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Information on EC 4.2.3.3 - methylglyoxal synthase and Organism(s) Escherichia coli and UniProt Accession P0A731
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4.2.3.3 methylglyoxal synthaseIUBMB Comments
Does not act on D-glyceraldehyde 3-phosphate.
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Word Map
- 4.2.3.3
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meibomian
-
glass
-
film
- tear
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ocular
-
eyelid
-
gather
-
grading
-
grimace
-
saccade
- dihydroxyacetone
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mongolian
- gerbil
-
glory
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microgels
- monoglycerides
-
dropout
-
break-up
- 1,2-propanediol
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ductility
-
schirmer
-
sire
- dhap
- polydactyly
-
alloy
-
phantom
-
corrosion
- microtia
-
orifice
- encephalocele
- cdt1
- orc6
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pre-replication
- synthesis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mgs, methylglyoxal synthase, methylglyoxal synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methylglyoxal synthetase
-
-
-
-
MGS
-
-
-
-
synthase, methylglyoxal
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
Does not act on D-glyceraldehyde 3-phosphate.
CAS REGISTRY NUMBER
COMMENTARY
37279-01-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycerone phosphate
methylglyoxal + phosphate
-
the unregulated production of methylglyoxal appears to be due to a rapid increase in the glycolysis intermediates from ribose degradation. Such a metabolic burden may result in methylglyoxal production by methylglyoxal synthase
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
catalyzes the elimination reaction of DHAP, which leads to phosphate and the enol of methylglyoxal, which is subsequently tautomerized to methylglyoxal in solution
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
converts dihydrocyacetone phosphate to enol pyruvaldehyde, this enol then tautomerizes to methylglyoxal in solution
-
?
dihydroxyacetone phosphate
?
-
first enzyme in the reaction sequence for the conversion of dihydroxyacetone phosphate to pyruvate, may play a role in the control of glycolysis
-
-
?
dihydroxyacetone phosphate
?
-
during elevated metabolism, the synthesis of methylglyoxal from dihydroxyacetone phosphate temporarily relieves the cells from stress caused by phosphorylated intermediates and allows the cells to grow for a limited time. If during this period the environment changes, e.g. the level of the carbon source is reduced, the cells are not only able to survive but are also able to colonize their environment
-
-
?
dihydroxyacetone phosphate
?
-
the enzyme plays an important role in the catabolism of the triose phosphates
-
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
-
the true product of the enzymatic reaction is the enol form of methylglyoxal which is ketonized in solution
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
converts dihydrocyacetone phosphate to a cis-enediolic intermediate, then catalyses the elimination of phosphate to form the enol of methylglyoxal
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
-
intermediate is enol pyruvaldehyde is stereospecifically formed
-
?
additional information
?
-
enzyme dos no catalyze the elimination reaction with glyceraldehyde phosphate
-
?
additional information
?
-
enzyme is not capable of abstracting the C2 proton from glyceraldehyde phosphate, which is an absolute requirement for the function of MGS
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycerone phosphate
methylglyoxal + phosphate
-
the unregulated production of methylglyoxal appears to be due to a rapid increase in the glycolysis intermediates from ribose degradation. Such a metabolic burden may result in methylglyoxal production by methylglyoxal synthase
-
-
?
dihydroxyacetone phosphate
?
-
first enzyme in the reaction sequence for the conversion of dihydroxyacetone phosphate to pyruvate, may play a role in the control of glycolysis
-
-
?
dihydroxyacetone phosphate
?
-
during elevated metabolism, the synthesis of methylglyoxal from dihydroxyacetone phosphate temporarily relieves the cells from stress caused by phosphorylated intermediates and allows the cells to grow for a limited time. If during this period the environment changes, e.g. the level of the carbon source is reduced, the cells are not only able to survive but are also able to colonize their environment
-
-
?
dihydroxyacetone phosphate
?
-
the enzyme plays an important role in the catabolism of the triose phosphates
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
acts as competitive inhibitor on the H98Q variant and as an allosteric-type inhibitor on the wild-type enzyme
Phosphoglycolate
inhibits wild-type enzyme and activates H98Q variant
phosphoglycolohydroxamic acid
-
tight binding inhibitor, neither a strictly competitive, non-competitive, nor uncompetitive mechanism
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, presence of phosphoglycolate
1.3
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, absence of phosphoglycolate
1.35
dihydroxyacetone phosphate
-
mutant lacking ten amino acids from C-terminal tail, Hill coefficient 1.3, pH 7.0, 60°C
2.74
dihydroxyacetone phosphate
-
wild-type, Hill coefficient 1, pH 7.0, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.96
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, absence of phosphoglycolate
6.08
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, absence of phosphoglycolate
17
dihydroxyacetone phosphate
pH 7, 25°C, H98Q mutant, presence of phosphoglycolate
2.1
dihydroxyacetone phosphate
-
mutant lacking ten amino acids from C-terminal tail, Hill coefficient 1.3, pH 7.0, 60°C
23.1
dihydroxyacetone phosphate
-
wild-type, Hill coefficient 1, pH 7.0, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
dihydroxyacetone phosphate
-
mutant lacking ten amino acids from C-terminal tail, Hill coefficient 1.3, pH 7.0, 60°C
8.4
dihydroxyacetone phosphate
-
wild-type, Hill coefficient 1, pH 7.0, 60°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with 2-phosphoglycolate, sitting drop vapor diffusion method
bound to formate and substiochiometric amounts of phosphate, hanging drop vapor diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H98Q
250fold lower catalytic activity than wild-type enzyme, change in conformation
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
D71N
additional information
-
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
D71N
-
reduced ratio of turnover-numer:Km-value by about 1000fold compared to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for avoiding impurities in the lactate production the mgsA gene is deleted
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
strains in which the genes for glycerol dehydrogenase, methylglyoxal synthase or both are overexpressed produce 1,2-propanediol as a fermentation product of glucose
synthesis
-
engineering of a functional 1,2-propanediol pathway through a combination of overexpression of genes involved in its synthesis from the key intermediate dihydroxyacetone phosphate and the manipulation of the fermentative glycerol utilization pathway, including the overexpression of methylglyoxal synthase, glycerol dehydrogenase, and aldehyde oxidoreductase. Rreplacement of the native Escherichia coli phosphoenolpyruvate-dependent dihydroxyacetone kinase with an ATP-dependent ihydroxyacetone kinase from Citrobacter freundii allows for higher 1,2-propanediol production. Ethanol is required as co-product, and inreases in 1,2-PDO titer and yield are achieved through the disruption of the pathways for acetate and lactate production. Manipulations result in an engineered Escherichia coli strain capable of producing 5.6 g/l 1,2-propanediol, at a yield of 21.3% w/w. This strain also performs well when crude glycerol is used as the substrate
synthesis
-
expressing Escherichia coli mgs gene in Corynebacterium glutamicum increases 1,2-propanediol yield 100fold. Simultaneous overexpression of mgs and cgR_2242, annotated as encoding putative aldo-keto reductase, enhances 1,2-propanediol production to 24 mM
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hopper, D.J.; Cooper, R.A.
The regulation of Escherichia coli methylglyoxal synthase a new control site in glycolysis
FEBS Lett.
13
213-216
1971
Klebsiella aerogenes, Escherichia coli, Pantoea ananatis, Providencia rettgeri, Proteus vulgaris, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Proteus vulgaris M 13, Providencia rettgeri M 9, Escherichia coli K 10, Klebsiella aerogenes SB 8, Serratia marcescens D 106
Hopper, D.J.; Cooper, R.A.
The purification and properties of Escherichia coli methylglyoxal synthase
Biochem. J.
128
321-329
1972
Escherichia coli
Summers, M.C.; Rose, I.A.
Proton transfer reactions of methylglyoxal synthase
J. Am. Chem. Soc.
99
4475-4478
1977
Escherichia coli
Ferguson, G.P.; Ttemeyer, S.; MacLean, M.J.; Booth, I.R.
Methylglyoxal production in bacteria: suicide or survival
Arch. Microbiol.
170
209-219
1998
Escherichia coli
Baskaran, S.; Rajan, D.P.; Balasubramanian, K.A.
Formation of methylglyoxal by bacteria isolated from human faeces
J. Med. Microbiol.
28
211-215
1989
Aeromonas hydrophila, Escherichia coli, Klebsiella sp., Morganella morganii, Proteus mirabilis, Proteus vulgaris, Salmonella sp., Shigella sp.
Saadat, D.; Harrison, D.H.T.
Identification of catalytic bases in the active site of Escherichia coli methylglyoxal synthase: cloning, expression, and functional characterization of conserved aspartic acid residues
Biochemistry
37
10074-10086
1998
Escherichia coli
Altaras, N.E.; Cameron, D.C.
Metabolic engineering of a 1,2-propanediol pathway in Escherichia coli
Appl. Environ. Microbiol.
65
1180-1185
1999
Escherichia coli
Ttemeyer, S.; Booth, N.A.; Nichols, W.W.; Dunbar, B.; Booth, I.R.
From famine to feast: the role of methylglyoxal production in Escherichia coli
Mol. Microbiol.
27
553-562
1998
Escherichia coli
Saadat, D.; Harrison, D.H.
Mirroring perfection: the structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate
Biochemistry
39
2950-2960
2000
Escherichia coli (P0A731)
Marks, G.T.; Harris, T.K.; Massiah, M.A.; Mildvan, A.S.; Harrison, D.H.
Mechanistic implications of methylglyoxal synthase complexed with phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR spectroscopy
Biochemistry
40
6805-6818
2001
Escherichia coli
Marks, G.T.; Susler, M.; Harrison, D.H.
Mutagenic studies on histidine 98 of methylglyoxal synthase: effects on mechanism and conformational change
Biochemistry
43
3802-3813
2004
Escherichia coli (P0A731)
Rose, I.A.; Nowick, J.S.
Methylglyoxal synthetase, enol-pyruvaldehyde, glutathione and the glyoxylase system
J. Am. Chem. Soc.
124
13047-13052
2002
Escherichia coli
Zhang, X.; Harrison, D.H.; Cui, Q.
Functional specificities of methylglyoxal synthase and triosephosphate isomerase: a combined QM/MM analysis
J. Am. Chem. Soc.
124
14871-14878
2002
Escherichia coli (P0A731)
Saadat, D.; Harrison, D.H.
The crystal structure of methylglyoxal synthase from Escherichia coli
Structure Fold. Des.
7
309-317
1999
Escherichia coli
Kim, I.; Kim, E.; Yoo, S.; Shin, D.; Min, B.; Song, J.; Park, C.
Ribose utilization with an excess of mutarotase causes cell death due to accumulation of methylglyoxal
J. Bacteriol.
186
7229-7235
2004
Escherichia coli
Grabar, T.B.; Zhou, S.; Shanmugam, K.T.; Yomano, L.P.; Ingram, L.O.
Methylglyoxal bypass identified as source of chiral contamination in l(+) and d(-)-lactate fermentations by recombinant Escherichia coli
Biotechnol. Lett.
28
1527-1535
2006
Escherichia coli (P0A731)
Yomano, L.P.; York, S.W.; Shanmugam, K.T.; Ingram, L.O.
Deletion of methylglyoxal synthase gene (mgsA) increased sugar co-metabolism in ethanol-producing Escherichia coli
Biotechnol. Lett.
31
1389-1398
2009
Escherichia coli, Escherichia coli LY160
Niimi, S.; Suzuki, N.; Inui, M.; Yukawa, H.
Metabolic engineering of 1,2-propanediol pathways in Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
90
1721-1729
2011
Escherichia coli
Clomburg, J.M.; Gonzalez, R.
Metabolic engineering of Escherichia coli for the production of 1,2-propanediol from glycerol
Biotechnol. Bioeng.
108
867-879
2011
Escherichia coli
Mohammadi, M.; Zareian, S.; Khajeh, K.
Conversion of non-allosteric methylglyoxal synthase into a homotropic allosteric enzyme by C-terminal deletion
J. Mol. Catal. B
107
95-99
2014
Escherichia coli
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