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(R)-S-lactoylglutathione
glutathione + methylglyoxal
gamma-glutamylcysteine-methylglyoxal hemithioacetal
?
gamma-glutamylcysteine-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
gamma-glutamylcysteine-phenylglyoxal hemithioacetal
?
gamma-glutamylcysteine-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione + 2,4-dimethylphenylglyoxal
S-(2,4-dimethyl)mandeloylglutathione
-
-
-
-
?
glutathione + 2-oxopropanal
(R)-S-lactoylglutathione
-
-
-
-
r
glutathione + 4,5-dioxovalerate
?
glutathione + 4-bromophenylglyoxal
S-(4-bromo)mandeloylglutathione
-
-
-
-
?
glutathione + 4-methylphenylglyoxal
S-(4-methyl)mandeloylglutathione
-
-
-
-
?
glutathione + bromophenylglyoxal
?
-
-
-
-
?
glutathione + glyoxal
S-glycolylglutathione
glutathione + hydroxypyruvaldehyde
?
-
-
-
-
?
glutathione + m-methoxyphenylglyoxal
S-(3-methoxy)mandeloylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
glutathione + methylglyoxal
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
glutathione + methylglyoxal
S-D-lactoylglutathione
glutathione + methylglyoxal
S-lactoylglutathione
glutathione + methylphenylglyoxal
?
-
-
-
-
?
glutathione + p-chlorophenylglyoxal
S-(4-chloro)mandeloylglutathione
glutathione + p-hydroxyphenylglyoxal
S-(4-hydroxy)mandeloylglutathione
-
-
-
-
?
glutathione + p-methoxyphenylglyoxal
S-(4-methoxy)mandeloylglutathione
-
-
-
-
?
glutathione + p-phenylphenylglyoxal
?
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
glutathione + phenylglyoxal
S-mandoylglutathione
-
-
-
-
?
glutathione ethyl ester + methylglyoxal
?
-
-
-
?
glutathione ethyl ester + methylglyoxal
S-lactoylglutathionyl ethyl ester
glutathione isopropyl ester + methylglyoxal
S-lactoylglutathionyl isopropyl ester
glutathione-glyoxal hemithioacetal
?
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-phenylglyoxal hemithioacetal
?
glutathionylspermidine + methylglyoxal
?
glutathionylspermidine + phenylglyoxal
?
-
-
-
-
?
homoglutathione-methylglyoxal hemithioacetal
(R)-S-lactoylhomoglutathione
homoglutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
homoglutathione-phenylglyoxal hemithioacetal
?
homoglutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
methylglyoxal + glutathione
(R)S-lactoylglutathione
Amaranthus sp.
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
methylglyoxal + glutathione
S-D-lactoylglutathione
-
-
-
?
methylglyoxal + reduced trypanothione
S-D-lactoyltrypanothione
-
-
-
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
N1-glutathionylspermidine + methylglyoxal
?
S-D-lactoyltrypanothione
methylglyoxal + reduced trypanothione
-
-
-
?
S-mandoylglutathione
glutathione + phenylglyoxal
-
-
-
?
S-mandoyltrypanothione
phenylglyoxal + trypanothione
-
-
-
?
trypanothione + 2 methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
trypanothione + phenylglyoxal
S-mandoyltrypanothione
-
-
-
-
?
additional information
?
-
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
r
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
-
r
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
-
?
(R)-S-lactoylglutathione
glutathione + methylglyoxal
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
-
-
-
-
?
glutathione + 4,5-dioxovalerate
?
-
no activity
-
-
?
glutathione + 4,5-dioxovalerate
?
-
-
-
-
?
glutathione + glyoxal
S-glycolylglutathione
-
-
-
-
?
glutathione + glyoxal
S-glycolylglutathione
-
-
-
-
?
glutathione + glyoxal
S-glycolylglutathione
-
-
-
-
?
glutathione + kethoxal
?
-
-
-
-
?
glutathione + kethoxal
?
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
glyoxalase I catalyzes the isomerization of a hemithioacetal, formed from glutathione and methylglyoxal, to lactic acid thioester
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
glyoxalase I catalyses the isomerization of the hemithioacetal formed non-enzymatically from methylglyoxal and glutathione to S-D-lactoylglutathione
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
r
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
cytosolic isozyme Glo1 is functional, but the recombinant Glo1-like protein is inactive in a standard enzyme assay
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
glutathione + methylglyoxal
?
-
detoxification of methylglyoxal
-
-
?
glutathione + methylglyoxal
?
-
detoxification of methylglyoxal
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
-
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
methylglyoxal is a highly reactive carbonyl compound generated by carbohydrate oxidation and glycolysis, is a major precursor of protein glycation and induces cytotoxicitay leading to apoptosis
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
methylglyoxal is a reactive dicarbonyl compound mainly produced by metabolic pathways such as glycolysis, binds to proteins or nucelic acids and forms advanced glycation end products
-
-
?
glutathione + methylglyoxal
S-((R)-lactoyl)glutathione
-
glutathione reacts with methylglyoxal forming a hemithioacetal, and then glyoxlase I catalyses the formation of S-D-lactoylglutathione
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
very poor substrate, specificity constant 280fold lower than of the N1-glutathionylspermidine
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-D-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
most active with methylglyoxal
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
most active with methylglyoxal
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the hemimercaptal adduct produced nonenzymatically from methylglyoxal and glutathione is the substrate
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
stereospecifically transfers hydrogen to form S-D-lactoylglutathione from methylglyoxal and glutathione
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
stereospecifically transfers hydrogen to form S-D-lactoylglutathione from methylglyoxal and glutathione
-
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
the substrat is the hemithioacetal of methylglyoxal and glutathione
-
?
glutathione + methylglyoxal
S-lactoylglutathione
-
-
-
-
?
glutathione + p-chlorophenylglyoxal
S-(4-chloro)mandeloylglutathione
-
-
-
-
?
glutathione + p-chlorophenylglyoxal
S-(4-chloro)mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
no activity detectable
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
no activity detectable
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
no activity
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione + phenylglyoxal
S-mandeloylglutathione
-
-
-
-
?
glutathione ethyl ester + methylglyoxal
S-lactoylglutathionyl ethyl ester
-
-
-
?
glutathione ethyl ester + methylglyoxal
S-lactoylglutathionyl ethyl ester
-
-
-
?
glutathione isopropyl ester + methylglyoxal
S-lactoylglutathionyl isopropyl ester
-
-
-
?
glutathione isopropyl ester + methylglyoxal
S-lactoylglutathionyl isopropyl ester
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, Gly-I may play a critical detoxifying role in glycolysis to maintain cellular activity and viability of prostatic cancer cells
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, operates in conjunction with glyoxalase II to convert cytotoxic methylglyoxal to nontoxic D-lactate
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-phenylglyoxal hemithioacetal
?
glutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-phenylglyoxal hemithioacetal
?
-
glutathione-phenylglyoxal hemithioacetal is formed non-enzymatically from phenylglyoxal and glutathione
-
?
glutathionylspermidine + methylglyoxal
?
-
-
-
-
?
glutathionylspermidine + methylglyoxal
?
-
most efficient substrate
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
non-enzymatic formation of hemithioacteal as substrate for gly I
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
glyoxalase I is a member of the metallogltathione transferase superfamily and plays a critical role in detoxification of the cytotoxic methylglyoxal to S-D-lactoylglutathione via 1,2-hydrogen transfer
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
non-enzymatic formation of hemithioacetal from methylglyoxal and reduced glutathione
enzyme activity is measured spectrophotometrically as a function of thioester formation, S-((R)-lactoyl)glutathione, by measuring the rate of change of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
non-enzymatic formation of hemithioacteal as substrate for gly I. The active site of gly I has binding affinity for zinc ion and hemithioacetal, and his His residue might be important for its catalytic activity
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
the hemiacetal of methylglyoxal + glutathione is used as substrate, pH 6.8, 20°C
the product formation is measured by monitoring the increase of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
methylglyoxal and glutathione form an intermediate, the hemithioacetal, which is catalyzed to S-D-lactoylglutathione by GlxI. Subsequently S-D-lactoylglutathione is hydrolyzed to D-lactate and glutathione by GlxII (EC 3.1.2.6)
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
determined monitoring the increase in absorbance at 240 nm for 5 min at 25°C, pH 7.0
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
-
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
the hemiacetal of methylglyoxal + glutathione is used as substrate, pH 7.0, 30°C
the formation is measured by monitoring the increase of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
the hemiacetal of methylglyoxal + glutathione is used as substrate, 25°C
the formation is measured by monitoring the increase of absorbance at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
liver homogenate, the effects of taurine, ethanol, and iron alone or in combination are analyzed, pH 7.0, 37°C
-
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
permeabilized cell suspensions, 30°C, pH 7.1
formation is monitored by measuring the increase at 240 nm
-
?
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
two major intracelluar thiols are used, glutathione and trypanothione, preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
-
-
?
methylglyoxal + trypanothione
S,S'-bis((R)-lactoyl)trypanothione
-
two major intracelluar thiols are used, glutathione and trypanothione
-
-
?
N1-glutathionylspermidine + methylglyoxal
?
specificity constant of N1-glutathionylspermidine 50fold less than of glutathione
-
-
?
N1-glutathionylspermidine + methylglyoxal
?
-
-
-
?
trypanothione + 2 methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + 2 methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
high specificity of the kinetoplastid Glo1 isoform for its trypanothione, i.e. N1,N8-bis(glutathionyl)spermidine, substrate as compared with glutathione
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
-
-
r
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
cell lysate, pH 7.0, 25°C
the formation is measured by monitoring at 240 nm
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
cell lysate, pH 7.0, 25°C
the formation is measured by monitoring at 240 nm
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
cell lysate of the recombinant protein, esxpression of GLO1 from Trypanosomas cruzi in Trypanosomas brucei which lacks GLO1 activity, pH 7.0, 25°C
the product formation is measured by monitoring at 240 nm
-
?
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
Amaranthus sp.
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the 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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
disinfected water from two drinking water production plants at the river Po in North Italy markedly perturb the crap liver detoxfifying system, in terms of both induction and inhibition of enzyme activities and glutathione content
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
?
additional information
?
-
-
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
?
additional information
?
-
-
the enzyme is associated with cell proliferation, the activity is modulated during the proliferation cycle with a maximal activity between day 2 and day 4 of culture growth
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
-
overexpression of the enzyme completely prevents both hyperglycemia-induced advanced glycation products from methylglyoxal and increased macromolecular endocytosis
-
-
?
additional information
?
-
-
Glo1 is the major cellular enzyme that catalyzes the metabolism of methylglyoxal and thereby protects against dicarbonyl glycation
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the Leishmania sp. glxI preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
-
-
?
additional information
?
-
-
spectrophotometric measurement of enzyme activity in tissue and cell culture, modified for use with a UV-transparent microplate for higher sample throughput, method, overview
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
GLO1 is required for osteoclastogenesis
-
-
?
additional information
?
-
-
glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
-
-
?
additional information
?
-
-
major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis
-
-
?
additional information
?
-
-
reaction involves abstraction of a proton from carbon 1 and reinsertion of the proton at carbon 2. Proton transfer takes place with limited proton exchange with the surrounding medium, and a hydride transfer is involved. In the absence of substrate or product, the metal is coordinated with 2 water molecules in addition to the side chains of Gln33 and Glu99 in the same subunit and His126 and Glu172 from the neighbouring subunit. During the catalytic process the water molecule are displaced by the incoming substrate. Glu172 serves as the acid-base in the catalytic mechanism.
-
-
?
additional information
?
-
-
alpha-ketoaldehydes may be formed in cells during oxidative processes, glyoxalase I is the main enzyme involved in the detoxification pathway for these highly toxic compounds
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
glyoxalase I activity is involved in the detoxification of toxic metabolites produced during lipid peroxidation
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
-
together with the second enzyme of the glyoxalase system, EC3.1.2.6, EC4.4.1.5 may detoxify the electrophilic 2-oxoaldehydes which can be formed in the cell from endogenous precursors
-
-
?
additional information
?
-
-
glyoxalase I catalyzes the isomerization reaction of thiohemiacetal, which is formed nonenzymatically from methylglyoxal and glutathione
-
-
?
additional information
?
-
-
study of the pathophysiological role of glyaylase I as an methylglyxal detoxifier in rat ischemia-reperfusion (I/R) injury
-
-
?
additional information
?
-
-
the glyoxalase system detoxifies methylglyoxal and is composed of two enzymes: glyoxylase I (GLO I), which metabolizes methylglyoxal to S-D-lactoylglutathione, and glyoxalase II (GLO II, EC 3.1.2.6) which converts S-D-lactoylglutathione to D-lactate
-
-
?
additional information
?
-
-
knockdown of glyoxalase I by SiRNA transfecetion in rat tubulart cells exacerbates cell-death by hyposia-reoxygenation compared to control cells. Glyoxalase I exerts renoprotective effects in renal ischemia-reperfusion (I/R) injury via the reduction in methylglyoxal accumulation in tubluar cells
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
-
the glyoxalase I activity is measured spectrophotometrically by S-D-lactoylglutathione formation at 240 nm
-
-
?
additional information
?
-
-
may serve to detoxify methylglyoxal produced from triosephosphates. Increased expression of glyoxalase I may be linked to a higher demand for ATP generation and to enhanced glycolysis in salt-stressed plants
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
activity with glutathione analogs
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
glutathione + methylglyoxal
(R)-S-lactoylglutathione
glutathione + methylglyoxal
?
glutathione-glyoxal hemithioacetal
?
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathionylspermidine + methylglyoxal
?
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
methylglyoxal + glutathione
(R)S-lactoylglutathione
Amaranthus sp.
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
S-((R)-lactoyl)glutathione
-
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
-
-
?
trypanothione + 2 methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
trypanothione + methylglyoxal
S,S'-bis((R)-lactoyl)trypanothione
-
-
-
-
?
additional information
?
-
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
r
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
(R)-S-lactoylglutathione
-
-
-
-
?
glutathione + methylglyoxal
?
-
detoxification of methylglyoxal
-
-
?
glutathione + methylglyoxal
?
-
detoxification of methylglyoxal
-
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, Gly-I may play a critical detoxifying role in glycolysis to maintain cellular activity and viability of prostatic cancer cells
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, operates in conjunction with glyoxalase II to convert cytotoxic methylglyoxal to nontoxic D-lactate
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
-
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
glutathione-methylglyoxal hemithioacetal
(R)-S-lactoylglutathione
glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
-
-
-
?
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system
-
-
r
methylglyoxal + glutathione
(R)-S-lactoylglutathione
-
first step in the glyoxalase system, detoxification of methylglyoxal
-
-
r
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
trypanothione + methylglyoxal
5,5'-bi((R)-lactoyl)trypanothione
-
-
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
Amaranthus sp.
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
disinfected water from two drinking water production plants at the river Po in North Italy markedly perturb the crap liver detoxfifying system, in terms of both induction and inhibition of enzyme activities and glutathione content
-
-
?
additional information
?
-
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
?
additional information
?
-
-
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the enzyme is a part of the glyoxalase system that is composed of EC 4.4.1.5 and EC 3.1.2.6. The glyoxalase system converts toxic alpha-keto aldehydes into their corresponding nontoxic 2-hydroxycarboxylic acids
-
-
?
additional information
?
-
-
the enzyme is associated with cell proliferation, the activity is modulated during the proliferation cycle with a maximal activity between day 2 and day 4 of culture growth
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
overexpression of the enzyme completely prevents both hyperglycemia-induced advanced glycation products from methylglyoxal and increased macromolecular endocytosis
-
-
?
additional information
?
-
-
Glo1 is the major cellular enzyme that catalyzes the metabolism of methylglyoxal and thereby protects against dicarbonyl glycation
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the Leishmania sp. glxI preferentially utilizes the hemithioacetal formed between methylglyoxal and trypanothione as the substrate
-
-
?
additional information
?
-
GLO1 is required for osteoclastogenesis
-
-
?
additional information
?
-
-
glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids
-
-
?
additional information
?
-
-
major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis
-
-
?
additional information
?
-
-
reaction involves abstraction of a proton from carbon 1 and reinsertion of the proton at carbon 2. Proton transfer takes place with limited proton exchange with the surrounding medium, and a hydride transfer is involved. In the absence of substrate or product, the metal is coordinated with 2 water molecules in addition to the side chains of Gln33 and Glu99 in the same subunit and His126 and Glu172 from the neighbouring subunit. During the catalytic process the water molecule are displaced by the incoming substrate. Glu172 serves as the acid-base in the catalytic mechanism.
-
-
?
additional information
?
-
-
alpha-ketoaldehydes may be formed in cells during oxidative processes, glyoxalase I is the main enzyme involved in the detoxification pathway for these highly toxic compounds
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
glyoxalase I activity is involved in the detoxification of toxic metabolites produced during lipid peroxidation
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
together with the second enzyme of the glyoxalase system, EC3.1.2.6, EC4.4.1.5 may detoxify the electrophilic 2-oxoaldehydes which can be formed in the cell from endogenous precursors
-
-
?
additional information
?
-
-
glyoxalase I catalyzes the isomerization reaction of thiohemiacetal, which is formed nonenzymatically from methylglyoxal and glutathione
-
-
?
additional information
?
-
-
study of the pathophysiological role of glyaylase I as an methylglyxal detoxifier in rat ischemia-reperfusion (I/R) injury
-
-
?
additional information
?
-
-
the glyoxalase system detoxifies methylglyoxal and is composed of two enzymes: glyoxylase I (GLO I), which metabolizes methylglyoxal to S-D-lactoylglutathione, and glyoxalase II (GLO II, EC 3.1.2.6) which converts S-D-lactoylglutathione to D-lactate
-
-
?
additional information
?
-
-
may serve to detoxify methylglyoxal produced from triosephosphates. Increased expression of glyoxalase I may be linked to a higher demand for ATP generation and to enhanced glycolysis in salt-stressed plants
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
additional information
?
-
-
the glyoxalase system is an ubiquitous pathway for the detoxification of highly reactive ketoaldehydes
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
methylglyoxal
-
10 mM, enhanced tolerance to toxic stress in transgenic Vigna mungo
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
Ca2+
-
activation of gly I
Ca2+
Amaranthus sp.
-
activation of gly I
Ca2+
-
activates apoenzyme
Ca2+
-
2.6fold increase of activity in the presence of 0.025 mM Ca2+
Ca2+
-
activation of gly I
Ca2+
-
activation of gly I
Ca2+
-
1 mM restores 25% of the activity of the apoenzyme
Ca2+
-
activation of gly I
Ca2+
-
activation of gly I
Ca2+
-
activates apoenzyme
Ca2+
-
activation of gly I
Ca2+
-
activates apoenzyme
Ca2+
-
restores activity after EDTA treatment
Ca2+
-
20mM, 32.8% reactivation of EDTA-treated enzyme
Ca2+
-
activation of gly I
Ca2+
-
activates apoenzyme
Ca2+
-
activation of gly I
Cd2+
activates 5% compared to Ni2+
Cd2+
-
6% of activity with Ni2+
Cd2+
-
reduced activity compared to Ni2+
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+
-
increased enzyme activity
Cd2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Cd2+
-
increased enzyme activity
Cd2+
reactivates GloA3 by 87% after treatment with dipicolinic acid
Cd2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Cd2+
-
increased enzyme activity
Co2+
activates 40% compared to Ni2+
Co2+
-
31% of activity with Ni2+
Co2+
-
reduced activity compared to Ni2+
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+
-
66% of activity with Zn2+
Co2+
reactivation of apo gly I
Co2+
reactivation of the apoenzyme
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+
-
increased enzyme activity
Co2+
activated by Ni2+ and Co2+
Co2+
results in about 25% of the activity with Ni2+
Co2+
-
reactivates apoenzyme
Co2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Co2+
-
increased enzyme activity
Co2+
-
can partially substitute for Ni2+
Co2+
increases GloA2 activity, hyper-reactivates GloA3 by 115% after treatment with dipicolinic acid
Co2+
apo form reactivated
Co2+
reactivation of apo gly I
Co2+
-
1mM, 78.6% reactivation of EDTA-treated enzyme
Co2+
-
only marginally less effective than nickel
Co2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Co2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Co2+
-
increased enzyme activity
Co2+
-
activated by Ni2+ and Co2+
Co2+
-
activation of gly I
Fe2+
-
0.5 mM activates 2.4fold
Fe2+
-
16% of activity with Ni2+
Fe2+
activation, Km: 0.010 mM, Vmax: 0.112 mmol/min/mg, kcat: 56 1/s
Fe2+
-
at least one iron per enzyme molecule, the second metal is zinc or manganese, apparantly depending on growth conditions
Fe2+
-
1mM, 8.4% reactivation of EDTA-treated enzyme
Mg2+
-
incubation of the Zn2+ depleted apoenzyme with Mg2+ restores 50% of the enzyme activity
Mg2+
-
required for maximal activity
Mg2+
-
activates apoenzyme
Mg2+
-
potent stimulator, optimal concentration: 16 mM
Mg2+
-
101% of activity with Zn2+
Mg2+
reactivation of gly I
Mg2+
-
1 mM restores 60% of the activity of the apoenzyme
Mg2+
only slight activation
Mg2+
-
activates apoenzyme
Mg2+
reactivates GloA3 by 26% after treatment with dipicolinic acid
Mg2+
apo form reactivated
Mg2+
reactivation of gly I
Mg2+
-
activates apoenzyme
Mg2+
-
restores activity after EDTA treatment
Mg2+
-
20mM, 13.7% reactivation of EDTA-treated enzyme
Mg2+
-
activates apoenzyme
Mn2+
-
activates apoenzyme
Mn2+
activates 5% compared to Ni2+
Mn2+
-
18% of activity with Ni2+
Mn2+
-
reduced activity compared to Ni2+
Mn2+
activation, Km: 0.010 mM, Vmax: 0.121 mmol/min/mg, kcat: 60 1/s
Mn2+
-
67% of activity with Zn2+
Mn2+
reactivation of the apoenzyme
Mn2+
-
1 mM restores 35% of the activity of the apoenzyme
Mn2+
-
in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Mn2+
-
increased enzyme activity
Mn2+
-
activates apoenzyme
Mn2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Mn2+
-
increased enzyme activity
Mn2+
hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
Mn2+
-
activates apoenzyme
Mn2+
-
1mM, 186% reactivation of EDTA-treated enzyme
Mn2+
-
activates apoenzyme
Mn2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Mn2+
-
increased enzyme activity
Ni2+
-
required for activity, dependent on, Ni2+ -activation class, the active Ni2+ -bound enzyme has an octahedral geometry
Ni2+
required, best divalent metal ion
Ni2+
-
required for activity
Ni2+
-
maximal activity in the presence of Ni2+
Ni2+
GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies
Ni2+
highest reactivation activity, Km: 0.027 mM, Vmax: 0.676 mmol/min/mg, kcat: 338 1/s
Ni2+
reactivation of apo gly I
Ni2+
-
Ni2+-activating class
Ni2+
reactivation of the apoenzyme, largest recovery in activity
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+
-
increased enzyme activity
Ni2+
activated by Ni2+ and Co2+
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+
-
activates apoenzyme
Ni2+
2.9fold increase in activity at 0.25 mM
Ni2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Ni2+
-
increased enzyme activity
Ni2+
activation, Km: 0.021 mM, Vmax: 0.497 mmol/min/mg, kcat: 247 1/s, kcat/Km: 12000000 1/M * s
Ni2+
activation, Km: 0.032 mM, vmax: 0.571 mmol/min/mg, kcat: 271 1/s, kcat/Km: 8500000 1/M * s
Ni2+
-
activates isozymes 1 and 2, Ni2+ -activation class
Ni2+
increases GloA2 activity, hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
Ni2+
apo form reactivated
Ni2+
reactivation of apo gly I
Ni2+
-
activates apoenzyme
Ni2+
-
1mM, 67.9% reactivation of EDTA-treated enzyme
Ni2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Ni2+
-
Ni2+-activating class
Ni2+
-
in decreasing order of activation: Ni2+, Co2+, Mn2+, Cd2+
Ni2+
-
increased enzyme activity
Ni2+
-
activated by Ni2+ and Co2+
Ni2+
-
activation of gly I
Zn2+
-
binding affinity
Zn2+
Amaranthus sp.
-
binding affinity
Zn2+
-
1 mol Zn2+ per subunit
Zn2+
-
activates apoenzyme
Zn2+
-
contains 1.4 gatom of Zn2+ per mol of enzyme
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
required for activity, no activity with Ni2+, Co2+ and Cd2+
Zn2+
-
Zn2+ -activation class, Zn2+ binds to the active site
Zn2+
4fold higher glyoxalase I activity when glyoxalase is isolated from Zn2+-grown bacteria
Zn2+
-
required for activity
Zn2+
-
zinc metalloenzymes
Zn2+
-
metalloenzyme with one Zn2+ per subunit
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+
-
required, zinc enzyme
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
essential role in catalytic mechanism
Zn2+
-
in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Zn2+
-
Zn2+ -activation class
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
reactivates apoenzyme
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
2.7fold increase in activity at 0.25 mM
Zn2+
-
addition of ZnSO4 during the overexpression results in increased catalytic activity and a decreased Km value
Zn2+
-
activation of glxI
Zn2+
activation of gloA3, metal ion binds tightly to the enzyme so that removal of metall ion requires more forceful conditions
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+
-
activates isozyme 3, Zn2+ -activation class
Zn2+
does not increase GloA2 activity, GloA3 contains Zn2+, reactivates GloA3 by 76% after treatment with dipicolinic acid
Zn2+
-
activates, Zn2+ -activation class
Zn2+
apo form reactivated
Zn2+
reactivation of gly I
Zn2+
-
two zinc ions per dimer. The zinc is required for structure and function. The monomer contains a single zinc ion
Zn2+
-
activates, beste metal ion, Zn2+ -activation class
Zn2+
-
activates, Zn2+ -activation class
Zn2+
-
zinc metalloenzymes
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
apoenzyme is catalytically inactive, but is partially restored by Zn2+
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
required for activity, 1 Zn2+ per subunit
Zn2+
-
activates, Zn2+ -activation class
Zn2+
-
0.5mM, 84.7% reactivation of EDTA-treated enzyme
Zn2+
-
metalloenzyme with one Zn2+ per subunit
Zn2+
-
major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Zn2+
-
Zn2+ -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
-
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
-
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 activity with Zn2+
additional information
-
no activity in the presence of Zn2+
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
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
no activity with Zn2+
additional information
-
no activity with Zn2+
additional information
-
inactive with Zn2+
additional information
-
no Zn2+ -activation
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
-
divalent cation required
additional information
-
not activated by Zn2+
additional information
not activated by Zn2+
additional information
-
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
-
inactive with Zn2+
additional information
inactive with Zn2+
additional information
inactive with Zn2+
additional information
inactive with Zn2+
additional information
-
no activation by Zn2+ of isozymes 1 and 2
additional information
-
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
-
no activation by Zn2+
additional information
-
not activated by Zn2+
additional information
-
Mg2+, Ca2+, Zn2+ no increase in enzyme activity
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(1E,4Z,6E)-4-(4-hydroxy-3-methoxybenzylidene)-1-(3-hydroxy-4-methoxyphenyl)-7-(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(3,4-dimethoxybenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(3-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(1E,6E)-4-(4-fluorobenzylidene)-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,6-diene-3,5-dione
-
three-ring curcumin derivative, in binding model two rings lay in the opening of the active site, the third is buried into hydrophobic pocket site
(2S)-2-amino-3-[([(2R)-3-[(4-bromobenzyl)sulfanyl]-1-[(carboxymethyl)amino]-1-oxopropan-2-yl]carbamoyl)amino]propanoic acid
-
-
(3Z)-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid
-
inhibitor based on binding mode of myricetin, contributuion of the Zn2+-chelating group to inhibitory activity
(S)-4-bromobenzyl glutathione
-
potent Glx-I inhibitor
(S)-4-bromobenzylglutathione cyclopentyl diester
-
competitive inhibitor of GLOI
(Z)-1-[N-(2-aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolate
-
decreases glyoxalase I expression and activity relative to untreated control cells, cells undergo apoptosis, apoptosis increases further on co-incubation with high glucose
1'-hydroxy-6'-phenyl-3,4'-bipyridin-2'(1'H)-one
-
-
1-chloro-2,4-dinitrobenzene
-
not reduced by dithiothreitol
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
10 mM, 65% inhibition
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
1-hydroxy-4,6-diphenylpyridin-2(1H)-one
-
-
1-hydroxy-4-phenyl-6-(1H-pyrrolo[2,3-b]pyridin-5-yl)pyridin-2(1H)-one
-
-
1-hydroxy-6-(1-pentyl-1H-pyrrolo[2,3-b]pyridin-5-yl)-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-(1H-indol-5-yl)-4-phenylpyridin-2(1H)-one
-
-
1-hydroxy-6-phenyl-4-(thiophen-3-yl)pyridin-2(1H)-one
-
-
1-hydroxy-6-phenyl-4-[4-(trifluoromethyl)phenyl]pyridin-2(1H)-one
-
-
1-hydroxy-6-[1-(2-methoxyethyl)-1H-indol-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-indol-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
-
-
2,3-Butanedione
-
time and concentration dependent inactivation
2,3-Dihydroxybenzoic acid
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2,4,6-trinnitrobenzenesulphonic acid
-
2 mM, 60% inhibition
2,6-pyridindicarboxylic acid
-
2 mM, approx. 50% inactivation after 10 min, almost complete inhibition after 180 min
2-([(4-methoxyphenyl)carbonyl]amino)-1-benzothiophene-3-carboxylic acid
-
inhibitor based on binding mode of myricetin
2-([(4-methoxyphenyl)carbonyl]amino)benzoic acid
-
inhibitor based on binding mode of myricetin
2-Hydroxy-5-nitrobenzyl bromide
-
-
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-(biphenyl-4-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
-
-
4-(but-1-yn-1-yl)-1-hydroxy-6-phenylpyridin-2(1H)-one
-
-
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-butyl-1-hydroxy-6-phenylpyridin-2(1H)-one
-
-
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
-
-
amino-group reagents
-
-
-
Baicalin
30% inhibition of rhGLO I at 0.1 mM
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
Co2+
apo form reactivated
cromoglycate
-
0.1 mM, 50% inhibition
D-glucono-delta-lactone
-
weak
dichlorophen
-
0.048 mM, 50% inhibition
diethyldicarbonate
-
2 mM, complete inhibition
dihydroxyfumaric acid
-
-
dipicolinic acid
greatest loss of GloA3 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
FeSO4
-
2.0 mM, 46.5% inhibition
flavone
IC50 wild type 56 microM, IC50 enzyme overexpressor 69 microM
formononetin 7-O-glucoside
-
0.074 mM, 50% inhibition
gerfelin
inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C
glutathione thioethers
-
competitive
glycerol
-
64% loss in Gly-I activity by 2.5% (v/v) glycerol, Gly-I inactivation by glycerol is fully prevented or reversed by 0.5 mM N-acetylcysteine
H2O2
-
2 mM, 2 h, significantly reduces enzyme activity from 0.2 U/single Caenorhabditis elegans (without addition of H2O2) to 0.065 U/single Caenorhabditis elegans
HgCl2
-
67% loss in Gly-I activity by 0.03 mM HgCl2, Gly-I inactivation by HgCl2 is fully prevented or reversed by 0.5 mM N-acetylcysteine
hyperin
below 5% inhibition of rhGLO I at 0.1 mM
I-
-
5 mM, complete inhibition
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
meso-tetrasubstituted porphyrines
-
-
-
N-Acetylimidazole
-
reversed by hydroxylamine
N-bromsuccinimide
-
0.0032 mM, 35% inhibition
N-[(1S,4Z)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohept-4-en-1-yl]-L-glutamine
-
beta-ketoester, competetive inhibitor
N-[(1S,4Z)-6-(4-bromophenyl)-1-[(carboxymethyl)carbamoyl]-4-hydroxy-6-oxohex-4-en-1-yl]-L-glutamine
-
beta-ketoester, competetive inhibitor
N-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-S-[(4-bromophenyl)(hydroxy)carbamoyl]-L-cysteinylglycine
-
tight-binding competitive inhibitor, stable toward gamma-glutamyltranspeptidase
N2-[[(2S)-2-amino-2-carboxyethyl]carbamoyl]-N-(4-bromophenyl)-N-hydroxy-L-glutaminylglycine
-
tight-binding carboanalog of hydroxamate
naringenin
50% inhibition of rhGLO I at 0.1 mM
NH2-gamma-Gla[-Glu(CON(OH)-4-bromophenyl)Gly-OH]-OH
-
-
NH2-gamma-Glu[-D-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
NH2-gamma-Glu[-Dab(N-(4-bromobenzoyl)-N'-hydroxyl)-Gly-OH]-OH
-
-
NH2-gamma-Glu[-Glu(CON(OH)-4-bromophenyl)-Gly-OH]-OH
-
-
NO3-
-
10 mM, 20% decrease of activity
oroxylin A
140% inhibition of rhGLO I at 0.1 mM
oxibendazol
-
0.11 mM, 50% inhibition
p-hydroxymercuribenzene sulfonate
-
1 mM, 64% inhibition
para-substituted S-benzylglutathione
-
-
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
pyridoxal 5'-phosphate
-
-
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-(1-naphthylmethyl)-glutathione
-
-
S-(2-chlorobenzyl)-glutathione
-
-
S-(2-hydroxybenzyl)-glutathione
-
-
S-(4-bromophenyl)glutathione
-
glyoxalase I
S-(4-nitrobenzyloxycarbonyl)glutathione
-
-
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
S-(N-hydroxy-N-methylcarbamoyl)glutathione
-
S-(N-hydroxy-N-p-bromophenylcarbamoyl)glutathione
-
S-(N-hydroxy-N-p-iodophenylcarbamoyl) glutathione
tight binding competitive inhibitor of human GLOI
S-(N-hydroxy-N-p-iodophenylcarbamoyl)glutathione
-
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
-
S-(omega-aminodecyl)glutathione
-
-
S-(p-bromobenzyl)glutathione
S-2,4-dinitrophenylglutathione
S-2,4-dinitrophenylglutathionylspermidine
S-4-bromobenzylglutathione
S-4-bromobenzylglutathione cyclopentyl diester
-
detanonoate, NO donor, competitive inhibitor, concentration-dependent down-regulation of glyoxalase I, increases intracellular methylglyoxal and causes apoptosis, overexpression of glyoxalase I protects against S-4-bromobenzylglutathione cyclopentyl diester-induced apoptosis under high glucose conditions
S-4-bromobenzylglutathionylspermidine
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
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
S-p-nitrobenzylglutathione
S-p-nitrobenzyloxycarbonylglutathione
-
S-p-nitrosobenzylglutathione
-
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
1,10-phenanthroline
decreases GloA3 activity
1,10-phenanthroline
-
reactivation by Mg2+, Mn2+ or Ca2+
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
baicalein
79% inhibition of rhGLO I at 0.1 mM
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
-
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
chrysin
-
-
Colchicine
-
decrease of activity of glyoxalase I
Colchicine
-
decrease of activity of glyoxalase I
coumarin-10
-
-
coumarin-4
-
-
coumarin-5
-
-
coumarin-8
-
-
coumarin-9
-
-
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
efficient inhibitor
curcumin
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Curcumin coordinates with the zinc ion
EDTA
-
1 mM
EDTA
-
0.1 mM, approx. 50% inactivation after 50 min, approx. 80% inhibition after 250 min
EDTA
-
10 mM, no inhibition
EDTA
-
reactivation by Mg2+, Mn2+ or Ca2+
fisetin
-
-
GSH
-
non-linear inhibition
GSH
-
non-linear inhibition
GSH
-
competitive; non-linear inhibition
GSH
-
non-linear inhibition
GSH
-
non-linear inhibition
indomethacin
-
indomethacin
-
combined study of kinetic analysis, molecular docking, and molecular dynamics. A remarkable correlation is observed between the experimental inhibitory affinity and predicted binding free energy parameter. DELTAGbind,pred of a glyoxalase I/inhibitor complex can be efficiently used to interpolate the experimental inhibitory affinity of a ligand of similar nature in the glyoxalase I enzyme system. Electrostatic contribution plays an important role in the inhibitory mechanisms. Indomethacin coordinates with the zinc ion and is able to occupy all four enzyme subsites, both subsites C and D may be occupied simultaneously
kaempferol
60% inhibition of rhGLO I at 0.1 mM
kaempferol
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 30°C, results in a decrease of D-lactate release
Lapachol
-
-
Lapachol
IC50 wild type 93 microM, IC50 enzyme overexpressor 96 microM
Lawsone
-
-
luteolin
90% inhibition of rhGLO I at 0.1 mM
luteolin
-
competitve inhibition, structually related to glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, pH 7.0, 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
-
5 mM, 50% inhibition of activity in cell lines
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
Mg2+
-
-
Mg2+
apo form reactivated
morin
-
-
MS-3
-
inhibitor produced by a mushroom Stereum hirsutum
MS-3
-
inhibitor produced by a mushroom Stereum hirsutum; mechanism of inhibition
myricetin
75% inhibition of rhGLO I at 0.1 mM
myricetin
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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
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substrate transition-state (Zn2+-bound methylglyoxal-glutathione hemithioacetal) mimetic inhibitor
Ni2+
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-
Ni2+
apo form reactivated
norlapachol
-
-
phthicol
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-
purpurogallin
IC50 wild type 70 microM, IC50 enzyme overexpressor 132 microM
purpurogallin
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0.015 mM, 50% inhibition
quercetin
-
-
quercetin
78% inhibition of rhGLO I at 0.1 mM
quercetin
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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-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
IC50 0.06 microM
S-(N-hydroxy-N-bromophenylcarbamoyl)gluthatione
-
IC50 0.06 microM
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
-
IC50 0.09 microM
S-(N-hydroxy-N-chlorophenylcarbamoyl)gluthatione
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IC50 0.11 microM
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
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IC50 2.5 microM
S-(N-hydroxy-N-phenylcarbamoyl)gluthatione
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IC50 10 microM
S-(p-bromobenzyl)glutathione
-
-
S-(p-bromobenzyl)glutathione
-
-
S-2,4-dinitrophenylglutathione
-
S-2,4-dinitrophenylglutathione
-
S-2,4-dinitrophenylglutathionylspermidine
-
S-2,4-dinitrophenylglutathionylspermidine
-
S-4-bromobenzylglutathione
-
S-4-bromobenzylglutathione
-
-
S-4-bromobenzylglutathione
-
S-4-bromobenzylglutathionylspermidine
linear competitive inhibitor
S-4-bromobenzylglutathionylspermidine
-
-
S-4-bromobenzylglutathionylspermidine
linear competitive inhibitor
S-4-bromobenzylglutathionylspermidine
-
potent linear competitive inhibitor, selectively inhibits trypanosomatid GLO1 activity
S-4-bromobenzylglutathionylspermidine
-
-
S-bromobenzylglutathione
-
-
S-bromobenzylglutathione
-
-
S-hexylglutathione
-
competitive inhibition
S-hexylglutathione
-
competitive
S-hexylglutathione
-
0.11 mM, 50% inhibition
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
S-p-bromobenzylglutathione
-
-
S-p-bromobenzylglutathione
-
competitive
S-p-bromobenzylglutathione
-
S-p-bromobenzylglutathione
55% inhibition of rhGLO I at 0.1 mM
S-p-nitrobenzylglutathione
-
-
S-p-nitrobenzylglutathione
-
-
Tetranitromethane
-
2 mM, 30% inhibition
vinblastine
-
decrease of activity of glyoxalase I
vinblastine
-
decrease of activity of glyoxalase I
Zn2+
-
0.5 mM, complete inhibition
Zn2+
inactivation of gly I, metal can bind to the enzyme gly I, but the resulting enzyme is inactive
Zn2+
apo form reactivated
Zn2+
inactivation of gly I
Zn2+
inactivation of gloA1; inactivation of gly I
Zn2+
-
0.1 mM, 75% inhibition at 0.1 mM, complete inhibition at 1.0 mM
Zn2+
-
inactivation of gly I
additional information
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-
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additional information
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additional information
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substrate-analogue inhibitors and transition-state inhibitors
-
additional information
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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
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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
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posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity
-
additional information
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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
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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
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inactive with Zn2+
-
additional information
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-
additional information
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additional information
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-
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additional information
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tight-binding inhibitors are very potent against the recombinant enzyme
-
additional information
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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
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additional information
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monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
-
additional information
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additional information
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no change in glyoxalase I activity in taurine-treated rats
-
additional information
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-
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additional information
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additional information
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pH-dependence of inhibition by porphyrins
-
additional information
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substrate-analogue inhibitors and transition-state inhibitors
-
additional information
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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
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additional information
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additional information
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S-4-bromobenzylglutathione is inactive as inhibitor
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