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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Metals Ions
Metals Ions on EC 4.4.1.5 - lactoylglutathione lyase
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Ca2+
Cd2+
Co2+
CuSO4
0.2 mM, extracellular, 30fold upregulated protein spot in the 2D-electrophoresis, identified as glyoxalase I, the expression is regulated by the operon yahCD-yaiAB
Fe2+
methylglyoxal
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10 mM, enhanced tolerance to toxic stress in transgenic Vigna mungo
Mg2+
Mn2+
NaCl
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the transgenic and the untransformed plants are exposed to 100 mM NaCl. The transgenic plants survived whereas the untransformed control plants fail to survive
Ni2+
Zn2+
additional information
Cd2+
activation, Km: 0.0089 mM, Vmax: 0.043 mmol/min/mg, kcat: 21 1/s
Cd2+
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can partially substitute for Zn2+, the proton-transfer step is partially rate-limiting for the Cd2+ -substituted enzyme utilizing alpha-deuterophenylglyoxal as substrate
Cd2+
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in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Cd2+
reactivates GloA3 by 87% after treatment with dipicolinic acid
Co2+
activation, Km: 0.012 mM, Vmax: 0.213 mmol/min/mg, kcat: 106 1/s
Co2+
GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies
Co2+
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1 mM, increases activity more than 100%. 1 mM restores 80% of the activity of the apoenzyme
Co2+
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in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Co2+
increases GloA2 activity, hyper-reactivates GloA3 by 115% after treatment with dipicolinic acid
Co2+
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major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Fe2+
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at least one iron per enzyme molecule, the second metal is zinc or manganese, apparantly depending on growth conditions
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incubation of the Zn2+ depleted apoenzyme with Mg2+ restores 50% of the enzyme activity
Mg2+
reactivates GloA3 by 26% after treatment with dipicolinic acid
Mn2+
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in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Mn2+
hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
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required for activity, dependent on, Ni2+ -activation class, the active Ni2+ -bound enzyme has an octahedral geometry
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+
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activates, Ni2+ -activation class, only one Ni2+ is needed for full enzyme activation
Ni2+
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in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Ni2+
dependent on, required for activity, Glu145 and Glu209 are involved in Ni2+ binding, Glu78 is not involved, the monomeric enzyme possesses a single Ni2+ coordination site despite containing two GLY I domains, 0.052 mol/mol enzyme for the recombinant enzyme expressed in Escherichia coli, and 1.258 mol/mol enzyme after exogenous addition of Ni2+
Ni2+
activation, Km: 0.021 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+
increases GloA2 activity, hyper-reactivates GloA3 by 146% after treatment with dipicolinic acid
Ni2+
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major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
Zn2+
4fold higher glyoxalase I activity when glyoxalase is isolated from Zn2+-grown bacteria
Zn2+
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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+
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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+
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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+
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in decreasing order of activation: Ni2+, Co2+, Cd2+, Mn2+, Zn2+
Zn2+
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addition of ZnSO4 during the overexpression results in increased catalytic activity and a decreased Km value
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+
does not increase GloA2 activity, GloA3 contains Zn2+, reactivates GloA3 by 76% after treatment with dipicolinic acid
Zn2+
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two zinc ions per dimer. The zinc is required for structure and function. The monomer contains a single zinc ion
Zn2+
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apoenzyme is catalytically inactive, but is partially restored by Zn2+
Zn2+
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major activation by Ni2+ and Co2+ but also exhibits some measureable activation by Zn2+
no activation by Zn2+, poor activity with Ca2+ and Mg2+, the active site geometry of the Ni2/Co2-activated enzyme forms an octahedral coordination with one metal atom, two water molecules, and four metal-binding ligands, while the inactive Zn2-bound enzyme form possesses a trigonal bipyramidal geometry with only one water molecule liganded to the metal center
additional information
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no activation by Zn2+, poor activity with Ca2+ and Mg2+, the active site geometry of the Ni2/Co2-activated enzyme forms an octahedral coordination with one metal atom, two water molecules, and four metal-binding ligands, while the inactive Zn2-bound enzyme form possesses a trigonal bipyramidal geometry with only one water molecule liganded to the metal center
additional information
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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
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not activated by Zn2+, Zn2+ can bind to the enzyme, but the resulting enzyme is inactive. Mg2+ does not bind to the apoGlxI as determined by isothermal titration calorimetry
additional information
not activated by Zn2+, Zn2+ can bind to the enzyme, but the resulting enzyme is inactive. Mg2+ does not bind to the apoGlxI as determined by isothermal titration calorimetry
additional information
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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
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a wide range of bivalent metal ions can substitute for zinc in glyoxalase I from mammalian sources, and several of them afford enzyme activities of similar magnitude to the zinc-containing glyoxalase I
additional information
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Mg2+, Ca2+, Zn2+ no increase in enzyme activity
additional information
no activating effect by Zn2+, Ca2+, Fe2+, and Mn2+
additional information
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Mg2+, Ca2+, Zn2+ no increase in enzyme activity
additional information
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broad metal-activation profile of the enzyme, the mechanism probably involves the formation of an enediol(ate) reaction intermediate
additional information
no activation by Zn2+
additional information
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no activation by Zn2+