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Information on EC 4.1.3.32 - 2,3-Dimethylmalate lyase
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EC Tree
4.1.3.32 2,3-Dimethylmalate lyaseSpecify your search results
Word Map
- 4.1.3.32
-
nicotinic
- barkeri
- clostridium
- phosphoenolpyruvate
- propionate
- icl
- niger
- tuberculosis
- oxalate
-
gem-diol
- isocitrate
-
racemic
- dimethylmaleate
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2,3-dimethylmalate lyase, (2r,3s)-dimethylmalate lyase, an07g08390, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(2R,3S)-dimethylmalate lyase
DMML
Lyase, 2,3-dimethylmalate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2R,3S)-2,3-dimethylmalate = propanoate + pyruvate
cleavage reaction on (2R,3S)-2,3-dimethylmalate lyase proceeds with inversion of configuration at C-3 of the substrate which becomes C-2 of propanoate
-
(2R,3S)-2,3-dimethylmalate = propanoate + pyruvate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(2R,3S)-2,3-dimethylmalate pyruvate-lyase (propanoate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
73562-28-4
-
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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
2,3-Dimethylmalate
Propanoate + pyruvate
-
(2R,3S)-2,3-dimethylmalate
-
?
2,3-Dimethylmalate
Propanoate + pyruvate
-
(2R,3S)-2,3-dimethylmalate
-
?
additional information
?
-
(2R,3S)-isocitrate, (R)-malate, (S)-malate, (2S)-methylmalate, (3S)-isopropylmalate, 3-butylmalate, phosphonopyruvate, carboxyphenolpyruvate, 3,3-difluoroxaloacetate, oxalate are no substrates
-
-
?
additional information
?
-
-
(2R,3S)-isocitrate, (R)-malate, (S)-malate, (2S)-methylmalate, (3S)-isopropylmalate, 3-butylmalate, phosphonopyruvate, carboxyphenolpyruvate, 3,3-difluoroxaloacetate, oxalate are no substrates
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-
?
additional information
?
-
(2R,3S)-isocitrate, (R)-malate, (S)-malated, (2S)-methylmalate, (3S)-isopropylmalate, 3-butylmalate, phosphonopyruvate, carboxyphosphoenolpyruvate, 3,3-difluoroxaloacetate, and oxalate are no substrates
-
-
?
additional information
?
-
-
(2R,3S)-isocitrate, (R)-malate, (S)-malated, (2S)-methylmalate, (3S)-isopropylmalate, 3-butylmalate, phosphonopyruvate, carboxyphosphoenolpyruvate, 3,3-difluoroxaloacetate, and oxalate are no substrates
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-
?
additional information
?
-
DMML also possesses significant oxaloacetate acetyl hydrolase activity
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-
?
additional information
?
-
-
DMML also possesses significant oxaloacetate acetyl hydrolase activity
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-
?
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
influence of Mg2+ on the equilibrium, inhibition at high concentration
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
(2R,3S)-isocitrate, (R)-malate, (S)-malate, and carboxyphosphoenolpyruvate are not inhibitors
-
additional information
-
(2R,3S)-isocitrate, (R)-malate, (S)-malate, and carboxyphosphoenolpyruvate are not inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.17
(2R)-ethyl-(3S)-methylmalate
wild type enzyme, at pH 7.5 and 25°C
1.17
(2R)-ethyl-(3S)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
12
(2R)-ethylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
2.2
(2R)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
2.7
(2R)-propyl-(3S)-methylmalate
wild type enzyme, at pH 7.5 and 25°C
2.7
(2R)-propyl-(3S)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
12
(2R,3S)-2-methylisocitrate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.036
(2R,3S)-dimethylmalate
mutant enzyme C124A, at pH 7.5 and 25°C
0.036
(2R,3S)-dimethylmalate
mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.22
(2R,3S)-dimethylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
3.6
(2R,3S)-dimethylmalate
mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
4.1
(2R,3S)-dimethylmalate
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25°C)
5.9
(2R,3S)-dimethylmalate
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
6
(2R,3S)-dimethylmalate
mutant enzyme D59S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
7.4
(2R,3S)-dimethylmalate
mutant enzyme D59A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
12
(2S,3R)-2-methylisocitrate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.2
(2R,3S)-2,3-dimethylmalate
-
pH and temperature not specified in the publication
0.00001
3,3-difluorooxaloacetate
-
kcat less than 0.00001 sec-1, pH and temperature not specified in the publication
63
(2R)-ethyl-(3S)-methylmalate
wild type enzyme, at pH 7.5 and 25°C
63
(2R)-ethyl-(3S)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
4.4
(2R)-ethylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
2.6
(2R)-methylmalate
-
pH and temperature not specified in the publication
2.64
(2R)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.79
(2R)-propyl-(3S)-methylmalate
wild type enzyme, at pH 7.5 and 25°C
0.79
(2R)-propyl-(3S)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.13
(2R,3S)-2-methylisocitrate
wild type enzyme, at pH 7.5 and 25°C
0.13
(2R,3S)-2-methylisocitrate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.00001
(2R,3S)-dimethylmalate
mutant Y44F, smaller than 0.00001 s-1
0.00001
(2R,3S)-dimethylmalate
mutant enzyme Y44F, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.000121
(2R,3S)-dimethylmalate
mutant enzyme C124S, at pH 7.5 and 25°C
0.000121
(2R,3S)-dimethylmalate
mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.00014
(2R,3S)-dimethylmalate
mutant enzyme D59S, at pH 7.5 and 25°C
0.00014
(2R,3S)-dimethylmalate
mutant enzyme D59S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.000178
(2R,3S)-dimethylmalate
mutant enzyme C124A, at pH 7.5 and 25°C
0.000178
(2R,3S)-dimethylmalate
mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.000427
(2R,3S)-dimethylmalate
mutant enzyme D59A, at pH 7.5 and 25°C
0.000427
(2R,3S)-dimethylmalate
mutant enzyme D59A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
2.8
(2R,3S)-dimethylmalate
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25°C)
11.7
(2R,3S)-dimethylmalate
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
19.2
(2R,3S)-dimethylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.13
(2S,3R)-2-methylisocitrate
wild type enzyme, at pH 7.5 and 25°C
0.13
(2S,3R)-2-methylisocitrate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.00001
(S)-malate
-
kcat less than 0.00001 sec-1, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
50
(2R)-ethyl-(3S)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.1
(2R)-ethylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
1
(2R)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.3
(2R)-propyl-(3S)-methylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.01
(2R,3S)-2-methylisocitrate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.01
(2S,3R)-2-methylisocitrate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.005
(2R,3S)-dimethylmalate
mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
20
(2R,3S)-dimethylmalate
mutant enzyme D59S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
30
(2R,3S)-dimethylmalate
mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
60
(2R,3S)-dimethylmalate
mutant enzyme D59A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
90
(2R,3S)-dimethylmalate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
700000
(2R,3S)-dimethylmalate
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25°C)
2000000
(2R,3S)-dimethylmalate
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5