1.1.1.39: malate dehydrogenase (decarboxylating)
This is an abbreviated version!
For detailed information about malate dehydrogenase (decarboxylating), go to the full flat file.
Word Map on EC 1.1.1.39
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1.1.1.39
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nadp
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fumarate
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nadp+-dependent
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l-malate
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alpha-glycerophosphate
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hydrogenosomes
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crassulacean
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nad+-malic
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alpha-gpd
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synthesis
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medicine
- 1.1.1.39
- nadp
- fumarate
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nadp+-dependent
- l-malate
- alpha-glycerophosphate
- hydrogenosomes
-
crassulacean
-
nad+-malic
-
alpha-gpd
- synthesis
- medicine
Reaction
Synonyms
AT2g13560, At4g00570, AZC3656 protein, cytosolic malic enzyme, decarboxylating NAD-malic enzyme, dehydrogenase, malate, diphosphate nucleotide dependent malic enzyme, DMA, DME, m-NAD-ME, malic enzyme, malic enzyme 2, malic enzyme-NAD, ME, ME-NAD, ME1, ME2, mitochondrial malic enzyme, mitochondrial NAD(P)+-dependent malic enzyme, mitochondrial NAD+-dependent malic enzyme, mitochondrial NAD-malic enzyme, mNAD-ME1, mNAD-ME2, NAD(P)+-malic enzyme, NAD+-dependent malic enzyme, NAD-dependent malate dehydrogenase (decarboxylating), NAD-dependent malic enzyme, NAD-dependent malic enzyme 1, NAD-dependent malic enzyme 2, NAD-malate dehydrogenase, NAD-malic enzyme, NAD-ME, NAD-ME1, NAD-ME2, NAD-MEH, NAD-preferring malic enzyme, NAD-preferring ME, NAD-specific malic enzyme, pyruvic-malic carboxylase
ECTree
1.1.1.39 malate dehydrogenase (decarboxylating)Advanced search results
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results (Engineering
Engineering on EC 1.1.1.39 - malate dehydrogenase (decarboxylating)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R50A
site-directed mutagenesis, the mutant does not show altered kinetics after addition of fumarate
R80A
site-directed mutagenesis, the mutant shows altered kinetics after addition of fumarate
R84A
site-directed mutagenesis, the mutant does not show altered kinetics after addition of fumarate
K143A
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site-directed mutagenesis, malate binding residue, mutant shows highly increased kcat for malate and fumarate compared to the wild-type enzyme
K362H
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the mutant enzyme displays a considerable elevation in Km for NADP+, and the kcat for NAD+ value is elevated compared to the wild-type enzyme
N434A
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site-directed mutagenesis, the interaction of the 434 position residue with malate is lost in the mutant, causing malate to reorient itself, leading to a slower decarboxylation
N434E
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site-directed mutagenesis, the longer glutamine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
N434M
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site-directed mutagenesis, the longer methionine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
N479Q
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site-directed mutagenesis, the stepwise oxidative decarboxylation mechanism observed for the wild-type enzyme changed to a concerted one, which is totally rate limiting, for the N479Q mutant enzyme
N479S
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site-directed mutagenesis, the mutant with the shorter serine side chain shows very similar values of KNAD+, Kmalate, and isotope effects relative to the wild-type enzyme, but V/Et is decreased 2000fold due to an increased freedom of rotation, resulting in nonproductively bound cofactor
R105A
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site-directed mutagenesis, fumarate binding residue, mutant shows 7-8fold reduced initial velocity with malate and Mg2+ compared to the wild-type enzyme, and is no longer activated by fumarate and malate
R181K
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site-directed mutagenesis, the mutant shows a 100fold increase in the Km for malate, a 30fold increase in the Ki for oxalate, and a 10fold increase in Ki for NADH, but only a slight or no change in KNAD compared to the wild-type enzyme
R181Q
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site-directed mutagenesis, the mutant shows a 100fold increase in the Km for malate, a 30fold increase in the Ki for oxalate, and a 10fold increase in Ki for NADH, but only a slight or no change in KNAD compared to the wild-type enzyme. The activity of the R181Q mutant can be partially rescued by ammonium ion likely by binding in the pocket vacated by the guanidinium group of R181
S433A
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site-directed mutagenesis, KNAD+ for the S433A mutant enzyme is increased by 80fold compared to the wild-type enzyme
S433C
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site-directed mutagenesis, the mutant enzyme exhibits 9fold and 500fold increases in Kmalate and KNAD, respectively, compared to the wild-type enzyme
additional information
additional information
construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
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construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
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construction of two chimeras NADME1q and NAD-ME2q by interchanging the first 176 amino residues between NAD-ME1 and -2, altered regulation in comparison to the wild-type enzymes, overview
additional information
construction of two chimeras NADME1q and NAD-ME2q by interchanging the first 176 amino residues between NAD-ME1 and -2, altered regulation in comparison to the wild-type enzymes, overview
additional information
construction of two chimeras NADME1q and NAD-ME2q by interchanging the first 176 amino residues between NAD-ME1 and -2, altered regulation in comparison to the wild-type enzymes, overview
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of chimeric protein NAD-ME1q, which is composed of the first 176 amino acid residues of isozyme NAD-ME2 and the central and C-terminal sequence of isozyme NAD-ME1, exhibits a significantly lower Km L-malate value than the parental isoforms and a hyperbolic behavior that is not modified by fumarate
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of chimeric protein NAD-ME1q, which is composed of the first 176 amino acid residues of isozyme NAD-ME2 and the central and C-terminal sequence of isozyme NAD-ME1, exhibits a significantly lower Km L-malate value than the parental isoforms and a hyperbolic behavior that is not modified by fumarate
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of the chimeric protein NAD-ME2q, that possesses the first 176 amino acid residues of NAD-ME1 and the central and C-terminal sequence of NAD-ME2, presents a sigmoidal L-malate response similar to the one for NAD-ME1, but also a higher Km L-malate value and a lower kcat value. NAD-ME2q is activated by fumarate and an increase in its concentration produces a decrease in Km and nH values. At 4 mM fumarate, the Lmalate saturation curve is hyperbolic (nH = 1.1) with an 8fold decrease in Km value. There are no significant changes in kcat value by addition of fumarate, which implies a 9fold increase in NAD-ME2q catalytic efficiency when compared to the enzyme in the absence of fumarate
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of the chimeric protein NAD-ME2q, that possesses the first 176 amino acid residues of NAD-ME1 and the central and C-terminal sequence of NAD-ME2, presents a sigmoidal L-malate response similar to the one for NAD-ME1, but also a higher Km L-malate value and a lower kcat value. NAD-ME2q is activated by fumarate and an increase in its concentration produces a decrease in Km and nH values. At 4 mM fumarate, the Lmalate saturation curve is hyperbolic (nH = 1.1) with an 8fold decrease in Km value. There are no significant changes in kcat value by addition of fumarate, which implies a 9fold increase in NAD-ME2q catalytic efficiency when compared to the enzyme in the absence of fumarate
additional information
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method optimization of the reverse reaction of the malic enzyme for HCO3- fixation into pyruvic acid to produce L-malic acid with NADH generation including the activity of glucose-6-phosphate dehydrogenase, EC1.1.1.49, from Leuconostoc mesenteroides
additional information
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method optimization of the reverse reaction of the malic enzyme for HCO3- fixation into pyruvic acid to produce L-malic acid with NADH generation including the activity of glucose-6-phosphate dehydrogenase, EC1.1.1.49, from Leuconostoc mesenteroides
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additional information
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stable knockdown of ME2 in K-562 tumor cells using three independent shRNA hairpins targeting ME2, effects on K562 cell proliferation, knockout of ME2 induces erythroid differentiation, phenotype, detailed overview
additional information
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siRNA knockdown of malic enzyme isozyme by 50% affects pyruvate carboxylase flux of the pyruvate derived from glutamate metabolism, insulin secretion in response to membrane depolarization using potassium chloride is unaffected by siRNA knockdown of malic enzyme, overview
additional information
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siRNA knockout of ME2 in INS-1 832/13 beta-cells, siRNA knockdown and isotopic labeling strategies, method optimization, overview
additional information
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generation of Me1 single and double knockdown cell lines, thereby generating cell line 753(H)/Me1-753(P), overview. The level of Me1 mRNA in the double-knockdown cell line Me1-753(H)/Me1-753(P) is decreased to 2% as compared with 14% in the single knockdown Me1-753(H) cell line. The level of Me2mRNAis lowered by only 10% in the Me1-753(H) cell line and Me3 mRNA is lowered by only 27% in the Me1-753(H) cell line and lowered by only 35% in the Me1-753(H)/Me1-753(P) cell line. Resident siRNA might interfere with the expression of the siRNA expressed from the second vector. Knockdown of isozyme ME3, EC 1.1.1.40, but not ME1 or ME2 (both EC 1.1.1.39) alone or together, inhibits insulin release stimulated by glucose, pyruvate or 2-aminobicyclo [2,2,1]heptane-2-carboxylic acid-plus-glutamine. In the Me3 double-knockdown cells, the level of Me1 mRNA is not significantly decreased in the Me3-628(P)/Me2-725(H) and Me3-1672(P)/Me2-725(H) cell lines. However, a 32%, 49%, and 47% decrease in ME1 activity is observed in the cell lines Me3-628(P), Me3-628(P)/Me2-725(H), and Me3-628(P)/Me2-2124(H), respectively
additional information
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expression of the tme gene, EC 1.1.1.40, under the control of the dme promoter, cannot restore the N2 fixation activity which is lost in dme mutant cells in alfalfa root nodules, despite elevated levels of TME within bacteroids, no symbiotic nitrogen fixation occurs in dme mutant strains, overview
additional information
azc3656 mutants show about 4fold reduced NAD+-malic enzyme activity
additional information
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azc3656 mutants show about 4fold reduced NAD+-malic enzyme activity
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