hemithioacetal) mimetic inhibitor
N-Acetylimidazole
-
reversed by hydroxylamine
N-bromosuccinimide
-
-
N-bromsuccinimide
-
0.0032 mM, 35% inhibition
N-[(1S,4Z)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohept-4-en-1-yl]-L-glutamine
-
beta-ketoester, competetive inhibitor
N-[(1S,4Z)-6-(4-bromophenyl)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohex-4-en-1-yl]-L-glutamine
-
beta-ketoester, competetive inhibitor
N-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
-
tight-binding competitive inhibitor, stable toward gamma-glutamyltranspeptidase
N2-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
-
tight-binding carboanalog of hydroxamate
Naringenin
-
50% inhibition of rhGLO I at 0.1 mM
NH2-gamma-Gla[-Glu(CON(OH)-4-bromophenyl)Gly-OH]-OH
-
-
NH2-gamma-Glu[-D-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
NH2-gamma-Glu[-Dab(N-(4-bromobenzoyl)-N'-hydroxyl)-Gly-OH]-OH
-
-
NH2-gamma-Glu[-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
Ni2+
-
apo form reactivated
Ni2+
-
activates
NO3-
-
10 mM, 20% decrease of activity
octyl-S-glutathione
-
-
oroxylin A
-
140% inhibition of rhGLO I at 0.1 mM
oxibendazol
-
0.11 mM, 50% inhibition
p-hydroxymercuribenzen sulfonate
-
1 mM, 64% inhibition
-
para-substituted S-benzylglutathione
-
-
Phenylglyoxal
-
-
phosphate
-
750 mM, strain BY4741, about 2fold decrease of glyoxalase I. In the YEpGLO1 strain, glyoxalase is higher than in BY4741, consistant with the overexpression of the glo1 gene. Enzyme inactivation is observed, cells subjected to 750 mM phosphate still show an increase of about 1.7fold relatively to BY4741 glyoxalase I activity
Purpurogallin
-
0.015 mM, 50% inhibition
Purpurogallin
-, Q5XQR1
IC50 wild type 70 microM, IC50 enzyme overexpressor 132 microM
pyridoxal
-
-
pyridoxal 5'-phosphate
-
-
pyridoxamine
-
-
quercetin
-
-
quercetin
-, Q5XQR1
IC50 wild type 26 microM, IC50 enzyme overexpressor 27 microM
quercetin
-
78% inhibition of rhGLO I at 0.1 mM
quercetin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30C, results in a decrease of D-lactate release
rutin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30C, results in a decrease of D-lactate release
S-(1-naphthylmethyl)-glutathione
-
-
S-(2-chlorobenzyl)-glutathione
-
-
S-(2-hydroxybenzyl)-glutathione
-
-
S-(4-bromophenyl)glutathione
-
glyoxalase I
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
IC50 0.06 microM
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
IC50 0.09 microM
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
IC50 0.11 microM
S-(N-hydroxy-N-methylcarbamoyl)glutathione
-
-
S-(N-hydroxy-N-p-bromophenylcarbamoyl)glutathione
-
-
S-(N-hydroxy-N-p-iodophenylcarbamoyl) glutathione
-
tight binding competitive inhibitor of human GLOI
S-(N-hydroxy-N-p-iodophenylcarbamoyl)glutathione
-
-
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
-
IC50 2.5 microM
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
-
IC50 10 microM
S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
-
S-(omega-aminodecyl)glutathione
-
-
S-(p-bromobenzyl)glutathione
-
-
S-(p-bromobenzyl)glutathione
-
-
S-2,4-dinitrophenylglutathione
-
-
S-2,4-dinitrophenylglutathione
Q68RJ8
-
S-2,4-dinitrophenylglutathionylspermidine
-
-
S-2,4-dinitrophenylglutathionylspermidine
Q68RJ8
-
S-4-bromobenzylglutathione
-, Q68RJ8
-
S-4-bromobenzylglutathione
-
-
S-4-bromobenzylglutathione cyclopentyl diester
-
detanonoate, NO donor, competitive inhibitor, concentration-dependent down-regulation of glyoxalase I, increases intracellular methylglyoxal and causes apoptosis, overexpression of glyoxalase I protects against S-4-bromobenzylglutathione cyclopentyl diester-induced apoptosis under high glucose conditions
S-4-bromobenzylglutathionylspermidine
-
potent linear competitive inhibitor, selectively inhibits trypanosomatid GLO1 activity
S-4-bromobenzylglutathionylspermidine
-
linear competitive inhibitor
S-4-bromobenzylglutathionylspermidine
Q68RJ8
linear competitive inhibitor
S-benzoxycarbonylglutathione
-
-
S-benzoxycarbonylglutathione derivatives
-
-
S-benzyl-glutathione
-
-
S-benzylglutathione
-
-
S-bromobenzylglutathione
-
-
S-hexylglutathione
-
competitive
S-hexylglutathione
-
-
S-hexylglutathione
-
0.11 mM, 50% inhibition
S-hexylglutathione
-
-
S-hexylglutathione
-
competitive inhibition
S-hexylglutathione
-
slows degradation of the wild-type enzyme and mutant E161Q/E345Q in comparison with uncomplexed protein
S-nitroso-N-acetyl-D,L-penicillamine
-
released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
S-nitrosocysteine
-
released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
S-nitrosoglutathione
-
glyoxal I activity in cells decreases rapidly within 30 min and reaches 10% of the control level within 2 h, activity returns to approx. 80% and 70% after removal of S-nitrosoglutathione or incubation with dithiothreitol, respectively, released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents
S-nitrosoglutathione
-, Q71KM3
-
S-p-bromobenzyl glutathione
-
competitive inhibitor, unstable toward gamma-glutamyltranspeptidase
S-p-bromobenzylglutathione
-
competitive
S-p-bromobenzylglutathione
-
-
S-p-bromobenzylglutathione
-
55% inhibition of rhGLO I at 0.1 mM
S-p-bromobenzylglutathione cyclopentyl diester
-
GLO1 inhibitor, inhibiting osteoclastogenesis, inhibition kinetics from 0.03 to 3 microM, dose-dependently inhibited, strongest inhibition at 3 microM, pH 7.0, 30C
S-p-nitrobenzoxycarbonylglutathione
-
-
S-p-nitrobenzylglutathione
-
-
S-p-nitrobenzyloxycarbonylglutathione
-
-
S-p-nitrosobenzylglutathione
-, Q71KM3
-
Tetranitromethane
-
-
Tetranitromethane
-
2 mM, 30% inhibition
Theobromine
-
-
theophylline
-
-
Tolmetin
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Tolmetin coordinates with the zinc ion
tryptophan
-
-
vinblastine
-
decrease of activity of glyoxalase I
xanthine
-
-
zinc (2S)-2-amino-3-([(3R)-3-([[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]methyl)-4-[(carboxylatomethyl)amino]-4-oxobutanoyl]amino)propanoate
-
-
zinc (2S)-2-amino-3-[([(2R)-3-[[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]-1-[(carboxylatomethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoate
-
-
Zn2+
-
0.5 mM, complete inhibition
Zn2+
-
0.1 mM, 75% inhibition at 0.1 mM, complete inhibition at 1.0 mM
Zn2+
-
inactivation of gly I, metal can bind to the enzyme gly I, but the resulting enzyme is inactive
Zn2+
-
apo form reactivated
Zn2+
P0A0T3
inactivation of gly I
Zn2+
-, Q9HU72, Q9HY85, Q9I5L8
inactivation of gloA1; inactivation of gly I
Zn2+
-
inactivation of gly I
Zomepirac
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms
Mg2+
-
apo form reactivated
additional information
-
pH-dependence of inhibition by porphyrins
-
additional information
-
substrate-analogue inhibitors and transition-state inhibitors
-
additional information
-, Q68RJ8
not inhibitory: S-methyl-glutathione, S-propyl-glutathione, S-butyl-glutathione, S-hexyl-glutathione, S-octyl-glutathione at 1 mM, S-p-nitrobenzyl-glutathione and S-p-bromobenzyl-glutathione at 250 microM
-
additional information
-
S-4-bromobenzylglutathione is inactive as inhibitor
-
additional information
-
reducing glyoxalase I RNA levels with advancing stage of Alzheimers disease and with increasing age, continuously decrease in middle and late stages of Alzheimers disease, glyoxalase I activity neither significantly changes with age nor with the course of the disease
-
additional information
-
exposure of HPMC cells to heat-sterilized peritoneal dialysis fluids results in reduced GLO-I activity, GSH depletion, and a decrease in cell viability. Pretreatment of heat-sterilized peritoneal dialysis with either a combination of GLO-I and GSH markedly reduces inhibitory effects toward HPMC cells. Exposure of HPMC cells to L-2-oxothiazolidine-carboxylic acid increases cellular GSH and prevents loss of GLO-I activity in response to heat-sterilized peritoneal dialysis
-
additional information
-
monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
-
additional information
-
1.21 mg/kg crayfish, selenium-enriched diet, male crayfish, shows a lowered enzyme activity, 85% inhibited at day 30, 45% inhibited at day 50. A depletion of enzyme activity indicates a compromised detixificant ability against peroxidative metabolites. Since selenium affects only treated males, it seems that males are more susceptible than females
-
additional information
-
inactive with Zn2+
-
additional information
-
no change in glyoxalase I activity in taurine-treated rats
-
additional information
-
methylglyoxal toxicity is evaluated by viability assays using BY4741 and the null mutant DELTAglo1, lacking the glyoxalase I activity. The reference BY4741 strain shows no methylglyxoal toxicity up to 10 mM. In contrast, strains with deficiencies in the glyoxalase system, i.e. DELTAglo1 have decreased viability, progessively more severe with increasing methylglyoxal concentration
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6-benzylaminopurine
-
-
abscisic acid
-
-
ascorbic acid
-
enhances slightly glyoxalase I activity, dose-dependently 0-2 g/l, pH 6.6, 37C
auxin
-
enhances activity of both gly I and II in Glycine max
Calmodulin
-
7.9fold increase of activity in the presence of Ca2+ and Mg2+
D-glucose
-
25 mM upregulates glyoxalase I activity and mRNA in LE cells when compared with either cells cultured with 5 mM glucose as control or with 20 mM L-glucose + 5 mM D-glucose
indole acetic acid
-
stimulation of activity of glyoxalase I
light
Amaranthus sp.
-
red and blue light exposure increases gly I activity in dark-gron Amaranthus sp. indicating expression of enzyme is under stringent regulation by photoreceptors in plants
-
Polyamines
-
activate
-
S-ethyl cysteine
-
enhances significantly glyoxalase I activity, dose-dependently 0-2 g/l, pH 6.6, 37C
S-propyl-cysteine
-
enhances significantly glyoxalase I activity, dose-dependently 0-2 g/l, pH 6.6, 37C
spermidine
-
gly I
methylglyoxal
-
addition at pH 5.0 results in a significant 98% increase in the glycolytic rate
additional information
-
enzyme acitivating in vivo: osmotic stress by sorbitol treatment, 0.9 M, 1 h. No increase in enzyme activity following sorbitol treatment when cycloheximide is present; not activating: incubation of purified enzyme with 0-300 mM glycerol in vitro
-
additional information
-
is up-regulated during acid challenge, is induced during acidic growth 3.5fold and following acid adaptation 2fold, is up-regulated approximately 7fold during the exponential growth phase compared with that in the stationary growth phase
-
additional information
-
glyoxalase I protein amounts are 1.5fold increased in early Alzheimers disease subjects
-
additional information
-
treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
-
additional information
-
1.21 mg/kg crayfish, selenium-enriched diet, female crayfish, results in a tendency to an increased enzyme activity
-
additional information
-
glyoxalase I is highly overexpressed in highly invasive tumors in comparison to tumors with low malignant potential
-
additional information
-
not only light but a number of other exogenous factors, such as hypoxia, temperature shock, and water stress, transduce their signal through Ca2+ that binds specific target proteins, including kinases, which in turn can activate gly I
-
additional information
Amaranthus sp.
-
not only light but a number of other exogenous factors, such as hypoxai, temperature shock, and water stress, transduce their signal through Ca2+ that binds specific target proteins, including kinases, which in turn can activate gly I
-
additional information
-
not only light but a number of other exogenous factors, such as hypoxia, temperature shock, and water stress, transduce their signal through Ca2+ that binds specific target proteins, including kinases, which in turn can activate gly I
-
additional information
-
no change in glyoxalase I activity in taurine-treated rats, 2% (w/v)
-
additional information
P16635
activity of glyoxalase I in transgenic Escherichia coli with Pseudomonas putida glyoxalase I under anaerobic conditions is 12fold higher than that in control cells
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.016
-
(R)-S-lactoylglutathione
-
pH 7.0, 0.5 mM CoCl2
0.028
-
(R)-S-lactoylglutathione
-
pH 7.0, 0.5 mM CoCl2
0.028
-
(R)-S-lactoylglutathione
-
30C, pH 7.0
0.029
-
(R)-S-lactoylglutathione
-
pH 7.0, 0.5 mM CoCl2
0.032
-
(R)-S-lactoylglutathione
-
pH 7.0, 0.5 mM NiCl2
0.045
-
(R)-S-lactoylglutathione
-
pH 7.0, 0.5 mM NiCl2
0.056
-
(R)-S-lactoylglutathione
-
pH 7.0, 0.5 mM NiCl2
0.061
-
(R)-S-lactoylglutathione
-
-
0.09
-
(R)-S-lactoylglutathione
-
30C, pH 7.0
0.12
-
(R)-S-lactoylglutathione
-
Brassica sp. gly I
0.07
-
2,4-dimethylphenylglyoxal
-
liver or erythrocyte enzyme
0.87
-
4,5-Dioxovalerate
-
-
1.2
-
4,5-Dioxovalerate
-
-
0.06
-
alpha-deuteriophenylglyoxal
-
-
0.2
-
gamma-glutamylcysteine-methylglyoxal hemithioacetal
Q9ZS21
30C, pH 7.5
0.24
-
gamma-glutamylcysteine-phenylglyoxal hemithioacetal
Q9ZS21
30C, pH 7.5
0.049
-
glutathione
-
-
0.35
-
glutathione
-
-
0.8
-
glutathione
-
pH 7.0, 25C
1.8
-
glutathione
-
with methylglyoxal; with phenylglyoxal
1.9
-
glutathione
-, Q68RJ8
-
0.042
-
glutathione ethyl ester
-
-
0.7
-
glutathione ethyl ester
-, Q68RJ8
-
0.053
-
glutathione isopropyl ester
-
-
0.3
-
glutathione isopropyl ester
-, Q68RJ8
-
0.58
-
glutathione-glyoxal hemithioacetal
-, Q71KM3
-
0.025
-
glutathione-methylglyoxal
Q9ZS21
30C, pH 7.5
0.0089
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Cd2+
0.01
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Fe2+; in the presence of Mn2+
0.012
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Co+
0.027
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Ni2+
0.077
-
glutathione-methylglyoxal hemithioacetal
-, Q71KM3
-
0.29
-
glutathione-methylglyoxal hemithioacetal
-
-
0.41
-
glutathione-methylglyoxal hemithioacetal
-
30C, pH 7.0
7.6
-
glutathione-methylglyoxal hemithioacetal
-, Q76E52
25C, pH 7.0, native Glb33
11
-
glutathione-methylglyoxal hemithioacetal
-, Q76E52
25C, pH 7.0, recombinant Glb33
0.049
-
glutathione-phenylglyoxal
Q9ZS21
30C, pH 7.5
0.008
-
glutathionylspermidine
-
with methylglyoxal
0.014
-
glutathionylspermidine
-
with phenylglyoxal
0.066
-
homoglutathione-methylglyoxal
Q9ZS21
30C, pH 7.5
0.027
-
homoglutathione-phenylglyoxal
Q9ZS21
30C, pH 7.5
0.2
-
kethoxal
-
-
0.03
-
m-methoxyphenylglyoxal
-
liver or erythrocyte enzyme
0.016
-
methylglyoxal
-
presence of Co2+, pH 7.0
0.028
-
methylglyoxal
-
presence of Co2+, pH 7.0
0.029
-
methylglyoxal
-
presence of Co2+, pH 7.0
0.032
-
methylglyoxal
-
presence of Ni2+, pH 7.0
0.045
-
methylglyoxal
-
presence of Ni2+, pH 7.0
0.056
-
methylglyoxal
-
presence of Ni2+, pH 7.0
0.078
-
methylglyoxal
-
-
0.09
-
methylglyoxal
-
liver or erythrocyte enzyme
0.13
-
methylglyoxal
-
-
0.14
-
methylglyoxal
-
-
0.21
-
methylglyoxal
-
-
0.32
-
methylglyoxal
-
-
0.34
-
methylglyoxal
-
-
0.35
-
methylglyoxal
-
-
0.44
-
methylglyoxal
-
-
0.5
-
methylglyoxal
-
-
0.53
-
methylglyoxal
-
-
0.91
-
methylglyoxal
-
-
1.25
-
methylglyoxal
-
-
1.6
-
methylglyoxal
-
pH 7.0, 25C
3.5
-
methylglyoxal
-
-
0.0272
-
methylglyoxal/glutathione hemithioacetal
P0AC81
-
-
0.192
-
methylglyoxal/glutathione hemithioacetal
-
-
-
0.46
-
methylglyoxal/glutathione hemithioacetal
-
-
-
0.8
-
methylglyoxal/glutathione hemithioacetal
-
-
-
0.064
-
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-, Q68RJ8
-
0.148
-
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
-
0.02
-
p-bromophenylglyoxal
-
liver or erythrocyte enzyme
0.02
-
p-chlorophenylglyoxal
-
liver or erythrocyte enzyme
0.03
-
p-hydroxyphenylglyoxal
-
liver or erythrocyte enzyme
0.01
-
p-methoxyphenylglyoxal
-
liver or erythrocyte enzyme
0.02
-
p-methylphenylglyoxal
-
liver or erythrocyte enzyme
0.02
-
p-phenylphenylglyoxal
-
liver or erythrocyte enzyme
0.19
-
perdeuteriomethylglyoxal
-
-
0.04
-
Phenylglyoxal
-
-
0.04
-
Phenylglyoxal
-
-
0.04
-
Phenylglyoxal
-
liver or erythrocyte enzyme
0.06
-
Phenylglyoxal
-
-
0.1
-
Phenylglyoxal
-
-
0.113
-
Phenylglyoxal
-
-
0.2
-
Phenylglyoxal
-
-
0.21
-
Phenylglyoxal
-
-
0.24
-
Phenylglyoxal
-
pH 7.0, 25C
0.31
-
Phenylglyoxal
-
-
0.0284
-
reduced trypanothione
-, Q5XQR1
recombinant enzyme, pH 7.2, room temperature
0.051
-
S-mandoyltrypanothione
-, Q68RJ8
purified enzyme, pH 7.0, 27C
0.071
-
trypanothione
-, Q68RJ8
-
0.109
-
trypanothione
-
with methylglyoxal
0.13
-
trypanothione
-
-
0.207
-
trypanothione
-
with phenylglyoxal
additional information
-
(R)-S-lactoylglutathione
-, Q68RJ8
more than 1.9, purified enzyme, pH 7.0, 27C
1.4
-
methylglyoxal/glutathione hemithioacetal
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
-
additional information
-
the KM value with Cd2+ is 0.0089 mM; the KM value with Co2+ is 0.012 mM; the KM value with Fe2+ is 0.01 mM; the KM value with Mn2+ is 0.01 mM; the KM value with Ni2+ is 0.027 mM
-
additional information
-
additional information
-, Q9HU72, Q9HY85, Q9I5L8
the KM value of Pseudomonas aeruginosa gloaA1 with Ni2+ is 0.032 mM; the KM value of Pseudomonas aeruginosa gloaA2 with Ni2+ is 0.021 mM; the KM value of Pseudomonas aeruginosa gloaA3 with Zn2+ is 0.287 mM
-
1.03
-
additional information
-
the apparent kinetic parameters are determined by varying the hemithioacetal concentration between 0.3 and 1.5 mM, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal
-
1.4
-
additional information
-
for the hemithioacetal as substrate
-
0.032
-
S-D-lactoyltrypanothione
-, Q68RJ8
purified enzyme, pH 7.0, 27C
additional information
-
S-mandoylglutathione
-, Q68RJ8
more than 0.08, purified enzyme, pH 7.0, 27C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1360
-
glutathione
-
-
164
-
glutathione ethyl ester
-
-
222
-
glutathione isopropyl ester
-
-
1170
-
glutathione isopropyl ester
-, Q68RJ8
-
1.5
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Fe2+
8
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Mn2+
21.4
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Cd2+
55.7
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Fe2+
60.2
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Mn2+
66.7
-
glutathione-methylglyoxal hemithioacetal
-, Q71KM3
-
106
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Co+
338
-
glutathione-methylglyoxal hemithioacetal
-
in the presence of Ni2+
1700
-
glutathione-methylglyoxal hemithioacetal
-
30C, pH 7.0
105
-
glutathionylspermidine
-
with phenylglyoxal
161
-
glutathionylspermidine
-
with methylglyoxal
11.4
-
methylglyoxal
-
-
69
-
methylglyoxal
-
presence of Co2+, pH 7.0
86
-
methylglyoxal
-
presence of Co2+, pH 7.0
146
-
methylglyoxal
-
presence of Co2+, pH 7.0
204
-
methylglyoxal
-
presence of Ni2+, pH 7.0
271
-
methylglyoxal
-
presence of Ni2+, pH 7.0
306
-
methylglyoxal
-
presence of Ni2+, pH 7.0
983
-
methylglyoxal
-
-
1130
-
methylglyoxal
-
-
1180
-
methylglyoxal
-
-
1820
-
methylglyoxal
-
-
338
-
methylglyoxal/glutathione hemithioacetal
P0AC81
-
-
83
-
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
-
1590
-
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-, Q68RJ8
-
0.53
-
Phenylglyoxal
-
-
81.7
-
Phenylglyoxal
-
-
617
-
Phenylglyoxal
-
-
1070
-
Phenylglyoxal
-
-
1100
-
Phenylglyoxal
-
-
6700
-
Phenylglyoxal
-
-
104
-
trypanothione
-
-
265
-
trypanothione
-
with phenylglyoxal
363
-
trypanothione
-
with methylglyoxal
1070
-
trypanothione
-, Q68RJ8
-
1820
-
methylglyoxal/glutathione hemithioacetal
-
-
-
additional information
-
additional information
-
the turnover number with Cd2+ is 21 s; the turnover number with Co2+ is 106 s; the turnover number with Fe2+ is 56 s; the turnover number with Mn2+ is 60 s; the turnover number with Ni2+ is 338 s
-
additional information
-
additional information
-, Q9HU72, Q9HY85, Q9I5L8
the turnover number of Pseudomonas aeruginosa gloaA1 with Ni2+ is 271 s; the turnover number of Pseudomonas aeruginosa gloaA2 with Ni2+ is 247 s; the turnover number of Pseudomonas aeruginosa gloaA3 with Zn2+ is 787 s
-
258.3
-
additional information
-
the apparent kinetic parameters are determined by using hemithioacetal as substrate, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0036
-
(1E,4Z,6E)-4-(4-hydroxy-3-methoxybenzylidene)-1-(3-hydroxy-4-methoxyphenyl)-7-(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30C
0.0046
-
(1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30C
0.0026
-
(1E,6E)-4-(3-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30C
0.0032
-
(1E,6E)-4-(4-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30C
0.0128
-
(2S)-2-amino-3-[([(2R)-3-[(4-bromobenzyl)sulfanyl]-1-[(carboxymethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoic acid
-
0.05 M phosphate buffer pH 6.6, 30C
0.00628
-
(S)-4-bromobenzyl glutathione
-
-
4.1
-
2,3-Butanedione
-
-
0.0036
-
4-[(4E)-5-(3,4-dimethoxyphenyl)-2-[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]-3-oxopenta-1,4-dien-1-yl]benzene-1,2-dicarbaldehyde
-
pH 7.1, 30C
0.0103
-
bisdemethoxycurcumin
-
-
0.1
-
chromoglycate
-
-
0.0051
-
curcumin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, competitive inhibition, pH 7.0, 30C
0.0182
-
curcumin
-
-
0.383
-
fenoprofen
-
pH 7.1, 30C
0.00015
-
gerfelin
-
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30C
0.0244
-
Indomethacin
-
-
0.0244
-
Indomethacin
-
pH 7.1, 30C
0.021
-
kaempferol
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30C
0.843
-
Ketoprofen
-
pH 7.1, 30C
0.00000617
-
L-gamma-glutamyl-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
-
-
0.035
-
luteolin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30C
0.00023
-
methyl gerfelin
-
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30C
0.17
-
methylglutathione
-, Q71KM3
-
0.013
-
myricetin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30C
0.1124
-
N-[(1S,4Z)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohept-4-en-1-yl]-L-glutamine
-
-
0.06688
-
N-[(1S,4Z)-6-(4-bromophenyl)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohex-4-en-1-yl]-L-glutamine
-
-
0.00219
-
N-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
-
-
0.0000326
-
N2-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
-
-
0.0000326
-
NH2-gamma-Gla[-Glu(CON(OH)-4-bromophenyl)Gly-OH]-OH
-
-
0.00000166
-
NH2-gamma-Glu[-D-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
0.000000123
-
NH2-gamma-Glu[-Dab(N-(4-bromobenzoyl)-N'-hydroxyl)-Gly-OH]-OH
-
-
0.00000617
-
NH2-gamma-Glu[-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
0.4
-
Phenylglyoxal
-
-
0.023
-
quercetin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30C
0.14
-
rutin
-
in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30C
0.00003
-
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
-
0.00006
-
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
-
0.00005
-
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
-
0.00008
-
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
-
0.000014
-
S-(N-hydroxy-N-p-bromophenylcarbamoyl)glutathione
-
-
0.00001
-
S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
-
0.5
-
S-2,4-dinitrophenylglutathione
-, Q68RJ8
-
0.645
-
S-2,4-dinitrophenylglutathione
-
-
0.669
-
S-2,4-dinitrophenylglutathionylspermidine
-, Q68RJ8
-
0.915
-
S-2,4-dinitrophenylglutathionylspermidine
-
-
0.000128
-
S-4-bromobenzylglutathione
-
-
0.5
-
S-4-bromobenzylglutathione
-, Q68RJ8
-
0.000536
-
S-4-bromobenzylglutathionylspermidine
-, Q68RJ8
-
0.0054
-
S-4-bromobenzylglutathionylspermidine
-
-
0.0126
-
S-4-bromobenzylglutathionylspermidine
-
-
0.00028
-
S-benzylglutathione
-
-
0.0057
-
S-bromobenzylglutathione
-
-
0.021
-
S-bromobenzylglutathione
-
-
0.015
-
S-hexylglutathione
-
-
0.00008
-
S-p-bromobenzylglutathione
-
-
0.032
-
S-p-nitrobenzylglutathione
-
-
0.083
-
S-p-nitrobenzylglutathione
-
-
0.06
-
S-p-nitrosobenzylglutathione
-, Q71KM3
-
0.19
-
S-p-nitrosobenzylglutathione
-, Q71KM3
-
0.00115
-
zinc (2S)-2-amino-3-([(3R)-3-([[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]methyl)-4-[(carboxylatomethyl)amino]-4-oxobutanoyl]amino)propanoate
-
0.05 M phosphate buffer pH 6.6, 30C
0.00219
-
zinc (2S)-2-amino-3-[([(2R)-3-[[(4-bromophenyl)(hydroxy)carbamoyl]sulfanyl]-1-[(carboxylatomethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoate
-
0.05 M phosphate buffer pH 6.6, 30C
0.335
-
Zomepirac
-
pH 7.1, 30C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.002
-
(3Z)-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid
-
pH 7.0, 25C
0.0546
-
2-([(4-methoxyphenyl)carbonyl]amino)-1-benzothiophene-3-carboxylic acid
-
pH 7.0, 25C
0.0932
-
2-([(4-methoxyphenyl)carbonyl]amino)benzoic acid
-
pH 7.0, 25C
-
0.011
-
baicalein
-
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25C, pH 7.0
0.056
-
flavone
-, Q5XQR1
IC50 wild type 56 microM
0.069
-
flavone
-, Q5XQR1
IC50 enzyme overexpressor 69 microM
0.0206
-
kaempferol
-
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25C, pH 7.0
0.093
-
Lapachol
-, Q5XQR1
IC50 wild type 93 microM
0.096
-
Lapachol
-, Q5XQR1
IC50 enzyme overexpressor 96 microM
0.007
-
luteolin
-
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25C, pH 7.0
0.00056
-
myricetin
-
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25C, pH 7.0
0.00056
-
myricetin
-
pH 7.0, 25C
0.07
-
Purpurogallin
-, Q5XQR1
IC50 wild type 70 microM
0.132
-
Purpurogallin
-, Q5XQR1
IC50 enzyme overexpressor 132 microM
0.0032
-
quercetin
-
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25C, pH 7.0
0.026
0.027
quercetin
-, Q5XQR1
IC50 wild type 26 microM, IC50 enzyme overexpressor 27 microM
0.00006
-
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
IC50 0.06 microM
0.00009
-
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
IC50 0.09 microM
0.00011
-
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
IC50 0.11 microM
0.0025
-
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
-
IC50 2.5 microM
0.01
-
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
-
IC50 10 microM
0.0332
-
S-4-bromobenzylglutathione
-
pH 7.0, 25C
0.023
-
S-p-bromobenzylglutathione
-
calculated, effectively inhibits rhGLO I at 25C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.023
-
-
recombinant protein, expressed in Trypanosoma brucei which lacks GLO1 activity, procyclic form, pH 7.0, 25C
0.038
-
-
recombinant protein, expressed in Trypanosoma brucei which lacks GLO1 activity, bloodstream form, pH 7.0, 25C
0.042
-
-
whole cell lysate, pH 7.0, 25C
0.085
-
-
whole cell lysate, pH 7.0, 25C
0.172
180
-
without addition of S-ethyl cysteine, s-propyl-cysteine, or ascorbic acid, pH 6.6, 37C
0.184
-
-
slightly increased activity compared to enzyme assay without ascorbic acid, pH 6.6, 37C
0.19
-
-
slightly increased activity compared to enzyme assay without ascorbic acid, pH 6.6, 37C
0.218
-
-
in the presence of 1 g/l S-ethyl cysteine, 1.2fold higher activity than without S-ethyl cysteine, pH 6.6, 37C
0.221
-
-
in the presence of 1 g/l S-propyl-cysteine, 1.3fold higher activity than without S-ethyl cysteine, pH 6.6, 37C
0.247
-
-
in the presence of 2 g/l S-ethyl cysteine, 1.4fold higher activity than without S-ethyl cysteine, pH 6.6, 37C
0.258
-
-
in the presence of 2 g/l S-propyl-cysteine, 1.5fold higher activity than without S-ethyl cysteine, pH 6.6, 37C
0.34
-
-, Q5XQR1
micromol/min/mg protein, native enzyme from crude lysate, pH 7.2, room temperature
0.4
-
-
breast cancer cell MDA-MD-231 cell, pH 7.0, 30C
0.9
-
-
brain astrocytoma 1321N1 cell, pH 7.0, 30C
1.17
-
-
breast cancer cell JIMT-1 cell, pH 7.0, 30C
1.4
-
-
prostate cancer cell PC-3 cell, pH 7.0, 30C
1.94
-
-
crude extract, at 22C
8.69
-
-
addition of 6 g/kg ethanol and iron, 57% activity of control without ethanol and iron
10.36
-
-
addition of 6 g/kg ethanol, 68% activity of control without ethanol
12.01
-
-
addition of 6 g/kg ethanol, iron, and 2% (w/v) taurine, 68% activity of control without ethanol, iron, and taurine
13.34
-
-
addition of 6 g/kg ethanol and 2% (w/v) taurine, 79% activity of control without ethanol and taurine
15.24
-
-
without addition of ethanol, iron, or taurine
15.62
-
-
addition of 2% (w/v) taurine, 102% activity of control without ethanol, iron, or taurine
46.2
-
-
wild-type, at pH 5.0
68.7
-
-
mutant, at pH 5.0
90
-
-, Q71KM3
-
105
-
-
towards phenylglyoxal
110
-
-
30C, pH 7.0
140
-
-
presence of Co2+, pH 7.0
150
-
-
30C, pH 7.0
159
-
-
-
180
-
-
presence of Co2+, pH 7.0
188.3
-
-
-
191
-
-
kidney enzyme
200
-
-
-
279
-
-
presence of Co2+, pH 7.0
284
-
-
towards methylglyoxal
356
-
-
after 184fold purification, at 22C
390
-
-
micromol/min/mg protein, Vmax (R)-S-lactoylglutathione, pH 7.0, 0.5 mM NiCl2, 279 micromol/min/mg protein Vmax (R)-S-lactoylglutathione, pH 7.0, 0.5 mM CoCl2; presence of Ni2+, pH 7.0
425
-
-
-
565
-
-
-
571
-
-
micromol/min/mg protein, Vmax (R)-S-lactoylglutathione, pH 7.0, 0.5 mM NiCl2, 180 micromol/min/mg protein Vmax (R)-S-lactoylglutathione, pH 7.0, 0.5 mM CoCl2; presence of Ni2+, pH 7.0
618
-
-
micromol/min/mg protein, Vmax (R)-S-lactoylglutathione, pH 7.0, 0.5 mM NiCl2, 140 micromol/min/mg protein Vmax (R)-S-lactoylglutathione, pH 7.0, 0.5 mM CoCl2; presence of Ni2+, pH 7.0
814
-
-
brain enzyme
925
-
-
-
943.6
-
-
-
944
-
-
-
950
-
-
liver
957
-
-
-
983
-
-
liver enzyme
1019
-
-
-
1150
-
-
-
1830
-
-
-
2110
-
-
erythrocytes
2200
-
-
-
2415
-
-
erythrocyte enzyme
3400
-
-, Q5XQR1
micromol/min/mg protein, recombinant enzyme, pH 7.2, room temperature
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
proliferating callus cltures show a 3.3fold increase in glyoxalase I activity during the logarithmic growth phase, activity is also induced during salt stress
additional information
-
-
8fold higher activity than in non-cancerous cells
additional information
-
-
Vmax methylglyoxal purified enzyme 2 mmol/min/mg protein, Vmax phenylglyoxal 0.197 mmol/min/mg protein, pH 7.0, 25C
additional information
-
Phaeosphaeria nodorum
-, Q696X2
23 U/mg protein wild type, 19 U/mg protein ectopic control mutant Gox1-2
additional information
-
-, Q68RJ8
40 nmol/min/mg Leishmania major extract, trypanothione, pH 7.0, 27C. Below 5 nmol/min/mg Leishmania major extract, pH 7.0, 27C
additional information
-
-
determined spectrophotometrically at 240 nm, glyoxalase I activities for 2-methyl-4-dimethylaminoazobenzene-fed rats (10 weeks fed) are 1.7times higher than that of control animals; determined spectrophotometrically at 240 nm, glyoxalase I activities for 3'-methyl-4-dimethylaminoazobenzene-fed rats (10 weeks fed) are 1.6times higher than that of control animals; determined spectrophotometrically at 240 nm, glyoxalase I activities for 4'-methyl-4-dimethylaminoazobenzene-fed rats (10 weeks fed) are 1.5times higher than that of control animals
additional information
-
-
enzyme activity decreases significantly from 0.2 U/single Caenorhabditis elegans at day 1 to 0.02 U/single Caenorhabditis elegans at day 12. In contrast mRNA expression of the homologue, CeGly did not decrease at day 12 but slightly increase, suggesting that post-transciptional modification of glyoxalase-1 protein, rather than decrease transcription, accounted for the age-related decrease in enzyme activity. The glyoxalase-1 homologue CeGly is subcloned into a Green Fluorescent Protein (GFP) vector under control of its native promotor. Enzymatic activity of CeGly in cultures of age-synchronized 1-day-old transgenic Caenorhabditis elegans overexpressing CeGly is ca. 200fold higher than in the wild-type strain. Increased enzymatic activity in transgenic animals results in a significant reduction of both methylglyoxal and methylglyoxal-derived arginine- and lysine-derived adducts. Increased glyxalase-1 activity significantly prolongs lifespan. Mean lifespan increases in transgenic animals from 13.3 days to 17.2 days and maximum lifespan from 28 days to 37 days
additional information
-
-
overexpression of Glo1 in human microvascular endothelial cells results in a 4fold increase in glyoxalase 1 activity
additional information
-
-
ischemia/reperfusion induces the reduction of GLO I activity in the kidney, which is asssociated with morphological damage and renal dysfunction
additional information
-
-
activity of glyoxalase I in Pisum sativum shows linear progression with development of shoots and roots of seedlings, cell division and proliferation further modulate the activity
additional information
-
-
the GLO1 activity of the transformed Vigna mungo plants is higher than in the untransformed control plants
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
-
6.5
7.5
-
-
6.5
7.5
-
-
6.5
-
-
assay at
6.6
-
-
assay at
6.8
-
-
assay at
7
-
-
assay at
7
-
-
assay at
7
-
-
assay at
7.1
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.8
-
-, Q71KM3
-
additional information
-
-
has a very broad pH optimum with two small local maxima at pH 7.0 and 7.5 and a third local maximum at pH 5.8
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
7.5
-
lgl mRNA levels are 3.5fold higher in cells grown at pH 5.0 than in cells grown at pH 7.5, levels of lgl transcript are increased 2.1fold in cells exposed to pH 5.5 for 2 h
5
9
-
50% of maximal activity at pH 5.0 and at pH 9.0
5.8
8.2
-
pH 5.8: about 30% of maximal activity, pH 8.2: about 85% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
additional information
-
-
enzyme assay at room temperature
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
-
-, Q9CJC0
calculated from sequence, 30fold upregulated protein spot in the 2D-electrophoresis, identified as glyoxalase I, the expression is regulated by the operon yahCD-yaiAB
4.9
-
-, Q68RJ8
chromatofocusing
5.2
-
-
calculated from amino acid sequence
5.3
-
-
isoelectric focusing
5.4
-
-
calculated from amino acid sequence
6
-
-, D6QLX5
calculated
7.8
-
-
-
8.1
-
-
mitochondrial form of Oryza sativa gly I
8.59
-
-
calculated
additional information
-
-
plant gly I ranges from 4.7-5.1
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
1321N1 cell; brain astrocytoma cell
Manually annotated by BRENDA team
-
Brodmann area 22, glyoxalase I levels are diminished in old aged brains but elevated in Alzheimers disease brains, Brodmann area 28, elevated amounts of advanced glycation end staining and decreased levels of glyoxalase I with advancing stage of Alzheimers disease
Manually annotated by BRENDA team
-
in situ hybridization experiments, developing mouse brain
Manually annotated by BRENDA team
-
MDA-MD-231 cell, JIMT-1 cell
Manually annotated by BRENDA team
-
the highest glyoxalase I concentration is found in mature bulbs
Manually annotated by BRENDA team
-
in situ hybridization experiments, Purkinje cells in the cerebellum express GLO1 mRNA strongly and specifically
Manually annotated by BRENDA team
-
in situ hybridization experiments, highest expression at postnatal day 14
Manually annotated by BRENDA team
-
in situ hybridization experiments, highest expression at postnatal day 14
Manually annotated by BRENDA team
-
in situ hybridization experiments, lining the third ventricle and choroid plexus
Manually annotated by BRENDA team
-
in situ hybridization experiments, highest expression at postnatal day 14
Manually annotated by BRENDA team
-
human dermal microvascular endothelial cell
Manually annotated by BRENDA team
-
breast cancer cell
Manually annotated by BRENDA team
-
male Balb/cA mice, 3-4 week old
Manually annotated by BRENDA team
-
transcription level and glyoxalase I activity are higher in pathological tissues than in normal ones
Manually annotated by BRENDA team
-
glyoxalase I activity and mRNA levels are elevated in diabetic lenses
Manually annotated by BRENDA team
-
GLOI is mainly localized in the anterior epithelium but the enzyme is diffusely present in outer cortical and nuclear regions of the human lens
Manually annotated by BRENDA team
-
Bcr-Abl+ leukemic stem cell
Manually annotated by BRENDA team
-
disinfected water from two drinking water production plants at the river Po in North Italy markedly perturb the crap liver detoxfifying system, in terms of both induction and inhibition of enzyme activities and glutathione content
Manually annotated by BRENDA team
-
breast cancer cell
Manually annotated by BRENDA team
-
prostate cancer cell
Manually annotated by BRENDA team
-
preferentially accumulated in phloem and sieve cells
Manually annotated by BRENDA team
Leishmania major Friedlin
-
-
-
Manually annotated by BRENDA team
-
preferentially accumulated in phloem and sieve cells
Manually annotated by BRENDA team
-
in situ hybridization experiments, highest expression at postnatal day 14
Manually annotated by BRENDA team
-
found to be conserved in tubers among different potato variants
Manually annotated by BRENDA team
-
in situ hybridization experiments, GLO1 is dominantly expressed in the embryonic ventricular zone at day 16, reducing the celluar level of methylglyoxal and suppressing the formation of argpyrimidine in the neural stem and progenitor cells
Manually annotated by BRENDA team
additional information
-
renal carcinoma cell, clear cell adenocarcinoma, 9fold increase in the transcription levels of glyoxalase I compared with pair-matched noncancerous tissues
Manually annotated by BRENDA team
additional information
-
HRP cell
Manually annotated by BRENDA team
additional information
-
LE cell, lens epithelial cells, activity of the enzyme in hyperglycemic conditions is nearly 20% higher than in control conditions
Manually annotated by BRENDA team
additional information
-
HPMC cell
Manually annotated by BRENDA team
additional information
-
ischemia/reperfusion induces the reduction of GLO I activity in the kidney, which is asssociated with morphological damage and renal dysfunction
Manually annotated by BRENDA team
additional information
-
permeabilized cells of Saccharomyces cerevisiae, with 0.01% (w/v) digitonin
Manually annotated by BRENDA team
additional information
-
gly I is present in all types of cells and tissues
Manually annotated by BRENDA team
additional information
-
present in all types of cells and tissues
Manually annotated by BRENDA team
additional information
-
gly I is present in all types of cells and tissues
Manually annotated by BRENDA team
additional information
-
in the bloodstream and procyclic form of the recombinant protein of Trpypanosomas brucei, overexpressed with GLO1 of Trypanosomas cruzi
Manually annotated by BRENDA team
additional information
-
young leaves of the transgenic plant Vigna mungo, transformed with gly1 from Brassica juncae using a transformation system via Agrobacterium tumefaciens, driven by a constitutive Cestrum yellow leaf curling viral promotor
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Enterococcus faecalis (strain ATCC 700802 / V583)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
14250
-
-
electrospray ionization mass spectrometry
15670
-
-
electrospray ionization mass spectrometry
16000
-
-
Western blot analysis of whole cell lysate, equivalent to the predicted molecular mass
16000
-
-
Western blot analysis of whole cell lysate, equivalent to the predicted molecular mass. Recombinant protein containing a tetracycline-inducible pLew100-TcGLO1 construct, expression of GLO1 of Trypanosoma cruzi in Trypanosoma brucei, Western blot analysis
16000
-
-
native enzyme, SDS-PAGE
21000
-
-
gel filtration
21000
-
-
calculated from amino acid sequence
23000
-
-
SDS-PAGE
25000
-
-
SDS-PAGE
28000
-
-
Western blot analysis
29670
-
-
electrospray ionization mass spectrometry
30000
-
P0AC81
gel filtration
31300
-
-
size exclusion chromatography and analytical ultracentrifugation
32000
-
-
gel filtration
32500
-
-
calculated from amino acid sequence
33000
-
-
gel giltration
33000
-
-
SDS-PAGE
34000
-
-
-
34000
-
-
gel filtration
35840
-
-
calculated from amino acid sequence
36000
-
-
gel filtration
37000
-
-
; Triticum aestivum gly I enzyme is a monomer
38000
-
-
gel filtration
38000
-
Q9ZS21
gel filtration
38700
-
-, Q68RJ8
gel filtration
41620
-
-
calculated from sequence, MALDI-TOF mass spectrometry
42000
-
-
gel filtration
42300
-
-, Q71KM3
gel filtration
43000
-
-
-
43000
-
-
equilibrium sedimentation
43000
-
-
gel filtration
43310
-
-, Q9CJC0
calculated from sequence, 30fold upregulated protein spot in the 2D-electrophoresis, identified as glyoxalase I, the expression is regulated by the operon yahCD-yaiAB
44000
-
-
gel filtration
44000
-
-
gel filtration
44000
-
-
; enzyme is a monomer
45000
-
-
gel filtration
45900
-
-
gel filtration
46000
-
-
-
46000
-
-
-
46000
-
-, Q5XQR1
SDS-PAGE, enzyme cross-linked with glutaraldehyde
48000
-
-
gel filtration
48000
-
-
gel filtration
48000
-
-
gel filtration
50000
-
-
liver and erythrocyte enzyme, gel filtration
51000
-
-
-
52000
-
-
gel filtration
54000
-
-
gel filtration
56000
-
-
gel filtration
58000
-
-
Brassica gly I enzyme
60000
-
-
gel filtration
60000
-
-
enzyme has two subunits
additional information
-
-, Q9HU72, Q9HY85, Q9I5L8
GlxI is longer than the Escherichia coli enzyme but similar to the Homo sapiens enzyme; size is similar to the Escherichia coli enzyme and to Pseudomonas aeruginose Glx1 GloA1
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 27000, SDS-PAGE
?
-
x * 20774, calculation from nucleotide sequence
?
-, Q76E52
x * 33000, SDS-PAGE, native and recombinant Glb33
?
O04885
x * 24000, SDS-PAGE
?
-
x * 15669, electrospray ionization mass spectrometry, x * 15669, calculated
?
-
x * 14251, electrospray ionization mass spectrometry, x * 14251, calculated
?
-
x * 14833, electrospray ionization mass spectrometry, x * 14834, calculated
?
-
x * 28000, Western blot analysis
?
-, D6QLX5
x * 35500, calculated
dimer
-
1 * 24000 + 1 * 25000, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 27000, SDS-PAGE
dimer
-
2 * 26000
dimer
-
2 * 21000, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 21500
dimer
-
1 * 27000 + 1 * 29000, SDS-PAGE
dimer
P0AC81
2 * 14919, electrospray mass spectrometry; 2 * 14990, SDS-PAGE
dimer
-
2 * 23000, SDS-PAGE
dimer
-
1 * 26000 + 1 * 29000, SDS-PAGE
dimer
Q9ZS21
2 * 21000, deduced from nucleotide sequence; 2 * 24000, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
dimer
-, Q5XQR1
2 * 23440, SDS-PAGE
dimer
-
2 * 148333, electrospray ionization mass spectrometry
dimer
-, Q68RJ8
2 * 16607, mass spectrometry
dimer
-
x * 17000, SDS-PAGE or Western blot analysis, x * 16647, predicted, x * 16650, MALDI-TOF-MS analysis
dimer
Q9HU72
GloA2 and GloA3, gel filtration
dimer
-
treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
dimer
-
gly1
dimer
-
-
dimer
-
2 * 27000-29000
heterodimer
-
enzyme has 2 subunits
heterodimer
-
Glycine max gly I enzyme has 2 subunits
homodimer
-
the homodimeric GlxI of Escherichia coli consists of two identical polypeptide chains with one tryptophan on each chain on position 61, with two symmetrical active sites where one metal ion has been observed in each individual active site. One active site binds to the Ni2+ ion, and the other active site is observed to be more selelective for a potent inhibitor
homodimer
-
mammalian glyoxalase I is composed of two equal subunits which both harbor an acitve site
homodimer
-
GlxI, containing activating metals all have two water molecules bound to the active site metal along with four protein side chains making up the homodimer of the enzyme: His5 A-subunit, Glu56 A-subunit, His74 B-subunit, Glu122 B-subunit. The inactive Zn2+-bound enzyme has the same four protein side chains bound to the metal, but only one water molecule is coordinated to the Zn2+
homodimer
-
2 * 20810, calculated from sequence, MALDI-TOF mass spectrometry, SDS-PAGE
homodimer
-, Q2PYM9
2 * 18200, calculated from amino acid sequence
monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
monomer
-
1 * 20000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE
monomer
-
1 * 38000, SDS-PAGE
monomer
-, Q71KM3
1 * 43600, SDS-PAGE, recombinant His-tagged PfGlx I
monomer
-
single polypeptide with two active sites that catalyze the same reaction
monomer
Q9XGF2
1 * 37000, SDS-PAGE
monomer
-
1 * 34000, SDS-PAGE
monomer
-
gel filtration
monomer
-
treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
monomer
-
1 * 44000; Aloe vera gly I
monomer
-
1 * 37000
monomer
Chlamydomonas reinhardtii 5177D mt-
-
1 * 24000, SDS-PAGE
-
monomer
Saccharomyces cerevisiae DKD-5D-H
-
1 * 33000, SDS-PAGE
-
monomer
Schizosaccharomyces pombe PR 109
-
1 * 34000, SDS-PAGE
-
additional information
-
enzyme is composed of a single polypeptide chain containing two active sites. It has been shown that there is a allosteric coupling between the two active sites
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-, D6QLX5
sequence contains two potential N-glycosylation sites
phosphoprotein
-
phosphorylated by calcium, calmodulin-dependent protein kinase II at Thr106 revealed by site-directed mutagenesis of several serine and threonine residues. Mutagenesis of Thr106 to Ala completely abolishes the phosphorylation. GLO1 is only phosphorylated when it is co-expressed with the catalytic subunit of calcium, calmodulin-dependent protein kinase II but no phosphorylation is observed when GLO1 is co-expressed with protein kinase A. Phosphorylation can suppress NF-kappaB-dependent reporter gene expression, more powerful in suppression than NO-mediated modification of GLO1. Tumor necrosis factor induces phosphorylation of GLO1 on Thr106
glutathionylation
-
glutathionylation strongly inhibits Glo1 activity in vitro
additional information
-
NO-mediated modification can suppress NF-kappaB-dependent reporter gene expression, less powerful in suppression than phosphorylation of GLO1
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a comparison of the X-ray structures of the Escherichia coli GlxI reconstituted with Zn2+ (inactive) and with the activating metals Co2+, Cd2+, Ni2+ reveals that all activating metals have an octahedral environment, but the Zn2+-bound form of the enzyme results in antrigonal bipyramidal five-coordinate environment around the metal. GlxI, containing activating metals all have two water molecules bound to the active site metal along with four protein side chains making up the homodimer of the enzyme: His5 A-subunit, Glu56 A-subunit, His74 B-subunit, Glu122 B-subunit. The inactive Zn2+-bound enzyme has the same four protein side chains bound to the metal, but only one water molecule is coordinated to the Zn2+
-
crystallization of apo GlxI and GlxI complexed with Ni2+ Co2+, Cd2+, Zn2+, and seleno-L-methionine-Ni2+ by vapor diffusion in hanging drops, 0.005 ml protein solution at 12-37 mg/ml is mixed with an equal volume of well solution containing 5-10% polyethylene glycol 1000 and 5-10% polyethylene glycol 8000, crystals diffract to 1.5-2.5 A, Zn2+-GlxI complex has trigonal bipyramidal instead of octhedral coordination with Ni2+, Co2+ and Cd2+ and is inactive
-
the homodimeric GlxI of Escherichia coli consists of two identical polypeptide chains with one tryptophan on each chain on position 61, with two symmetrical active sites wehre one metal ion has been observed in each individual active site. One active site binds to the Ni2+ ion, and the other active site is observed to be more selelective for a potent inhibitor
-
crystal sructure of glyoxalase I in complex with S-(N-hydroxy-N-p-bromophenylcarbamoyl)glutathione and S-p-nitrobenzyloxycarbonylglutathione at 2.0 and 1.72 A, respectively
-
crystal structure of glyoxalase I complexed with S-benzylglutathione and S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
molecular docking of all inhibitors tested into crystal structure, PDB entry 1QIN. In the binding model of the three-ring curcumin derivatives, two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site. 6 ns molecular dynamics simulations of compound (1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione show two important hydrogen bonds: one is between hydroxyl oxygen atom of compound (1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione and the nitrogen atom in residue Arg37, and one between the hydroxyl oxygen of the compound inside the hydrophobic pocket and the carbonyl oxygen of residue Met179. The original hydrogen bond disappears but a new and stable one is formed. The average distance from Zn2+ to outer carbonyl oxygen of compound (1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione is about 2.095 A during 6 ns simulation. Pi-pi stacking interaction is observed between a phenyl ring of the ligand and residue Phe67
-
recombinant enzyme in complex with S-benzyl-glutathione
-
sitting drop vapor diffusion method, using 62% (v/v) 2-methyl-2,4-pentanediol and 100 mM Tris-HCl pH 8.5
-, Q2PYM9
2.0 A resolution
-
to 2.0 A resolution, three protein dimers per asymmetric unit in spacegroup P21212, structural differences from both Escherichia coli GLO1 and human GLO1, loop between strands beta6 and beta7 is shortened, 15-residue C-terminal helix is not present in Escherichia coli GLO1, although a helix is observed at the C-terminus of human GLO1, it is in a different orientation and 10 residues shorter
-, Q68RJ8
complex with methyl-gerfelin, structural resolution at 1.7 A. The model contains one protein homodimer, two zinc ions, and two methyl-gerfelin molecules in an asymmetric unit. The two active sites of the homodimer are located at the dimer interface and are characterized by a zinc-ion-binding site, a glutathione-binding site, and a hydrophobic pocket. In the active site, the zinc ion is on octahedral coordination and is bound by Gln34, Glu100, His127, Glu173 and two hydroxyl groups of methyl-gerfelin directly
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
10
-
stable at 4C for at least 24h
7.5
8.5
-
4C, 24 h, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
40
-
pH 7.0, 30 min, stable
60
-
-
100% activity after 4 h incubation at 60C, 50% inactivation after 150 min incubation at 64C or after 60 min incubation at 65C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme is fully stable in dialysis in contrast to the metal-free enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for 3 weeks
-
-20C, stable for several weeks
-
-30C, in presence of glutathione, stable for 6 months
-
-30C, stable for at least 2 months
-
0C or -70C, native enzyme loses 0-10% of activity, metal-free enzyme loses 30-40% of activity during 40 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, DEAE-cellulose column chromatography, hydroxyapatite column chromatography, and S-hexylglutathione-agarose column chromatography
-
60C, DEAE-52 cellulose, S-hexylglutathione Sepharose 6 B affinity, gel filtraton
-
wild-type and rebombinant protein
-
recombinant glyoxalase I
Q9ZS21
from erythrocytes, purity above 90%
-
Ni-NTA resin column chromatography
-
purification of endogenous and His-tagged enzyme, wild-type and mutants (T106A, S44A, S68A, S93A, T97A, T101A). The amount of purified enzyme is higher, when GLO1 (wild-type and mutants) is co-expressed with calcium,calmodulin-dependent protein kinase II, suggesting that the kinase induces the stabilization of GLO1
-
Co2+ affinity column chromatography and Superdex S75 gel filtration
-, Q2PYM9
by affinity chromatography
-
; recombinant enzyme
-
recombinant glyoxalase I
-
native and recombinant glyoxalase I
-, Q76E52
by gel filtration
-
; recombinant enzyme
-
GloA2 and GloA3, by gel filtration
Q9HU72
recombinant glyoxalase I
-
partial
-
to homogeneity via nickel affinity and anion exchange chromatography
-
; recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli XL1-Blue cells
-
expression in Nicotiana tabaccum improves salinity tolerance of tobacco plants
O04885
expression of cDNA in Escherichia coli and in tobacco
O04885
Brassica sp. gly I, cloning and overexpression in tobacco, transgenic plants tolerate higher concentrations of NaCl
-
the glyoxalase-1 homologue CeGly is subcloned into a Green Fluorescent Protein (GFP) vector under control of its native promotor. Enzymatic activity of CeGly in cultures of age-synchronized 1-day-old transgenic Caenorhabditis elegans overexpressing CeGly is ca. 200fold higher than in the wild-type strain. Increased enzymatic activity in transgenic animals results in a significant reduction of both methylglyoxal and methylglyoxal-derived arginine- and lysine-derived adducts. Increased glyoxalase-1 activity significantly prolongs lifespan. Mean lifespan increases in transgenic animals from 13.3 days to 17.2 days and maximum lifespan from 28 days to 37 days
-
expression in Escherichia coli
-
overexpressed in Escherichia coli BL21 (DE3), purified
-
recombinant overproduction of gly1 in Escherichia coli in the presence of Ni2+ in the growth medium results in the formation of active enzyme, overproduction of in the presence of Zn2+ in the growth medium results in the formation of inactive enzyme
-
Brassica sp. gly I, cloning and overexpression in tobacco, transgenic plants tolerate higher concentrations of NaCl
-
expression of cDNA in Escherichia coli
Q9ZS21
expressed in Rattus norvegicus
-
expression in Escherichia coli
-
GST-GLOI fusion protein is expressed in Escherichia coli BL21 (DE3)pLysS cells
-
into vector pCMS-EGFP, overexpression in HRP cells
-
overexpression of Glo1 in endothelial cells to investigate the effect on hyperglycemia-induced impairment of angiogenesis in vitro. The overexpression results in an increased protection against dicarbonyl glycation of endothelial cell protein protecting against hyperglycemia-induced angiogenesis deficit. The formation of tube structures through hyperglycemia decreases by 32%
-
the gene for glyxalase I is located on chromosome 6, locus 6p21,3-6p21,2. Study of A419C (E111A) single nucleotide polymorphism of the glyoxalase I gene
-
wild-type and mutants (T106A, S44A, S68A, S93A, T97A, T101A) expressed and co-expressed in HEK-293 cells, co-expression of His-tagged GLO1 with the catalytic subunit of calcium, calmodulin-dependent protein kinase II and protein kinase A. GLO1 is only phosphorylated when it is co-expressed with the catalytic subunit of calcium, calmodulin-dependent protein kinase II but no phosphorylation is observed when GLO1 is co-expressed with protein kinase A. Overexpression of wild-type GLO1 suppresses tumor-necrosis factor-induced NF-kappaB-dependent reporter gene expression. Supression of the basal and tumor-necrosis factor-induced NF-kappaB activity is significantly stronger upon expression of a GLO1 mutant that is either deficient for the NO-mediated modification or phosphorylation on Thr106
-
expression in Escherichia coli and Leishmania donovani
-, Q5XQR1
expressed in Escherichia coli BL21-Codon-Plus cells
-, Q2PYM9
expression in Escherichia coli
-, Q68RJ8
expression in Escherichia coli
-
expression in Escherichia coli
-
cloning of cDNA, expression in Escherichia coli
-, Q76E52
expression in Escherichia coli XL1 Blue
Phaeosphaeria nodorum
-, Q696X2
expression in Escherichia coli
-
pQE30 constructs of the wild-type and mutants expressed in Escherichia coli strain M15
-
expression in Escherichia coli
-
isolation and overproduction of glxI enzymes from Pseudomonas aeruginosa using Escherichia coli expression systems; isolation and overproduction of glxI enzymes from Pseudomonas aeruginosa using Escherichia coli expression systems; isolation and overproduction of glxI enzymes from using Escherichia coli expression systems
-, Q9HU72, Q9HY85, Q9I5L8
gloA2 and gloA3 ligated into vector pET22b, overexpression in Escherichia coli BL21(gammaDE3)
Q9HU72
expressed in transgenic Escherichia coli
P16635
expression in Escherichia coli
-
rats, overexpressing human GLO I show e.g. improvement of the tubulointerstitial injury and renal function
-
expression in Escherichia coli
-
overexpressing mutant YEpGLO1, shows increased methylglyoxal resistance
-
expression in Saccharomyces cerevisiae
-
expression in yeast
-
expressed in tobacco leaves via Agrobacterium tumefaciens infection
-
pET15b-GLO1 construct expressed in Escherichia coli BL21(DE3)pLysS cells
-
Trypanosoma brucei lacks GLO1 activity. GLO1 of Trypanosoma cruzi is overexpressed in Trypanosoma brucei in the procyclic and the bloodstream form to complete the glyoxalase system, resulting in an increased resistance to methylglyoxal and increased conversion of methylglyoxal to D-lactate, demonstrating that glyoxalase II (GLO2, EC 3.1.2.6) is functional in vivo
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the activity of glyoxalase I increases with increasing NaCl concentration, activity of glyoxalase I is significantly increased 1.2, 1.3, and 1.6fold more than control plants for 450, 600, and 750 mM NaCl treatment, respectively
-
glyoxlase I activity decreases in heavy metal stress (exposure to 0.5 mM CdCl2)
-
low temperature (4C) stress shows the highest induction (2.6fold) of glyoxalase I activity, followed by salinity (exposure to 400 mM NaCl) and drought (exposure to 10% (v/v) PEG) stress for 7 days
-
expression of GLO1 is induced by stress inducers such as methylglyoxal, H2O2, KCl, and NaCl
-, D6QLX5
in the human lens, GLOI activity and immunoreactivity both decrease with age
-
troglitazone downregulates GLO-1 expression
-
troglitazone treatment (0.025-0.1 mM) reduces glyoxalase I protein expression in glioma
-
activation of receptor for advanced glycation endproducts by S100A12 protein decreases the expression of glyoxalase 1
-
Gly-I activity in N-acetylcysteine-exposed cells is 40% higher than that in control cells
-
compared with the respective parental cells, hypoxia adapted-Bcr-Abl+ cells have higher levels of protein and higher enzyme activity of glyoxalase-I. High Glo-I expression is sustained in hypoxia adapted-chronic myeloid leukemia cells after 6 months in normoxia
-
glyoxylase I expression is upregulated up to 10fold at the mRNA and protein level in metastatic melanoma tissue
-
aged ovaries show a 2.9fold decreased protein level and a 1.4fold decreased RNA level of GLO1
-
GLI expression is not affected by ursolic acid
-
oleanolic acid treatments at 0.1 or 0.2% (v/v) dose-dependently enhances renal glyoxalase I activity and up-regulates renal glyoxalase I mRNA expression
-
methylglyoxal-mediated anxiolysis involves elevated expression of glyoxalase 1 in the brain, methylglyoxal treatment increases expression of GLO1 only in CD1 mice that do not have extra copies of GLO1. GLO1 expression is ubiquitously elevated in low-anxiety-related behavior-phenotype brain. Methylglyoxal injections into the lateral ventricle of hyper-anxious-related behavior-phenotype mice enhance GLO1 expression
-
high Glo1 expression is strongly associated with high anxiety-like behavior in mice
-
quantification of protein abundance in cerebellar tissue reveals, after normalization, a significant 3.9fold increase of GLO1 in 14N labeled LABs compared to 15N labeled high anxious behavior-mice
-
activity of glyoxalase I decreased under NaCl stress, at 48 h of NaCl stress the decrease is maximum
-
the expression of GLO1 is induced following treatment with Ca2+ and is dependent on the mitogen-activated protein kinase Hog1 protein and the Msn2/Msn4 transcription factors, the Ca2+-induced expression of GLO1 is enhanced in the presence of FK506
-
the expression of GLO1 is induced following treatment with Ca2+ and is dependent on the mitogen-activated protein kinase Hog1 protein and the Msn2/Msn4 transcription factors, the Ca2+-induced expression of GLO1 is enhanced in the presence of FK506
Saccharomyces cerevisiae YPH250
-
-
Gly I expression is induced by the inoculation of Fusarium graminearum in wheat spikes, the magnitude of Gly I mRNAs enhances significantly about twofold in 100 mM NaCl, however, with the increase of NaCl concentration to 150 and 500 mM, the Gly I mRNAs decrease to the similar level as control. When treated with ZnCl2, the mRNA level of Gly I in leaves increases gradually with the increase of ZnCl2 concentration
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H5Q
-
active in the presence of both Ni2+ and Zn2+
H74Q
-
the native His74 metal ligand substituted with a Gln residue, maintains a homodimeric quaternary structure in solution as does the wild-type enzyme
A111E
-
the mutation is associated with an increased risk of this neoplasia in breast cancer
E111A
-
the mutation is associated with estrogen-negative breast cancer
E172Q
-
100000fold lower activity than wild-type
E99Q
-
10000fold lower activity than wild-type
E99Q/Q33E
-
100fold lower activity than wild-type
S44A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S68A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S93A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T101A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T106A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, phosphorylation of GLO1 is completely abolished
T97A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
E161Q
-
maximum catalytic efficiency is 60% of the wild-type enzyme
E161Q/E272Q
-
maximum catalytic efficiency is 60% of the wild-type enzyme
E161Q/E345Q
-
almost completely inactivated
E161Q/R186/E272Q
-
kinetics are biphasic
E272Q
-
maximum catalytic efficiency is 60% of the wild-type enzyme
E345Q
-
kinetics are biphasic, maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5
E91Q
-
maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5
E91Q/E345Q
-
maximum catalytic efficiency is 7% of the wild-type enzyme
R22E
-
decreased substrate affinity
R22E/E91Q/E345Q
-
kinetics are monophasic, substrate binding at the high-affinity binding site A is abrogated, the mutant seems to be trapped in the conformation that predominates at lower substrate concentrations
DELTAglo1
-
glyoxalase I null mutant
E163Q
-
58% of wild-type kcat
E163Q/E318Q
-
0.02% of wild-type kcat
E318Q
-
16% of wild-type kcat
additional information
-, D6QLX5
gene GLO1 complements the glo1 mutation of Saccharomyces cerevisiae
YEpGLO1
-
overexpressing mutant, shows increased methylglyoxal resistance
additional information
-
lgl isogenic knockout mutant LGLKO, has no detectable enzyme activity, results in an acid-sensitive phenotype, glycolytic rate at pH 5.0 is higher for the mutant than for wild-type
additional information
-
lgl isogenic knockout mutant LGLKO, has no detectable enzyme activity, results in an acid-sensitive phenotype, glycolytic rate at pH 5.0 is higher for the mutant than for wild-type
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
flow cytometry method for GLO-1 detection in human leukocytes isolated from peripheral blood samples to investigate GLO-1 expression in leukocyte subsets from type 1 and 2 diabetes mellitus patients. Expression index of GLO-1-positive cells is slightly increased in mononuclear leukocytes from diabetic patients. This result correlates with the increase in GLO-1 activity in the whole blood samples of type 2 diabetes patients
medicine
-
possible role of glyoxalase I in the chemoresistance displayed by kidney tumor, possible use of glyoxalase I inhibitors as anticancer drugs, increase in glyoxalase I lowers level of the potent apoptosis activator methylglyoxal
medicine
-
glyoxalase I is critical for pericyte survival under hyperglycemic conditions, its inactivation and/or down-regulation by NO donor may contribute to pericyte death by apoptosis during early stages of diabetic retinopathy
medicine
-
decrease of glyoxalase I expression with increasing Alzheimers disease stage might be one reason for methylglyoxal-induced neuronal impairment, apoptosis, and advanced glycation end formation in plaques and tangles
medicine
-
Glo-I is a molecular target for treatment of Bcr-Abl+ leukemias and, in particular, Abl TKI-resistant quiescent Bcr-Abl+ leukemic cells that have acquired stem-like characteristics in the process of adapting to a hypoxic environment
medicine
-
polymorphisms in glyoxalase 1 gene are not associated with the prevalence of hypertension, markers of atherosclerosis and advanced glycation endproducts and are weakly associated with pulse pressure and systolic blood pressure, impaired glucose metabolism and type 2 diabetes mellitus
medicine
-
flow cytometry method for GLO-1 detection in human leukocytes isolated from peripheral blood samples to investigate GLO-1 expression in leukocyte subsets from type 1 and 2 diabetes mellitus patients. Expression index of GLO-1-positive cells is slightly increased in mononuclear leukocytes from diabetic patients. This result correlates with the increase in GLO-1 activity in the whole blood samples of type 2 diabetes patients
drug development
-, Q5XQR1
difference of the substrate specificity of the human and the Leishmania enzyme could be used for designing selective inhibitors against the parasite
drug development
-, Q68RJ8
mutually exclusive substrate specificities and substantial differences between the active sites of the Leishmania major and human GLO1 enzymes indicate that selective inhibition of LmGLO1 may be possible
drug development
-
cancer therapy, inhibitors of the glyoxalase system would be expected to suppress the growth of cancer cells and could find clinical use as anticancer drug
analysis
-
practical experiments for students to determine the effect of exposure to oxidative stress conditions on yeast glyoxalase I, investigation of kinetic parameters
drug development
-
design of a metabolically stable glyoxalase-I inhibitor, which may be useful in potentiating the antitumor activity of alpha-ketoaldehydes
drug development
-
beta-ketoesters function as a possible zinc-chelating component of Glx-I inhibitors
medicine
-
role in dental caries, LGL functions in the detoxification of methylglyoxal, resulting in increased aciduricity
medicine
-
role in dental caries, LGL functions in the detoxification of methylglyoxal, resulting in increased aciduricity
-
medicine
-
high degree of similarity between the trypanosomatid and bacterial GLO1 proteins, contrasting substrate specificities of human and trypanosomatid glyoxalase enzymes suggest that the glyoxalase system may be an attractive target for anti-trypanosomal chemotherapy
medicine
-
upregulation of glyoxalase I in diabetes, this upregulation is inadequate to normalize methylglyoxal levels, which can lead to methylglyoxal retention and chemical modification of proteins
additional information
-
GloI has two functional active sites with similar catalytic activities and pH profiles but different substrate affinities. Glu91/Glu272 and Glu345/Glu161 are isofunctional to Glu99 and Glu172 in human GloI, respectively. As a consequence, Glu91 and Glu345 are part of active site A between the N- and C-terminal domains, and Glu272 and Glu161 form active site B between the intermediate domains. Both active sites are able to adopt two different conformations and are allosterically coupled
additional information
Q9HU72
Pseudomonas aeruginosa possesses GlxI enzymes from two metal activation classes. The gloA1 and gloA2 genes encode non-Zn2+ dependent glyoxalase I enzymes and the gloA3 gene encodes a Zn2+-dependent homolog
additional information
-
is able to exist in two alternative domain-swapped forms. Active site and an essential metal binding site are disassembled and reassembled by the process of domain swapping. 3D domain swapping can be regulated by a small organic ligand
additional information
P16635
compared to control cells, transgenic cells with Pseudomonas putida glyoxalase I display a significant reduction of 35-43% in intracellular methylglyoxal and a significant decrease of 30% in extracellular methylglyoxal. Expression of Pseudomonas putida glyoxalase I in transgenic Escherichia coli markedly improves cell growth and results in a 50% increase in 1,3-propanediol production