Information on EC 4.2.3.3 - methylglyoxal synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.2.3.3
-
RECOMMENDED NAME
GeneOntology No.
methylglyoxal synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycerone phosphate = methylglyoxal + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
-
Propanoate metabolism
-
-
chorismate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
Does not act on D-glyceraldehyde 3-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
37279-01-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
isolated from human faeces
-
-
Manually annotated by BRENDA team
goat
-
-
Manually annotated by BRENDA team
ATCC 824
-
-
Manually annotated by BRENDA team
SB 8
-
-
Manually annotated by BRENDA team
K 10 strain
-
-
Manually annotated by BRENDA team
strain LY160
-
-
Manually annotated by BRENDA team
isolated from human faeces
-
-
Manually annotated by BRENDA team
isolated from human faeces
-
-
Manually annotated by BRENDA team
D 1080
-
-
Manually annotated by BRENDA team
isolated from human faeces
-
-
Manually annotated by BRENDA team
M 13
-
-
Manually annotated by BRENDA team
M 9
-
-
Manually annotated by BRENDA team
Mirb.
-
-
Manually annotated by BRENDA team
isolated from human faeces
-
-
Manually annotated by BRENDA team
D 106
-
-
Manually annotated by BRENDA team
isolated from human faeces
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate
?
show the reaction diagram
dihydroxyacetone phosphate
methylglyoxal + phosphate
show the reaction diagram
glycerone phosphate
methylglyoxal + phosphate
show the reaction diagram
glycerone phosphate
pyruvaldehyde + phosphate
show the reaction diagram
-
tautomerization to methylglyoxal
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate
?
show the reaction diagram
dihydroxyacetone phosphate
methylglyoxal + phosphate
show the reaction diagram
-
-
-
-
?
glycerone phosphate
methylglyoxal + phosphate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-diphosphoglycerate
-
-
2-mercaptoethanol
-
-
2-phosphoglycerate
2-Phosphoglycolate
-
inhibits
3-bromoacetol phosphate
-
irreversible inactivation by reacting with a nucleophilic group located in the active center, dihydroxyacetone phosphate or phosphate protects
3-chloroacetol phosphate
-
competitive
3-iodoacetol phosphate
-
irreversible inactivation by reacting with a nucleophilic group located in the active center, dihydroxyacetone phosphate or phosphate protects
3-phosphoglycerate
arsenate
-
-
diphosphate
fructose 1,6-diphosphate
glucose 1-phosphate
-
-
glucose 6-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
methylglyoxal
-
linear noncompetitive inhibitor
phosphate
phosphoenolpyruvate
Phosphoglycolate
-
inhibits wild-type enzyme and activates H98Q variant
phosphoglycolohydroxamic acid
-
tight binding inhibitor, neither a strictly competitive, non-competitive, nor uncompetitive mechanism
additional information
-
no inactivation by iodoacetate or p-mercuribenzoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phosphoglycolate
-
activates H98Q variant
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 6.3
dihydroxyacetone phosphate
0.56
glycerone phosphate
allosteric enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00003 - 338
dihydroxyacetone phosphate
325
glycerone phosphate
Thermus sp. GH5
B3VH91
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00004 - 653
dihydroxyacetone phosphate
278
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000093
phosphate
-
pH 7, 25C, H98Q variant
0.0000058
Phosphoglycolate
-
pH 7, 25C, H98N variant
0.000093
phosphoglycolohydroxamic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
H98Q variant
6.8
-
H98N variant
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 8.3
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50% of maximal activity at pH 5.6 and at pH 8.3
6.6 - 7.6
-
pH 6.6: about 50% of maximal activity, pH 7.6: about 55% of maximal activity
8 - 10.5
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pH 8: about 50% of maximal activity, pH 9.5-10.5: optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
-
4 * 15000, SDS-PAGE
17000
-
4 * 17000, SDS-PAGE
26000
-
x * 26000, SDS-PAGE
31000
-
GEMMA analysis, minor peak
53000
-
gel filtration
60000
-
gel filtration
66000
-
2 * 66000, SDS-PAGE
135000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homohexamer
6 * 14300, gel filtration, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bound to formate and substiochiometric amounts of phosphate, hanging drop vapor diffusion method
-
complexed with 2-phosphoglycolate, sitting drop vapor diffusion method
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hanging drop vapor diffusion method
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sitting drop vapor diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 75
100% activity after 15 min
80
-
wild-type, half-life 3 min, mutant with C-terminal extension YQRYLADRLK, half-life 10 min
85
-
10 min, wild-type retains 84 of initial activity, mutant R97E shows complete loss of activity
100
-
1 min, complete inactivation
additional information
-
phosphate stabilizes towards both cold-induced inactivation and against heat-induced inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
D71N mutant enzyme rapidly becomes inactive in the absence of phosphate
-
dihydroxyacetone phosphate or bovine serum albumin stabilizes
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phosphate stabilizes towards both cold-induced inactivation and against heat-induced inactivation
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removal of phosphate from the purified enzyme leads to rapid loss of activity, which is more pronounced at 0C than at 22C. Dihydroxyacetone phosphate and bovine serum albumin overcome the inactivation to some extent
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 1 month
-
4C, 10 mM imidazole buffer, pH 7.0, 1 mM EDTA, 1 mM KH2PO4, 0.05% v/v 2-mercaptoethanol, 0.1-0.5 mg/ml protein, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heat shock (70C, 15 min), anion-exchange chromatography (Q-Sepharose)
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
for avoiding impurities in the lactate production the mgsA gene is deleted
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overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101E
-
reduced ratio of turnover-numer:Km-value by about 10000fold compared to the wild-type enzyme
D101N
-
reduced ratio of turnover-numer:Km-value by about 10000fold compared to the wild-type enzyme
D71E
-
reduced ratio of turnover-numer:Km-value by about 1000fold compared to the wild-type enzyme
H98N
-
50fold decrease in kcat
H98Q
-
250fold lower catalytic activity than wild-type enzyme, change in conformation
D10N
-
almost complete loss of activity
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
S55D
-
mutant has lost its allostery
S55K
-
increase in sensitivity to phosphate
V101A
-
mutant has lost its allostery
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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