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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

Reaction

(R)-S-lactoylglutathione
=
glutathione
+
2-oxopropanal

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

     4 Lyases
         4.4 Carbon-sulfur lyases
             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
                4.4.1.5 lactoylglutathione lyase

Engineering

Engineering on EC 4.4.1.5 - lactoylglutathione lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H5Q
-
active in the presence of both Ni2+ and Zn2+
H74Q
the native His74 metal ligand substituted with a Gln residue, maintains a homodimeric quaternary structure in solution as does the wild-type enzyme
A111E
-
the mutation is associated with an increased risk of this neoplasia in breast cancer
E111A
-
the mutation is associated with estrogen-negative breast cancer
E172Q
-
100000fold lower activity than wild-type
E99Q
-
10000fold lower activity than wild-type
E99Q/Q33E
-
100fold lower activity than wild-type
S44A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S68A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
S93A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T101A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
T106A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, phosphorylation of GLO1 is completely abolished
T97A
-
co-expressed with calcium, calmodulin-dependent protein kinase II, extensively phosphorylated, Western blot analysis
E145Q
the mutant shows altered thermodynamic parameters for Ni2+ ion binding compared to the wild-type enzyme
E209D
inactive mutant
E78Q
the mutant shows altered thermodynamic parameters for Ni2+ ion binding compared to the wild-type enzyme
E161Q
-
maximum catalytic efficiency is 60% of the wild-type enzyme
E161Q/E272Q
-
maximum catalytic efficiency is 60% of the wild-type enzyme
E161Q/E345Q
-
almost completely inactivated
E161Q/R186/E272Q
-
kinetics are biphasic
E272Q
-
maximum catalytic efficiency is 60% of the wild-type enzyme
E345Q
-
kinetics are biphasic, maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5
E91Q
-
maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5
E91Q/E345Q
-
maximum catalytic efficiency is 7% of the wild-type enzyme
R22E
-
decreased substrate affinity
R22E/E91Q/E345Q
-
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
DELTAglo1
-
glyoxalase I null mutant
E163Q
-
58% of wild-type kcat
E163Q/E318Q
-
0.02% of wild-type kcat
E318Q
-
16% of wild-type kcat
YEpGLO1
-
overexpressing mutant, shows increased methylglyoxal resistance
additional information