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Information on EC 4.4.1.5 - lactoylglutathione lyase
for references in articles please use BRENDA:EC4.4.1.5
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EC Tree 4 Lyases
4.4 Carbon-sulfur lyases
4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
4.4.1.5 lactoylglutathione lyase
IUBMB Comments
Also acts on 3-phosphoglycerol-glutathione.
The enzyme appears in viruses and cellular organisms
- 4.4.1.5
-
glycation
-
detoxify
- gsh
-
dicarbonyls
- erythrocyte
- d-lactate
- adduct
- dismutase
-
endproducts
- rage
- s-transferase
- mellitus
-
methylglyoxal-induced
-
glyoxalases
-
byproduct
- hyperglycemia
-
glutathione-dependent
- phosphoglucomutase
-
metalloenzyme
- hemithioacetal
-
mg-induced
- hla-a
- aldose
- 3-deoxyglucosone
-
enediolate
-
d-lactic
-
pentosidine
-
cyclopentyl
- mdhar
- haptoglobin
- aminoguanidine
- diesters
- monodehydroascorbate
- 6-phosphogluconate
-
anti-glycation
- dehydroascorbate
-
anxiety-like
-
gsh-dependent
- pyridoxamine
- analysis
- trypanothione
- medicine
- drug development
showSynonyms
glyoxalase i, glyoxalase 1, glo-1, glo-i, glo i, glyoxalase-i, glyoxalase-1, gly-i, lactoylglutathione lyase, glyoxylase i, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldoketomutase
-
-
-
-
Glo1
GloA
GloA1
GloA2
GloA3
GloI
Glx-I
GLXI
Gly I
glyoxalase I
glyoxalase-1
glyoxalase-I
glyoxylase I
ketone-aldehyde mutase
-
-
-
-
lactoylglutathione methylglyoxal lyase
LGL
lyase, lactoylglutathione
-
-
-
-
methylglyoxalase
-
-
-
-
methylglyoxylase
-
-
-
-
S-D-lactoylglutathione methylglyoxal lyase
-
-
-
-
S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
S-D-lactoylglutathione:methylglyoxal lyase
s00004g335
STM3117
YaiA
Glo1
-
-
GLXI
-
-
-
-
glyoxalase I
-
-
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxalase I
-
-
glyoxylase I
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-S-lactoylglutathione = glutathione + 2-oxopropanal
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 + 2-oxopropanal
intramolecular hydride migration is the rate-determining step
-
(R)-S-lactoylglutathione = glutathione + 2-oxopropanal
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 + 2-oxopropanal
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 + 2-oxopropanal
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 + 2-oxopropanal
-
-
-
-
(R)-S-lactoylglutathione = glutathione + 2-oxopropanal
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 + 2-oxopropanal
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
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
addition
-
-
of RSH
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
methylglyoxal degradation I, methylglyoxal degradation VIII
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SYSTEMATIC NAME
IUBMB Comments
(R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing; glutathione-forming)
Also acts on 3-phosphoglycerol-glutathione.
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CAS REGISTRY NUMBER
COMMENTARY
9033-12-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
gamma-glutamylcysteine-methylglyoxal hemithioacetal
?
Substrates: gamma-glutamylcysteine-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
gamma-glutamylcysteine-phenylglyoxal hemithioacetal
?
Substrates: gamma-glutamylcysteine-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + 2,4-dimethylphenylglyoxal
S-(2,4-dimethyl)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + 4-bromophenylglyoxal
S-(4-bromo)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + 4-methylphenylglyoxal
S-(4-methyl)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + m-methoxyphenylglyoxal
S-(3-methoxy)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + p-hydroxyphenylglyoxal
S-(4-hydroxy)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + p-methoxyphenylglyoxal
S-(4-methoxy)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione-glyoxal hemithioacetal
?
Substrates: -
Products: -
Products: -
?
homoglutathione-methylglyoxal hemithioacetal
(R)-S-lactoylhomoglutathione
Substrates: homoglutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
homoglutathione-phenylglyoxal hemithioacetal
?
Substrates: homoglutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
methylglyoxal + glutathione
(R)S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
S-D-lactoylglutathione
Substrates: -
Products: -
Products: -
?
methylglyoxal + reduced trypanothione
S-D-lactoyltrypanothione
Substrates: -
Products: -
Products: -
?
S-D-lactoyltrypanothione
methylglyoxal + reduced trypanothione
Substrates: -
Products: -
Products: -
?
S-mandoylglutathione
glutathione + phenylglyoxal
Substrates: -
Products: -
Products: -
?
S-mandoyltrypanothione
phenylglyoxal + trypanothione
Substrates: -
Products: -
Products: -
?
trypanothione + phenylglyoxal
S-mandoyltrypanothione
-
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + 2-oxopropanal
-
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + 2-oxopropanal
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + 2-oxopropanal
Orbilia oligospora ATCC2492
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
Substrates: -
Products: -
Products: -
r
(R)-S-lactoylglutathione
glutathione + methylglyoxal
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
Substrates: -
Products: -
Products: -
r
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
Substrates: -
Products: -
Products: -
?
glutathione + 2-oxopropanal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + 2-oxopropanal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + 2-oxopropanal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
r
glutathione + 4,5-dioxovalerate
?
-
Substrates: -
Products: -
Products: -
?
glutathione + 4,5-dioxovalerate
?
-
Substrates: no activity
Products: -
Products: -
?
glutathione + glyoxal
S-glycolylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + glyoxal
S-glycolylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: glyoxalase I catalyzes the isomerization of a hemithioacetal, formed from glutathione and methylglyoxal, to lactic acid thioester
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: glyoxalase I catalyses the isomerization of the hemithioacetal formed non-enzymatically from methylglyoxal and glutathione to S-D-lactoylglutathione
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
r
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: cytosolic isozyme Glo1 is functional, but the recombinant Glo1-like protein is inactive in a standard enzyme assay
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
glutathione + methylglyoxal
?
-
Substrates: detoxification of methylglyoxal
Products: -
Products: -
?
glutathione + methylglyoxal
?
-
Substrates: detoxification of methylglyoxal
Products: -
Products: -
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
Substrates: 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
Products: -
Products: -
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
Substrates: 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
Products: -
Products: -
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
Substrates: glutathione reacts with methylglyoxal forming a hemithioacetal, and then glyoxlase I catalyses the formation of S-D-lactoylglutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
Substrates: very poor substrate, specificity constant 280fold lower than of the N1-glutathionylspermidine
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: most active with methylglyoxal
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: most active with methylglyoxal
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: the hemimercaptal adduct produced nonenzymatically from methylglyoxal and glutathione is the substrate
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: stereospecifically transfers hydrogen to form S-D-lactoylglutathione from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: the substrat is the hemithioacetal of methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: stereospecifically transfers hydrogen to form S-D-lactoylglutathione from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione + methylglyoxal
S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + p-chlorophenylglyoxal
S-(4-chloro)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + p-chlorophenylglyoxal
S-(4-chloro)mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: no activity detectable
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: no activity detectable
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: no activity
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione ethyl ester + methylglyoxal
S-lactoylglutathionyl ethyl ester
Substrates: -
Products: -
Products: -
?
glutathione ethyl ester + methylglyoxal
S-lactoylglutathionyl ethyl ester
Substrates: -
Products: -
Products: -
?
glutathione isopropyl ester + methylglyoxal
S-lactoylglutathionyl isopropyl ester
Substrates: -
Products: -
Products: -
?
glutathione isopropyl ester + methylglyoxal
S-lactoylglutathionyl isopropyl ester
Substrates: -
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: 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
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: 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
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-phenylglyoxal hemithioacetal
?
Substrates: glutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-phenylglyoxal hemithioacetal
?
-
Substrates: glutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from phenylglyoxal and glutathione
Products: -
Products: -
?
glutathionylspermidine + methylglyoxal
?
-
Substrates: most efficient substrate
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: non-enzymatic formation of hemithioacteal as substrate for gly I
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
Substrates: 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
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
Substrates: non-enzymatic formation of hemithioacetal from methylglyoxal and reduced glutathione
Products: 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
Products: 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
-
Substrates: 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
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: the hemiacetal of methylglyoxal + glutathione is used as substrate, pH 6.8, 20°C
Products: the product formation is measured by monitoring the increase of absorbance at 240 nm
Products: the product formation is measured by monitoring the increase of absorbance at 240 nm
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
Substrates: 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)
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
Substrates: -
Products: determined monitoring the increase in absorbance at 240 nm for 5 min at 25°C, pH 7.0
Products: determined monitoring the increase in absorbance at 240 nm for 5 min at 25°C, pH 7.0
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
Substrates: the hemiacetal of methylglyoxal + glutathione is used as substrate, pH 7.0, 30°C
Products: the formation is measured by monitoring the increase of absorbance at 240 nm
Products: the formation is measured by monitoring the increase of absorbance at 240 nm
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: -
Products: product measured by monitoring the increase of absorbance at 240 nm by formation of S-D-lactoylglutathione, pH 6.6, 37°C
Products: product measured by monitoring the increase of absorbance at 240 nm by formation of S-D-lactoylglutathione, pH 6.6, 37°C
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: the hemiacetal of methylglyoxal + glutathione is used as substrate, 25°C
Products: the formation is measured by monitoring the increase of absorbance at 240 nm
Products: the formation is measured by monitoring the increase of absorbance at 240 nm
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: liver homogenate, the effects of taurine, ethanol, and iron alone or in combination are analyzed, pH 7.0, 37°C
Products: -
Products: -
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: permeabilized cell suspensions, 30°C, pH 7.1
Products: formation is monitored by measuring the increase at 240 nm
Products: formation is monitored by measuring the increase at 240 nm
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione
Products: -
Products: -
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione
Products: -
Products: -
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione
Products: -
Products: -
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione, preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
Products: -
Products: -
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: two major intracelluar thiols are used, glutathione and trypanothione
Products: -
Products: -
?
N1-glutathionylspermidine + methylglyoxal
?
Substrates: specificity constant of N1-glutathionylspermidine 50fold less than of glutathione
Products: -
Products: -
?
N1-glutathionylspermidine + methylglyoxal
?
Substrates: -
Products: -
Products: -
?
trypanothione + 2 methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + 2 methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
Products: -
Products: -
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
Substrates: -
Products: -
Products: -
r
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: cell lysate, pH 7.0, 25°C
Products: the formation is measured by monitoring at 240 nm
Products: the formation is measured by monitoring at 240 nm
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: cell lysate, pH 7.0, 25°C
Products: the formation is measured by monitoring at 240 nm
Products: the formation is measured by monitoring at 240 nm
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: cell lysate of the recombinant protein, esxpression of GLO1 from Trypanosomas cruzi in Trypanosomas brucei which lacks GLO1 activity, pH 7.0, 25°C
Products: the product formation is measured by monitoring at 240 nm
Products: the product formation is measured by monitoring at 240 nm
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the calculated longer-range electrostatic attractive potential for the enzyme is centred between and above the two active sites, suggesting a possible approach trajectory for the substrate targeted initially to a position above the two active sites followed by migration to one of the two active sites allowing for enzymatic reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
-
Substrates: overexpression of the enzyme completely prevents both hyperglycemia-induced advanced glycation products from methylglyoxal and increased macromolecular endocytosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: Glo1 is the major cellular enzyme that catalyzes the metabolism of methylglyoxal and thereby protects against dicarbonyl glycation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the Leishmania sp. glxI preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: spectrophotometric measurement of enzyme activity in tissue and cell culture, modified for use with a UV-transparent microplate for higher sample throughput, method, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
Substrates: GLO1 is required for osteoclastogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
Products: -
Products: -
?
additional information
?
-
-
Substrates: major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase I activity is involved in the detoxification of toxic metabolites produced during lipid peroxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: study of the pathophysiological role of glyaylase I as an methylglyxal detoxifier in rat ischemia-reperfusion (I/R) injury
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase I catalyzes the isomerization reaction of thiohemiacetal, which is formed nonenzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase I activity is measured spectrophotometrically by S-D-lactoylglutathione formation at 240 nm
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with glutathione analogs
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glutathione-glyoxal hemithioacetal
?
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
Substrates: 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
Products: -
Products: -
?
trypanothione + 2 methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + 2-oxopropanal
-
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + 2-oxopropanal
Substrates: -
Products: -
Products: -
?
(R)-S-lactoylglutathione
glutathione + 2-oxopropanal
Orbilia oligospora ATCC2492
Substrates: -
Products: -
Products: -
?
glutathione + 2-oxopropanal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + 2-oxopropanal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
Substrates: -
Products: -
Products: -
r
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
glutathione + methylglyoxal
?
-
Substrates: detoxification of methylglyoxal
Products: -
Products: -
?
glutathione + methylglyoxal
?
-
Substrates: detoxification of methylglyoxal
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: 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
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: 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
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
Substrates: glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: -
Products: -
Products: -
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system
Products: -
Products: -
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
Substrates: first step in the glyoxalase system, detoxification of methylglyoxal
Products: -
Products: -
r
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: overexpression of the enzyme completely prevents both hyperglycemia-induced advanced glycation products from methylglyoxal and increased macromolecular endocytosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: Glo1 is the major cellular enzyme that catalyzes the metabolism of methylglyoxal and thereby protects against dicarbonyl glycation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the Leishmania sp. glxI preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
Products: -
Products: -
?
additional information
?
-
Substrates: GLO1 is required for osteoclastogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
Products: -
Products: -
?
additional information
?
-
-
Substrates: major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase I activity is involved in the detoxification of toxic metabolites produced during lipid peroxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: study of the pathophysiological role of glyaylase I as an methylglyxal detoxifier in rat ischemia-reperfusion (I/R) injury
Products: -
Products: -
?
additional information
?
-
-
Substrates: glyoxalase I catalyzes the isomerization reaction of thiohemiacetal, which is formed nonenzymatically from methylglyoxal and glutathione
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
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additional information
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Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
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additional information
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Substrates: the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Co2+
CuSO4
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+
methylglyoxal
10 mM, enhanced tolerance to toxic stress in transgenic Vigna mungo
Mg2+
Mn2+
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+
Zn2+
additional information
Cd2+
activation, Km: 0.0089 mM, Vmax: 0.043 mmol/min/mg, kcat: 21 1/s
Cd2+
-
can partially substitute for Zn2+, the proton-transfer step is partially rate-limiting for the Cd2+ -substituted enzyme utilizing alpha-deuterophenylglyoxal as substrate
Cd2+
-
in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Cd2+
reactivates GloA3 by 87% after treatment with dipicolinic acid
Co2+
activation, Km: 0.012 mM, Vmax: 0.213 mmol/min/mg, kcat: 106 1/s
Co2+
GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies
Co2+
-
1 mM, increases activity more than 100%. 1 mM restores 80% of the activity of the apoenzyme
Co2+
-
in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Co2+
increases GloA2 activity, hyper-reactivates GloA3 by 115% after treatment with dipicolinic acid
Co2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Fe2+
-
at least one iron per enzyme molecule, the second metal is zinc or manganese, apparantly depending on growth conditions
Mg2+
-
incubation of the Zn2+ depleted apoenzyme with Mg2+ restores 50% of the enzyme activity
Mg2+
reactivates GloA3 by 26% after treatment with dipicolinic acid
Mn2+
-
in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Mn2+
hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
Ni2+
-
required for activity, dependent on, Ni2+ -activation class, the active Ni2+ -bound enzyme has an octahedral geometry
Ni2+
highest reactivation activity, Km: 0.027 mM, Vmax: 0.676 mmol/min/mg, kcat: 338 1/s
Ni2+
GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies
Ni2+
-
activates, Ni2+ -activation class, only one Ni2+ is needed for full enzyme activation
Ni2+
-
in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Ni2+
dependent on, required for activity, Glu145 and Glu209 are involved in Ni2+ binding, Glu78 is not involved, the monomeric enzyme possesses a single Ni2+ coordination site despite containing two GLY I domains, 0.052 mol/mol enzyme for the recombinant enzyme expressed in Escherichia coli, and 1.258 mol/mol enzyme after exogenous addition of Ni2+
Ni2+
activation, Km: 0.032 mM, vmax: 0.571 mmol/min/mg, kcat: 271 1/s, kcat/Km: 8500000 1/M * s
Ni2+
activation, Km: 0.021 mM, Vmax: 0.497 mmol/min/mg, kcat: 247 1/s, kcat/Km: 12000000 1/M * s
Ni2+
increases GloA2 activity, hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
Ni2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Zn2+
4fold higher glyoxalase I activity when glyoxalase is isolated from Zn2+-grown bacteria
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+
-
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+
-
activates, Zn2+ -activation class. Presence of two active sites, with each active-site Zn2+ ion bound by two amino acid residues from one subunit and two other residues from the second subunit. Water molecules are proximal to the Zn2+ centre. The presence of a repeating betalphabetabetabeta secondary-structural motif is discovered in the molecular structure
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+
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+
activation of gloA3, metal ion binds tightly to the enzyme so that removal of metall ion requires more forceful conditions
Zn2+
does not increase GloA2 activity, GloA3 contains Zn2+, reactivates GloA3 by 76% after treatment with dipicolinic acid
Zn2+
-
two zinc ions per dimer. The zinc is required for structure and function. The monomer contains a single zinc ion
Zn2+
-
apoenzyme is catalytically inactive, but is partially restored by Zn2+
Zn2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
additional information
-
no activation by Zn2+, trigonal bipyramidal geometry of the inactive Zn2+ -bound enzyme. The octahedral metal ligand geometry appears to be mechanistically quintessential to Glo1 enzymatic activity, regardless of the Glo1 metal-activation class
additional information
no activation by Zn2+, poor activity with Ca2+ and Mg2+, the active site geometry of the Ni2/Co2-activated enzyme forms an octahedral coordination with one metal atom, two water molecules, and four metal-binding ligands, while the inactive Zn2-bound enzyme form possesses a trigonal bipyramidal geometry with only one water molecule liganded to the metal center
additional information
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no activation by Zn2+, poor activity with Ca2+ and Mg2+, the active site geometry of the Ni2/Co2-activated enzyme forms an octahedral coordination with one metal atom, two water molecules, and four metal-binding ligands, while the inactive Zn2-bound enzyme form possesses a trigonal bipyramidal geometry with only one water molecule liganded to the metal center
additional information
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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
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
-
no activation by Ni2+. The two metals stabilize the transition state, possibly an enediol(ate)-like transition state, to different extents and/or there is a differential contribution to a mechanism that requires exchange of the water ligands on the metal with the oxygens of the substrate hemithioacetal, homodimeric in nature with two subunits identified in the structure,with each active site being formed by residues from each of the two subunits and two water (or hydroxide) molecules completing the octahedral metal-co-ordination environment
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
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Mg2+, Ca2+, Zn2+ no increase in enzyme activity
additional information
no activating effect by Zn2+, Ca2+, Fe2+, and Mn2+
additional information
-
Mg2+, Ca2+, Zn2+ no increase in enzyme activity
additional information
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broad metal-activation profile of the enzyme, the mechanism probably involves the formation of an enediol(ate) reaction intermediate
additional information
no activation by Zn2+
additional information
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no activation by Zn2+
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INHIBITOR
ORGANISM
UNIPROT
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-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-hydroxy-6-(1-pentyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-[1-(2-methoxyethyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-[1-(3-methoxypropyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
-
-
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
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-indol-1-yl]methyl]benzamide
-
-
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-pyrrolo[2,3-b]pyridin-1-yl]methyl]benzamide
-
-
4,6-diphenyl-N-hydroxypyridone
-
a lead compound for non-peptidic inhibitor screening against glyoxalase I
4-bromoacetoxy-1-(S-glutathionyl)-acetoxy butane
-
competitive inhibition of GLO1, the inhibitor is able to covalently bind to the free sulfhydryl group of Cys60 in the hydrophobic binding pocket adjacent to the enzyme active site and partially inactivate the enzyme, no complete inhibition, binding structure analysis, overview
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
6-(1-butyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-1-hydroxy-4-phenylpyridin-2(1H)-one
-
-
buthionine sulfoximine
-
58% loss in Gly-I activity by 0.05 mM buthionine sulfoximine
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
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
flavone
IC50 wild type 56 microM, IC50 enzyme overexpressor 69 microM
gerfelin
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C
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
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
isolupalbigenin
treatment of HL-60 cells leads to significant accumulation of substrate methylglyoxal and the caspase 3 activity of the cell lysate increases. Compound shows anti-proliferative activity against HL-60 cells
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
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
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
rutin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
S-(N-hydroxy-N-p-iodophenylcarbamoyl) glutathione
tight binding competitive inhibitor of human GLOI
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-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-p-bromobenzyl glutathione
-
competitive inhibitor, unstable toward gamma-glutamyltranspeptidase
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, 30°C
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
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
-
-
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
1,10-phenanthroline
-
2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
1-Naphthaleneacetic acid
-
activity decreases by approximately 50% during differentiation in Brassica sp. gly I
1-Naphthaleneacetic acid
-
activity decreases by approximately 50% during differentiation in Brassica sp. gly I
benzyladenine
-
activity decreases by approximately 50% during differentiation in Brassica sp. gly I
benzyladenine
-
activity decreases by approximately 50% during differentiation in Brassica sp. gly I
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
curcumin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, pH 7.0, 30°C, more efficient inhibition of GLO1 compared to quercetin, myricetin, kaempferol, luteolin, or rutin as inhibitor, results in a decrease of D-lactate release
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
EDTA
-
0.1 mM, approx. 50% inactivation after 50 min, approx. 80% inhibition after 250 min
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
kaempferol
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
Lapachol
IC50 wild type 93 microM, IC50 enzyme overexpressor 96 microM
luteolin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
methyl gerfelin
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30°C
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
methylglyoxal
-
addition at pH 7.0 results in a modest 28% decrease in the glycolytic rate
MS-3
-
inhibitor produced by a mushroom Stereum hirsutum; mechanism of inhibition
myricetin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
myricetin
-
substrate transition-state (Zn2+-bound methylglyoxal-glutathione hemithioacetal) mimetic inhibitor
purpurogallin
IC50 wild type 70 microM, IC50 enzyme overexpressor 132 microM
quercetin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
quercetin
IC50 wild type 26 microM, IC50 enzyme overexpressor 27 microM
S-4-bromobenzylglutathionylspermidine
-
potent linear competitive inhibitor, selectively inhibits trypanosomatid GLO1 activity
S-hexylglutathione
-
slows degradation of the wild-type enzyme and mutant E161Q/E345Q in comparison with uncomplexed protein
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
Zn2+
inactivation of gly I, metal can bind to the enzyme gly I, but the resulting enzyme is inactive
Zn2+
inactivation of gloA1; inactivation of gly I
additional information
-
substrate-analogue inhibitors and transition-state inhibitors
-
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
-
posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity
-
additional information
-
design of 4-(7-azaindole)-substituted 6-phenyl-N-hydroxypyridones, thermodynamic binding parameters, binding modeling using the enzyme's crystal structure, overview. Inhibitory activity of 6-phenyl-N-hydroxypyridones with various substituents at 4-position
-
additional information
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
-
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
-
tight-binding inhibitors are very potent against the recombinant enzyme
-
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
-
monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
-
additional information
-
no change in glyoxalase I activity in taurine-treated rats
-
additional information
-
substrate-analogue inhibitors and transition-state inhibitors
-
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
-
additional information
-
S-4-bromobenzylglutathione is inactive as inhibitor
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
enhances slightly glyoxalase I activity, dose-dependently 0-2 g/l, pH 6.6, 37°C
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
light
-
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
-
methylglyoxal
-
addition at pH 5.0 results in a significant 98% increase in the glycolytic rate
S-ethyl cysteine
-
enhances significantly glyoxalase I activity, dose-dependently 0-2 g/l, pH 6.6, 37°C
S-propyl-cysteine
-
enhances significantly glyoxalase I activity, dose-dependently 0-2 g/l, pH 6.6, 37°C
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
-
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
-
the octahedral metal ligand geometry appears to be mechanistically quintessential to Glo1 enzymatic activity, regardless of the Glo1 metal-activation class
-
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
-
glyoxalase I protein amounts are 1.5fold increased in early Alzheimers disease subjects
-
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
-
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
-
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
-
1.21 mg/kg crayfish, selenium-enriched diet, female crayfish, results in a tendency to an increased enzyme activity
-
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
activity of glyoxalase I in transgenic Escherichia coli with Pseudomonas putida glyoxalase I under anaerobic conditions is 12fold higher than that in control cells
-
additional information
-
activity of glyoxalase I in transgenic Escherichia coli with Pseudomonas putida glyoxalase I under anaerobic conditions is 12fold higher than that in control cells
-
additional information
-
no change in glyoxalase I activity in taurine-treated rats, 2% (w/v)
-
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
-
additional information
-
not activating: incubation of purified enzyme with 0-300 mM glycerol in vitro
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
4-bromophenylglyoxal, 4-methylphenylglyoxal
-
liver or erythrocyte enzyme
-
0.0284
reduced trypanothione
recombinant enzyme, pH 7.2, room temperature
0.0998
(R)-S-lactoylglutathione
recombinant enzyme, pH 7.2, temperature not specified in the publication
7.6
glutathione-methylglyoxal hemithioacetal
25°C, pH 7.0, native Glb33
11
glutathione-methylglyoxal hemithioacetal
25°C, pH 7.0, recombinant Glb33
0.362
methylglyoxal
presence of Zn2+, 37°C, pH 6.6
0.406
methylglyoxal
presence of Ni2+, 37°C, pH 6.6
0.588
methylglyoxal
presence of Co2+, 37°C, pH 6.6
1.03
methylglyoxal
-
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
1.9
methylglyoxal
37°C, pH 6.6
0.064
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
0.148
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
additional information
(R)-S-lactoylglutathione
more than 1.9, purified enzyme, pH 7.0, 27°C
additional information
(R)-S-lactoylglutathione
-
more than 1.9, purified enzyme, pH 7.0, 27°C
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
reaction will be diffusion-limited under subsaturating conditions
-
additional information
additional information
-
the KM value with Ni2+ is 0.027 mM
-
additional information
additional information
the KM value with Ni2+ is 0.027 mM
-
additional information
additional information
-
the KM value with Co2+ is 0.012 mM
-
additional information
additional information
the KM value with Co2+ is 0.012 mM
-
additional information
additional information
-
the KM value with Cd2+ is 0.0089 mM
-
additional information
additional information
the KM value with Cd2+ is 0.0089 mM
-
additional information
additional information
-
the KM value with Mn2+ is 0.01 mM
-
additional information
additional information
the KM value with Mn2+ is 0.01 mM
-
additional information
additional information
-
the KM value with Fe2+ is 0.01 mM
-
additional information
additional information
the KM value with Fe2+ is 0.01 mM
-
additional information
additional information
-
the KM value of Pseudomonas aeruginosa gloaA1 with Ni2+ is 0.032 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA1 with Ni2+ is 0.032 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA1 with Ni2+ is 0.032 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA1 with Ni2+ is 0.032 mM
-
additional information
additional information
-
the KM value of Pseudomonas aeruginosa gloaA2 with Ni2+ is 0.021 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA2 with Ni2+ is 0.021 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA2 with Ni2+ is 0.021 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA2 with Ni2+ is 0.021 mM
-
additional information
additional information
-
the KM value of Pseudomonas aeruginosa gloaA3 with Zn2+ is 0.287 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA3 with Zn2+ is 0.287 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA3 with Zn2+ is 0.287 mM
-
additional information
additional information
the KM value of Pseudomonas aeruginosa gloaA3 with Zn2+ is 0.287 mM
-
additional information
additional information
-
the monomeric enzyme has two different active sites with similar kcat values, but distinct Km values
-
additional information
S-mandoylglutathione
more than 0.08, purified enzyme, pH 7.0, 27°C
additional information
S-mandoylglutathione
-
more than 0.08, purified enzyme, pH 7.0, 27°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
70.96
(R)-S-lactoylglutathione
recombinant enzyme, pH 7.2, temperature not specified in the publication
258.3
glutathione
-
the apparent kinetic parameters are determined by using hemithioacetal as substrate, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal
83
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
1590
N-[3-[(4-aminobutyl)amino]propyl]-L-gamma-glutamyl-L-cysteinylglycine
-
additional information
additional information
-
the turnover number with Ni2+ is 338 s
-
additional information
additional information
the turnover number with Ni2+ is 338 s
-
additional information
additional information
-
the turnover number with Co2+ is 106 s
-
additional information
additional information
the turnover number with Co2+ is 106 s
-
additional information
additional information
-
the turnover number with Cd2+ is 21 s
-
additional information
additional information
the turnover number with Cd2+ is 21 s
-
additional information
additional information
-
the turnover number with Mn2+ is 60 s
-
additional information
additional information
the turnover number with Mn2+ is 60 s
-
additional information
additional information
-
the turnover number with Fe2+ is 56 s
-
additional information
additional information
the turnover number with Fe2+ is 56 s
-
additional information
additional information
-
the turnover number of Pseudomonas aeruginosa gloaA1 with Ni2+ is 271 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA1 with Ni2+ is 271 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA1 with Ni2+ is 271 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA1 with Ni2+ is 271 s
-
additional information
additional information
-
the turnover number of Pseudomonas aeruginosa gloaA2 with Ni2+ is 247 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA2 with Ni2+ is 247 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA2 with Ni2+ is 247 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA2 with Ni2+ is 247 s
-
additional information
additional information
-
the turnover number of Pseudomonas aeruginosa gloaA3 with Zn2+ is 787 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA3 with Zn2+ is 787 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA3 with Zn2+ is 787 s
-
additional information
additional information
the turnover number of Pseudomonas aeruginosa gloaA3 with Zn2+ is 787 s
-
additional information
additional information
-
the monomeric enzyme has two different active sites with similar kcat values, but distinct Km values
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7100
(R)-S-lactoylglutathione
recombinant enzyme, pH 7.2, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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, 30°C
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, 30°C
0.0026
(1E,6E)-4-(3-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30°C
0.0032
(1E,6E)-4-(4-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
pH 7.1, 30°C
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, 30°C
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, 30°C
0.00015
gerfelin
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C
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, 30°C
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, 30°C
0.00023
methyl gerfelin
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30°C
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, 30°C
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
-
-
0.023
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, 30°C
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, 30°C
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, 30°C
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, 30°C
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, 30°C
0.0005
S-4-bromobenzylglutathionylspermidine
-
pH and temperature not specified in the publication
0.005
S-4-bromobenzylglutathionylspermidine
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
(3Z)-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid
Homo sapiens
-
pH 7.0, 25°C
0.00828
1'-hydroxy-6'-phenyl-3,4'-bipyridin-2'(1'H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00119
1-hydroxy-4,6-diphenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00028
1-hydroxy-4-phenyl-6-(1H-pyrrolo[2,3-b]pyridin-5-yl)pyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00051
1-hydroxy-6-(1-pentyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
1-hydroxy-6-(1H-indol-5-yl)-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00152
1-hydroxy-6-phenyl-4-(thiophen-3-yl)pyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00813
1-hydroxy-6-phenyl-4-[4-(trifluoromethyl)phenyl]pyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
1-hydroxy-6-[1-(2-methoxyethyl)-1H-indol-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000014
1-hydroxy-6-[1-(2-methoxyethyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
1-hydroxy-6-[1-(3-methoxypropyl)-1H-indol-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000011
1-hydroxy-6-[1-(3-methoxypropyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0546
2-([(4-methoxyphenyl)carbonyl]amino)-1-benzothiophene-3-carboxylic acid
Homo sapiens
-
pH 7.0, 25°C
0.00048
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-indol-1-yl]methyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
3-[[5-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-1H-pyrrolo[2,3-b]pyridin-1-yl]methyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0084
4-(biphenyl-4-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.01
4-(but-1-yn-1-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.01
4-butyl-1-hydroxy-6-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
6-(1-butyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-1-hydroxy-4-phenylpyridin-2(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.09
6-sulfamoylsaccharin
Homo sapiens
-
pH and temperature not specified in the publication
-
0.011
baicalein
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.0206
kaempferol
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.007
luteolin
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.021
S-(p-bromobenzyl)glutathione
Homo sapiens
-
pH and temperature not specified in the publication
0.023
S-p-bromobenzylglutathione
Homo sapiens
calculated, effectively inhibits rhGLO I at 25°C, pH 7.0
0.00056
myricetin
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.0032
quercetin
Homo sapiens
indicate that the hydroxy groups at the B ring of flavonoids contribute to the human GLO I inhibitory activity of the flavonoid compounds at 25°C, pH 7.0
0.026 - 0.027
quercetin
Leishmania donovani
IC50 wild type 26 microM, IC50 enzyme overexpressor 27 microM
0.00006
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
Plasmodium falciparum
-
IC50 0.06 microM
0.00011
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
Plasmodium falciparum
-
IC50 0.11 microM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.023
-
recombinant protein, expressed in Trypanosoma brucei which lacks GLO1 activity, procyclic form, pH 7.0, 25°C
0.038
-
recombinant protein, expressed in Trypanosoma brucei which lacks GLO1 activity, bloodstream form, pH 7.0, 25°C
0.172 - 180
-
without addition of S-ethyl cysteine, s-propyl-cysteine, or ascorbic acid, pH 6.6, 37°C
0.184
-
slightly increased activity compared to enzyme assay without ascorbic acid, pH 6.6, 37°C
0.19
-
slightly increased activity compared to enzyme assay without ascorbic acid, pH 6.6, 37°C
0.218
-
in the presence of 1 g/l S-ethyl cysteine, 1.2fold higher activity than without S-ethyl cysteine, pH 6.6, 37°C
0.221
-
in the presence of 1 g/l S-propyl-cysteine, 1.3fold higher activity than without S-ethyl cysteine, pH 6.6, 37°C
0.247
-
in the presence of 2 g/l S-ethyl cysteine, 1.4fold higher activity than without S-ethyl cysteine, pH 6.6, 37°C
0.258
-
in the presence of 2 g/l S-propyl-cysteine, 1.5fold higher activity than without S-ethyl cysteine, pH 6.6, 37°C
0.34
micromol/min/mg protein, native enzyme from crude lysate, pH 7.2, room temperature
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
120
purified recombinant enzyme with Ni2+ addition, pH 7.2, temperature not specified in the publication
13.34
-
addition of 6 g/kg ethanol and 2% (w/v) taurine, 79% activity of control without ethanol and taurine
15.62
-
addition of 2% (w/v) taurine, 102% activity of control without ethanol, iron, or taurine
3400
micromol/min/mg protein, recombinant enzyme, pH 7.2, room temperature
390
571
618
8.3
purified recombinant enzyme without metal ion, pH 7.2, temperature not specified in the publication
8.69
-
addition of 6 g/kg ethanol and iron, 57% activity of control without ethanol and iron
additional information
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
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
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
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
-
the GLO1 activity of the transformed Vigna mungo plants is higher than in the untransformed control plants
additional information
the GLO1 activity of the transformed Vigna mungo plants is higher than in the untransformed control plants
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
-
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
40 nmol/min/mg Leishmania major extract, trypanothione, pH 7.0, 27°C. Below 5 nmol/min/mg Leishmania major extract, pH 7.0, 27°C
additional information
-
40 nmol/min/mg Leishmania major extract, trypanothione, pH 7.0, 27°C. Below 5 nmol/min/mg Leishmania major extract, pH 7.0, 27°C
additional information
23 U/mg protein wild type, 19 U/mg protein ectopic control mutant Gox1-2
additional information
-
23 U/mg protein wild type, 19 U/mg protein ectopic control mutant Gox1-2
additional information
-
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
additional information
-
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
-
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
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
-
Vmax methylglyoxal purified enzyme 2 mmol/min/mg protein, Vmax phenylglyoxal 0.197 mmol/min/mg protein, pH 7.0, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.5
6.6
7.5
7.8
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
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pH RANGE
ORGANISM
UNIPROT
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
5.8 - 8.2
-
pH 5.8: about 30% of maximal activity, pH 8.2: about 85% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
additional information
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
calculated from sequence, 30fold upregulated protein spot in the 2D-electrophoresis, identified as glyoxalase I, the expression is regulated by the operon yahCD-yaiAB
additional information
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Trypanosoma brucei
causative agent of onchocerciasis, GloI expression is induced by oxidative stress
-
-
brenda
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
-
-
brenda
glyoxalase I expression is induced during salt stress
SwissProt
brenda
-
-
-
brenda
two isoforms of glyoxalase I showing different electrophoretic properties result from a change in one amino acid residue at psotion 11 (Ala/Gln)
-
-
brenda
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
-
-
brenda
subsp. japonica, gene GLX-I or LOC_Os08g09250
UniProt
brenda
active cytosolic glyoxalase 1, inactive glyoxalase 1-like protein
-
-
brenda
-
-
-
brenda
-
37413, 37421, 37431, 37433, 37434, 37437, 37439, 37446, 37450, 37451, 37452, 37455, 649441, 652123, 653582, 653583, 678641, 678673, 707439, 729177
-
-
brenda
strains BY4741, null mutant DELTAglo1, and overexpressed strain YEpGLO1
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is absent from the necrotic core of atherosclerotic plaques
brenda
in situ hybridization experiments, Purkinje cells in the cerebellum express GLO1 mRNA strongly and specifically
brenda
in situ hybridization experiments, highest expression at postnatal day 14
brenda
in situ hybridization experiments, highest expression at postnatal day 14
brenda
in situ hybridization experiments, lining the third ventricle and choroid plexus
brenda
in situ hybridization experiments, highest expression at postnatal day 14
brenda
transcription level and glyoxalase I activity are higher in pathological tissues than in normal ones
brenda
in situ hybridization experiments, highest expression at postnatal day 14
brenda
-
found to be conserved in tubers among different potato variants
brenda
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
brenda
additional information
-
aortic sinus derived from apolipoprotein-E-knockout mouse on a high-fat diet for 6 months, enzyme expression is restricted to a subset of cells
brenda
-
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
brenda
-
GLOI is mainly localized in the anterior epithelium but the enzyme is diffusely present in outer cortical and nuclear regions of the human lens
brenda
-
glyoxalase I activity and mRNA levels are elevated in diabetic lenses
brenda
-
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
brenda
-
preferentially accumulated in phloem and sieve cells
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
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
brenda
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
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
additional information
-
renal carcinoma cell, clear cell adenocarcinoma, 9fold increase in the transcription levels of glyoxalase I compared with pair-matched noncancerous tissues
brenda
additional information
renal carcinoma cell, clear cell adenocarcinoma, 9fold increase in the transcription levels of glyoxalase I compared with pair-matched noncancerous tissues
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
additional information
-
LE cell, lens epithelial cells, activity of the enzyme in hyperglycemic conditions is nearly 20% higher than in control conditions
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
additional information
-
ischemia/reperfusion induces the reduction of GLO I activity in the kidney, which is asssociated with morphological damage and renal dysfunction
brenda
additional information
-
permeabilized cells of Saccharomyces cerevisiae, with 0.01% (w/v) digitonin
brenda
additional information
-
present in all types of cells and tissues
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
additional information
-
gly I is present in all types of cells and tissues
brenda
additional information
-
in the bloodstream and procyclic form of the recombinant protein of Trpypanosomas brucei, overexpressed with GLO1 of Trypanosomas cruzi
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
bound to outer membrane
brenda
-
bound to outer membrane
-
brenda
additional information
-
the enzyme does not localize to glycosomes and has no peroxisome-targeting signal
-
brenda
additional information
-
the enzyme does not localize to glycosomes and has no peroxisome-targeting signal
-
brenda
additional information
-
the enzyme does not localize to glycosomes and has no peroxisome-targeting signal
-
brenda
additional information
-
the enzyme does not localize to glycosomes and has no peroxisome-targeting signal
-
brenda
additional information
-
the parasite genome encodes 2 glyoxalases I, a cytosolic isoform, and a Glo1-like protein that localizes to the apicoplast
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
homology-based structural modeling, overview
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
-
regarding the quaternary structure, the monomeric enzyme probably resulted from a second gene-duplication event in the course of evolution
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
malfunction
-
nondiabetic GLO1-knockdown mice demonstrate increased 20S methylglyoxal modification resulting in impaired proteasomal activity
malfunction
-
GLO I heterozygous mutants exhibit reduced methylglyoxal detoxification
malfunction
-
increased methylglyoxal levels, resulting from decreased enzyme activity, induce apoptosis in fully differentiated podocytes, as well as in endothelial cells and macrophages in hypoxic regions of atherosclerotic arteries
malfunction
-
increased methylglyoxal levels, resulting from decreased enzyme activity, induce apoptosis in fully differentiated podocytes, as well as in endothelial cells and macrophages in hypoxic regions of atherosclerotic arteries
metabolism
-
the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
-
the enzyme acts in a system with glyoxalase 2 and glutathione. The allosteric regulation of the high-activity and the high-affinity conformation of the enzyme might be an adaptation to altered methylglyoxal fluxes
metabolism
-
the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and glutathione
metabolism
-
the conversion of methylglyoxal into lactic acid depends on the isomerase Glo1 (glyoxalase I), the thioesterase Glo2 (glyoxalase II) and reduced glutathione (GSH) as a coenzyme, together they compose the glyoxalase system
metabolism
the glyoxalase system catalyzes the conversion of toxic, metabolically produced 2-oxoaldehydes, such as methylglyoxal, into their corresponding nontoxic 2-hydroxycarboxylic acids, leading to detoxification of these cellular metabolites
metabolism
the glyoxalase system constitutes the major pathway for the detoxification of metabolically produced cytotoxin methylglyoxal into a non-toxic metabolite D-lactate
metabolism
-
glyoxalase I is the first enzyme of the methylglyoxal detoxification pathway
metabolism
-
the glyoxalase system is composed of glyoxalase I, glyoxalase II, and glutathione as cofactor
metabolism
-
the glyoxalase system is composed of glyoxalase I, glyoxalase II, and glutathione as cofactor
metabolism
-
the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
-
the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
-
the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
-
the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
-
the enzyme is the critical regulator for lactoylglutathione and lysine lactoylation
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
-
the enzyme is essential and contributes to the detoxification of (exogenous) methylglyoxal
physiological function
-
malaria parasites are expected to require a functional glyoxalase system to prevent the potentially toxic accumulation of methylglyoxal and advanced glycation end-products
physiological function
the glyoxalase system catalyzes the conversion of toxic, metabolically produced 2-oxoaldehydes, such as methylglyoxal, into their corresponding nontoxic 2-hydroxycarboxylic acids, leading to detoxification of these cellular metabolites
physiological function
-
the glyoxalase pathway is responsible for conversion of cytotoxic methylglyoxal to D-lactate. Methylglyoxal toxicity arises from its ability to form advanced glycation end products on proteins, lipids and DNA
physiological function
-
methylglyoxal is a key player in vascular dysfunction, particularly due to its capacity to induce the formation of oxidative stress, cell death andendothelial dysfunction, glyoxylase I is the rate-limiting enzyme in the glyoxalase system for detoxifcation of methylglyoxal, accumulation of methylglyoxal and methylglyoxal-derived advanced glycation end-products may be a major contributing factor to atherosclerotic plaque rupture. Intracellular accumulation of methylglyoxal in endothelial cells causes dysfunction as indicated by expression of adhesion molecules such as vascular cell adhesion molecule 1 expression, which can be prevented by Glo1 overexpression
physiological function
-
the enzyme is part of the glyoxylate system, whose function is to detoxify reactive metabolites, which mainly accumulate during hyperglycaemic metabolism, major substrate is methylglyoxal. The mean glyoxalase I activity of atherosclerotic tissue from aortic and coronary artery samples is significantly reduced compared with healthy tissue derived from the same vessel, indicating a role for glyoxalase I in atherogenesis, the enzyme plays a role in inflammatory response, hypertension, and diabetic microvascular complications, overview
physiological function
-
the enzyme is part of the glyoxylate system, whose function is to detoxify reactive metabolites, which mainly accumulate during hyperglycaemic metabolism, major substrate is methylglyoxal. The mean glyoxalase I activity of atherosclerotic tissue from aortic and coronary artery samples is significantly reduced compared with healthy tissue derived from the same vessel, indicating a role for glyoxalase I in atherogenesis, the enzyme plays a role in inflammatory response, hypertension, and diabetic microvascular complications, overview
physiological function
-
the enzyme is essential and contributes to the detoxification of (exogenous) methylglyoxal
physiological function
overexpression in Vigna mungo driven by a constitutive Cestrum yellow leaf curling viral promoter. Transgenic plants show improved survival under salt stress. The higher level of Glyoxalase I activity in transgenic lines is directly correlated with their ability to withstand salt stress
physiological function
-
a mutant deficient in glyoxylase I is more sensitive to methylglyoxal and also more susceptible to human neutrophil killing. Inhibition of neutrophil myeloperoxidase rescues the gloA-deficient mutant. The mutant strain is slower at disseminating into the blood in the murine model
physiological function
a deletion mutant exhibits a notable growth inhibition coupled with oxidative DNA damage and membrane disruptions. Growth of the mutant in glucose minimal medium does not result in any inhibition. Endogenous expression of recombinant Lgl in serovar Typhi leads to an increased resistance and growth in presence of external methylglyoxal
physiological function
the enzyme is very important for Arthrobotrys oligospora to resist soil fungistasis and to detoxify methylglyoxal
physiological function
-
Arabidopsis plants overexpressing isoform GLYI11 possess increased capacities to tolerate freezing temperatures
physiological function
-
a deletion mutant exhibits a notable growth inhibition coupled with oxidative DNA damage and membrane disruptions. Growth of the mutant in glucose minimal medium does not result in any inhibition. Endogenous expression of recombinant Lgl in serovar Typhi leads to an increased resistance and growth in presence of external methylglyoxal
-
physiological function
-
a mutant deficient in glyoxylase I is more sensitive to methylglyoxal and also more susceptible to human neutrophil killing. Inhibition of neutrophil myeloperoxidase rescues the gloA-deficient mutant. The mutant strain is slower at disseminating into the blood in the murine model
-
physiological function
Orbilia oligospora ATCC2492
-
the enzyme is very important for Arthrobotrys oligospora to resist soil fungistasis and to detoxify methylglyoxal
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14251
-
x * 14251, electrospray ionization mass spectrometry, x * 14251, calculated
14833
-
x * 14833, electrospray ionization mass spectrometry, x * 14834, calculated
14834
-
x * 14833, electrospray ionization mass spectrometry, x * 14834, calculated
15669
-
x * 15669, electrospray ionization mass spectrometry, x * 15669, calculated
15818
2 * 15818, His6-tagged enzyme, sequence calculation, the enzyme forms two active sites, each within single subunits
16000
16647
-
x * 17000, SDS-PAGE or Western blot analysis, x * 16647, predicted, x * 16650, MALDI-TOF-MS analysis
16650
-
x * 17000, SDS-PAGE or Western blot analysis, x * 16647, predicted, x * 16650, MALDI-TOF-MS analysis
17000
-
x * 17000, SDS-PAGE or Western blot analysis, x * 16647, predicted, x * 16650, MALDI-TOF-MS analysis
20647
-
2 * 20647, sequence calculation, 2 * 21000, recombinant enzyme, SDS-PAGE
20810
2 * 20810, calculated from sequence, MALDI-TOF mass spectrometry, SDS-PAGE
21000
23000
24000
25000
26000
27000
29000
33000
34000
36000
37000
38000
42000
43000
43310
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
46000
48000
58000
60000
additional information
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
-
Western blot analysis of whole cell lysate, equivalent to the predicted molecular mass
21000
-
2 * 20647, sequence calculation, 2 * 21000, recombinant enzyme, SDS-PAGE
additional information
-
size is similar to the Escherichia coli enzyme and to Pseudomonas aeruginose Glx1 GloA1
additional information
size is similar to the Escherichia coli enzyme and to Pseudomonas aeruginose Glx1 GloA1
additional information
size is similar to the Escherichia coli enzyme and to Pseudomonas aeruginose Glx1 GloA1
additional information
size is similar to the Escherichia coli enzyme and to Pseudomonas aeruginose Glx1 GloA1
additional information
-
GlxI is longer than the Escherichia coli enzyme but similar to the Homo sapiens enzyme
additional information
GlxI is longer than the Escherichia coli enzyme but similar to the Homo sapiens enzyme
additional information
GlxI is longer than the Escherichia coli enzyme but similar to the Homo sapiens enzyme
additional information
GlxI is longer than the Escherichia coli enzyme but similar to the Homo sapiens enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
homodimer
monomer
additional information
?
-
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
dimer
2 * 15818, His6-tagged enzyme, sequence calculation, the enzyme forms two active sites, each within single subunits
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
-
x * 17000, SDS-PAGE or Western blot analysis, x * 16647, predicted, x * 16650, MALDI-TOF-MS analysis
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
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
-
2 * 20647, sequence calculation, 2 * 21000, recombinant enzyme, SDS-PAGE
homodimer
2 * 20810, calculated from sequence, MALDI-TOF mass spectrometry, SDS-PAGE
homodimer
-
mammalian glyoxalase I is composed of two equal subunits which both harbor an acitve site
monomer
-
the monomeric enzyme has two different active sites with similar kcat values, but distinct Km values. Both active sites adopt two discrete conformations and are allosterically coupled in a substrate concentration-dependent manner
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
-
single polypeptide with two active sites that catalyze the same reaction
additional information
homology-based structural modeling, overview
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glutathionylation
glutathionylation strongly inhibits Glo1 activity in vitro
glycoprotein
sequence contains two potential N-glycosylation sites
phosphoprotein
side-chain modification
-
posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity
additional information
-
NO-mediated modification can suppress NF-kappaB-dependent reporter gene expression, less powerful in suppression than phosphorylation of GLO1
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
phosphoprotein
-
the enzyme is susceptible to post-translational modifications, in particular phosphorylation in response to TNFalpha, a key mediator of inflammation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme with bound Zn2+ or Ni2+, sitting drop vapor diffusion, in 20% v/v isopropyl alcohol and 30% w/v PEG3350 in 0.1 M HEPES buffer, pH 7.5, X-ray diffraction structure determination and analysis at 2.45 A and 2.06 A resolution, respectively. The Ni2+-bound non-His-tagged CLO GlxI structure is solved by molecular replacement using the Zn2+-bound structure as search model
the initial high-throughput X-ray structure containing Zn2+ bound in the two active sites shows a trigonal bipyramidal geometry, inactive Zn2+ -bound enzyme, whereas the active Ni2+ -bound enzyme has an octahedral geometry
-
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
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X-ray structure of the homodimeric humanGlo1 in the presence of the bound inhibitor S-benzylglutathione
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sitting drop vapor diffusion method, using 62% (v/v) 2-methyl-2,4-pentanediol and 100 mM Tris-HCl pH 8.5
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
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
S44A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S68A
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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
E145Q
the mutant shows altered thermodynamic parameters for Ni2+ ion binding compared to the wild-type enzyme
E78Q
the mutant shows altered thermodynamic parameters for Ni2+ ion binding compared to the wild-type enzyme
E161Q/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/E91Q/E345Q
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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
YEpGLO1
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overexpressing mutant, shows increased methylglyoxal resistance
additional information
additional information
gene GLO1 complements the glo1 mutation of Saccharomyces cerevisiae
additional information
-
gene GLO1 complements the glo1 mutation of Saccharomyces cerevisiae
additional information
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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
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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100% activity after 4 h incubation at 60°C, 50% inactivation after 150 min incubation at 64°C or after 60 min incubation at 65°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C or -70°C, native enzyme loses 0-10% of activity, metal-free enzyme loses 30-40% of activity during 40 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
60°C, DEAE-52 cellulose, S-hexylglutathione Sepharose 6 B affinity, gel filtraton
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ammonium sulfate precipitation, DEAE-cellulose column chromatography, hydroxyapatite column chromatography, and S-hexylglutathione-agarose column chromatography
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Co2+ affinity column chromatography and Superdex S75 gel filtration
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
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recombinant enzyme
recombinant enzyme from Escherichia coli strain JM103 by S-hexylglutathione affinity chromatography and gel filtration
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recombinant glyoxalase I
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage og the His-tag by thrombin, and elimination of the tag by benzamidine affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Brassica sp. gly I, cloning and overexpression in tobacco, transgenic plants tolerate higher concentrations of NaCl
expression in Escherichia coli
expression in Nicotiana tabaccum improves salinity tolerance of tobacco plants
gene clo glxI, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene GLX-I or LOC_Os08g09250, functional complementation of Saccaromyces cerevisiae GLY I mutant DELTAGLO I, heterologous expression in Escherichia coli and Nicotiana tabacum resulting in improved adaptation to various abiotic stresses caused by increased scavenging of methylglyoxal, lower Na+/K+ ratio and maintenance of reduced glutathione levels in the hosts
gloA2 and gloA3 ligated into vector pET22b, overexpression in Escherichia coli BL21(gammaDE3)
GST-GLOI fusion protein is expressed in Escherichia coli BL21 (DE3)pLysS cells
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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
overexpressing mutant YEpGLO1, shows increased methylglyoxal resistance
-
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%
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pQE30 constructs of the wild-type and mutants expressed in Escherichia coli strain M15
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rats, overexpressing human GLO I show e.g. improvement of the tubulointerstitial injury and renal function
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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
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
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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
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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
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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
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Brassica sp. gly I, cloning and overexpression in tobacco, transgenic plants tolerate higher concentrations of NaCl
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Brassica sp. gly I, cloning and overexpression in tobacco, transgenic plants tolerate higher concentrations of NaCl
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expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of receptor for advanced glycation endproducts by S100A12 protein decreases the expression of glyoxalase 1
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activity of glyoxalase I decreased under NaCl stress, at 48 h of NaCl stress the decrease is maximum
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aged ovaries show a 2.9fold decreased protein level and a 1.4fold decreased RNA level of GLO1
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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
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expression of GLO1 is induced by stress inducers such as methylglyoxal, H2O2, KCl, and NaCl
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
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Gly-I activity in N-acetylcysteine-exposed cells is 40% higher than that in control cells
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glyoxlase I activity decreases in heavy metal stress (exposure to 0.5 mM CdCl2)
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glyoxylase I expression is upregulated up to 10fold at the mRNA and protein level in metastatic melanoma tissue
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high Glo1 expression is strongly associated with high anxiety-like behavior in mice
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isoforms GLYI02, GLYI19, GLYI31 and GLYI35 are significantly downregulated after S. sclerotiorum pathogen infection in the resistant cultivar ZY821 and sensitive cultivar Westar, while the expression of isoforms GLYI08 and GLYI10 is down-regulated in resistant cultivar ZY821. Isoforms GLYI02, GLYI06, GLYI09, GLYI13, GLYI15, GLYI17, GLYI18, GLYI21, GLYI24, GLYI26, GLYI30, and GLYI34 are down-regulated under heat stress (40 C, 3 h). Isoforms GLYI06, GLYI09, GLYI11, GLYI24 and GLYI34 are low expressed under drought stress (withdrawing water, 3 days)
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low temperature (4°C) 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
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maximum expression at the exponential growth phase
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
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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
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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
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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
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the expression levels of isoforms GLYI07, GLYI24 and GLYI25 are significantly up-regulated after S. sclerotiorum pathogen infection in the resistant cultivar ZY821 and sensitive cultivar Westar. The expression of isoforms GLYI08 and GLYI10 is up-regulated in sensitive cultivar Westar. The expression levels of isoforms GLYI03, GLYI05, GLYI08, GLYI11, GLYI19, GLYI20, GLYI27, GLYI31, GLYI33 and GLYI35 are up-regulated under heat stress (40 C, 3 h). The expression of isoforms GLYI13, GLYI15, GLYI17, GLYI18, GLYI21 and GLYI30 increases under drought stress (withdrawing water, 3 days). Isoform GLYI11 is significantly induced under both chilling and freezing stresses regardless of cold acclimation
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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 promoter of Glo1 harbours an nuclear factor kappaB-responsive element, indicating a link between inflammation and reduced Glo1 expression
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troglitazone treatment (0.025-0.1 mM) reduces glyoxalase I protein expression in glioma
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maximum expression at the exponential growth phase
maximum expression at the exponential growth phase
-
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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
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
additional information
analysis
-
practical experiments for students to determine the effect of exposure to oxidative stress conditions on yeast glyoxalase I, investigation of kinetic parameters
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
drug development
difference of the substrate specificity of the human and the Leishmania enzyme could be used for designing selective inhibitors against the parasite
drug development
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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
drug development
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
drug development
-
the enzyme is a promising drug target, since the functional monomeric Glo1 from Plasmodium falciparum differs significantly from its human homologue
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
-
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
medicine
-
role in dental caries, LGL functions in the detoxification of methylglyoxal, resulting in increased aciduricity
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
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
-
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
-
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
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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
treatment of HL-60 cells leads to significant accumulation of substrate methylglyoxal and the caspase 3 activity of the cell lysate increases. Compound shows anti-proliferative activity against HL-60 cells
medicine
-
role in dental caries, LGL functions in the detoxification of methylglyoxal, resulting in increased aciduricity
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additional information
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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
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
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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
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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
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
additional information
-
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
EXTERNAL LINKS (specific for EC-Number 4.4.1.5)
Transporter Classification Database (TCDB): 9.A.15.3.1
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Release 2026.1 (March 2026)
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