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
-
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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Subunits
Subunits on EC 4.4.1.5 - lactoylglutathione lyase
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dimer
heterodimer
homodimer
monomer
additional information
?
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x * 15669, electrospray ionization mass spectrometry, x * 15669, calculated
?
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x * 14251, electrospray ionization mass spectrometry, x * 14251, calculated
?
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x * 14833, electrospray ionization mass spectrometry, x * 14834, calculated
dimer
2 * 15818, His6-tagged enzyme, sequence calculation, the enzyme forms two active sites, each within single subunits
dimer
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treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
dimer
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x * 17000, SDS-PAGE or Western blot analysis, x * 16647, predicted, x * 16650, MALDI-TOF-MS analysis
GlxI, containing activating metals all have two water molecules bound to the active site metal along with four protein side chains making up the homodimer of the enzyme: His5 A-subunit, Glu56 A-subunit, His74 B-subunit, Glu122 B-subunit. The inactive Zn2+-bound enzyme has the same four protein side chains bound to the metal, but only one water molecule is coordinated to the Zn2+
homodimer
the homodimeric GlxI of Escherichia coli consists of two identical polypeptide chains with one tryptophan on each chain on position 61, with two symmetrical active sites where one metal ion has been observed in each individual active site. One active site binds to the Ni2+ ion, and the other active site is observed to be more selelective for a potent inhibitor
homodimer
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2 * 20647, sequence calculation, 2 * 21000, recombinant enzyme, SDS-PAGE
homodimer
2 * 20810, calculated from sequence, MALDI-TOF mass spectrometry, SDS-PAGE
homodimer
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mammalian glyoxalase I is composed of two equal subunits which both harbor an acitve site
monomer
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the monomeric enzyme has two different active sites with similar kcat values, but distinct Km values. Both active sites adopt two discrete conformations and are allosterically coupled in a substrate concentration-dependent manner
monomer
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treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione
monomer
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single polypeptide with two active sites that catalyze the same reaction
homology-based structural modeling, overview
additional information
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enzyme is composed of a single polypeptide chain containing two active sites. It has been shown that there is a allosteric coupling between the two active sites