4.2.3.3: methylglyoxal synthase
This is an abbreviated version!
For detailed information about methylglyoxal synthase, go to the full flat file.
Word Map on EC 4.2.3.3
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4.2.3.3
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meibomian
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glass
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film
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tear
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ocular
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eyelid
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gather
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grading
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grimace
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saccade
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dihydroxyacetone
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mongolian
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gerbil
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glory
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microgels
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monoglycerides
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dropout
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break-up
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1,2-propanediol
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ductility
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schirmer
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sire
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dhap
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polydactyly
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alloy
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phantom
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corrosion
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microtia
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orifice
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encephalocele
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cdt1
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orc6
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pre-replication
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synthesis
- 4.2.3.3
-
meibomian
-
glass
-
film
- tear
-
ocular
-
eyelid
-
gather
-
grading
-
grimace
-
saccade
- dihydroxyacetone
-
mongolian
- gerbil
-
glory
-
microgels
- monoglycerides
-
dropout
-
break-up
- 1,2-propanediol
-
ductility
-
schirmer
-
sire
- dhap
- polydactyly
-
alloy
-
phantom
-
corrosion
- microtia
-
orifice
- encephalocele
- cdt1
- orc6
-
pre-replication
- synthesis
Reaction
Synonyms
EC 4.2.99.11, methylglyoxal synthase, methylglyoxal synthetase, MGS, MgsA, msgA, synthase, methylglyoxal
ECTree
4.2.3.3 methylglyoxal synthaseAdvanced search results
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results (Engineering
Engineering on EC 4.2.3.3 - methylglyoxal synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Q62R
D101E
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reduced ratio of turnover-numer:Km-value by about 10000fold compared to the wild-type enzyme
D101N
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reduced ratio of turnover-numer:Km-value by about 10000fold compared to the wild-type enzyme
D71E
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reduced ratio of turnover-numer:Km-value by about 1000fold compared to the wild-type enzyme
D71N
H98Q
250fold lower catalytic activity than wild-type enzyme, change in conformation
DELTAR97
strong decrease in activity, increase in Hill coefficient from 1 of wild-type to 3.3
G56A
significant increase in Hill coefficient, large decrease in turnover number
G56S
significant increase in Hill coefficient, large decrease in turnover number
R97E
strong decrease in activity, increase in Hill coefficient from 1 of wild-type to 3.4
R97K
V101I
mutant has lost its heterotropic cooperativity, exhibits homotropic allostery, displays significantly reduced catalytic efficiency
V101S
mutant has lost its heterotropic cooperativity, exhibits homotropic allostery, displays significantly reduced catalytic efficiency
D100N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D100V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R80D/D100R
the mutant shows increased catalytic efficiency compared to the wild type enzyme
R80I
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R80K
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R80Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information
D71N
-
reduced ratio of turnover-numer:Km-value by about 1000fold compared to the wild-type enzyme
R97K
mutant has lost its heterotropic cooperativity, exhibits homotropic allostery, displays significantly reduced catalytic efficiency
R97K
strong decrease in activity, increase in Hill coefficient from 1 of wild-type to 1.5
additional information
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mutant lacking ten amino acids from C-terminal tail shows homotropic cooperative behavior in presence of dihydroxyacetone phosphate and is not only more flexible but also less stable compared to wild-type
additional information
a mutant carrying one additional His residue between residues Arg22 and His23 shos remarkable increase in thermostability, whereas a mutant carrying two additional His residues between residues Arg22 and His23 is very unstable. Replacing His23 in the latter mutant by Ala leads to a decrease in half-lifecompared to wild-type, but increase compared to the original mutant
additional information
mutant enzyme with C-terminal extension YQRYLADRLK to arrange a salt bridge between Arg140 and the proximal aspartate at position 10. Mutant shows an increase in Hill coefficient from 1.5 of wild-type to 1.99 and an increase in thermostability. Introduction of mutation D10N in this mutant reverts the Hill coefficient to 1.44
additional information
mutant protein carrying the C-terminal tail of Escherichia coli enzyme containing an Arg residue shows elevated cooperativity in the presence of phosphate
