4.4.1.5: lactoylglutathione lyase
This is an abbreviated version!
For detailed information about lactoylglutathione lyase, go to the full flat file.
Word Map on EC 4.4.1.5
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4.4.1.5
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glycation
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detoxify
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gsh
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dicarbonyls
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erythrocyte
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d-lactate
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adduct
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dismutase
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endproducts
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rage
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s-transferase
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mellitus
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methylglyoxal-induced
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glyoxalases
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byproduct
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hyperglycemia
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glutathione-dependent
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phosphoglucomutase
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metalloenzyme
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hemithioacetal
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mg-induced
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hla-a
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aldose
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3-deoxyglucosone
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enediolate
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d-lactic
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pentosidine
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cyclopentyl
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mdhar
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haptoglobin
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aminoguanidine
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diesters
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monodehydroascorbate
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6-phosphogluconate
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anti-glycation
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dehydroascorbate
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anxiety-like
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gsh-dependent
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pyridoxamine
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analysis
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trypanothione
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medicine
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drug development
- 4.4.1.5
-
glycation
-
detoxify
- gsh
-
dicarbonyls
- erythrocyte
- d-lactate
- adduct
- dismutase
-
endproducts
- rage
- s-transferase
- mellitus
-
methylglyoxal-induced
-
glyoxalases
-
byproduct
- hyperglycemia
-
glutathione-dependent
- phosphoglucomutase
-
metalloenzyme
- hemithioacetal
-
mg-induced
- hla-a
- aldose
- 3-deoxyglucosone
-
enediolate
-
d-lactic
-
pentosidine
-
cyclopentyl
- mdhar
- haptoglobin
- aminoguanidine
- diesters
- monodehydroascorbate
- 6-phosphogluconate
-
anti-glycation
- dehydroascorbate
-
anxiety-like
-
gsh-dependent
- pyridoxamine
- analysis
- trypanothione
- medicine
- drug development
Reaction
Synonyms
aldoketomutase, CLO GlxI, Glb33, GLI, GLO I, GLO-1, GLO-I, Glo1, GloA, GloA1, GloA2, GloA3, GloI, Glx I, Glx-I, Glx1, GLXI, Gly I, gly-I, GLY1, glyoxalase 1, glyoxalase I, glyoxalase-1, glyoxalase-I, glyoxylase I, GmGlyox I, ketone-aldehyde mutase, lactoylglutathione lyase, lactoylglutathione methylglyoxal lyase, LGL, lyase, lactoylglutathione, methylglyoxalase, methylglyoxylase, OsGLYI-11.2, PfGlx I, rhGLO I, S-D-lactoylglutathione methylglyoxal lyase, S-D-lactoylglutathione methylglyoxal lyase (isomerizing), S-D-lactoylglutathione:methylglyoxal lyase, SpGlo1, STM3117, YaiA
ECTree
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Engineering
Engineering on EC 4.4.1.5 - lactoylglutathione lyase
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H74Q
the native His74 metal ligand substituted with a Gln residue, maintains a homodimeric quaternary structure in solution as does the wild-type enzyme
A111E
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the mutation is associated with an increased risk of this neoplasia in breast cancer
S44A
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co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S68A
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co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S93A
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co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T101A
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co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T106A
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co-expressed with calcium, calmodulin-dependent protein kinase II, phosphorylation of GLO1 is completely abolished
T97A
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co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
E145Q
the mutant shows altered thermodynamic parameters for Ni2+ ion binding compared to the wild-type enzyme
E78Q
the mutant shows altered thermodynamic parameters for Ni2+ ion binding compared to the wild-type enzyme
E161Q/E272Q
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maximum catalytic efficiency is 60% of the wild-type enzyme
E345Q
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kinetics are biphasic, maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5
E91Q
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maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5
E91Q/E345Q
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maximum catalytic efficiency is 7% of the wild-type enzyme
R22E/E91Q/E345Q
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kinetics are monophasic, substrate binding at the high-affinity binding site A is abrogated, the mutant seems to be trapped in the conformation that predominates at lower substrate concentrations
YEpGLO1
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overexpressing mutant, shows increased methylglyoxal resistance
additional information
gene GLO1 complements the glo1 mutation of Saccharomyces cerevisiae
additional information
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gene GLO1 complements the glo1 mutation of Saccharomyces cerevisiae
additional information
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lgl isogenic knockout mutant LGLKO, has no detectable enzyme activity, results in an acid-sensitive phenotype, glycolytic rate at pH 5.0 is higher for the mutant than for wild-type
additional information
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lgl isogenic knockout mutant LGLKO, has no detectable enzyme activity, results in an acid-sensitive phenotype, glycolytic rate at pH 5.0 is higher for the mutant than for wild-type
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