1.1.1.37: malate dehydrogenase
This is an abbreviated version!
For detailed information about malate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.37
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1.1.1.37
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succinate
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isocitrate
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citrate
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isoenzymes
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oxaloacetate
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isozyme
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glucose-6-phosphate
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tricarboxylic
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aminotransferase
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phosphoenolpyruvate
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carboxylase
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hexokinase
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dismutase
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esterase
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tca
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alpha-ketoglutarate
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creatine
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fumarase
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aldolase
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carboxykinase
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transaminase
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krebs
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phosphoglucomutase
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aconitase
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gpi
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horn
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citric
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medullary
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phosphofructokinase
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6-phosphogluconate
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nadp-dependent
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trigeminal
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1.1.1.27
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allozyme
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meloidogyne
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glyoxysomal
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groes
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nadp-malate
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alpha-glycerophosphate
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watermelon
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phosphoglucose
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pqq
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monomorphic
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second-stage
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isoenzymatic
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root-knot
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perineal
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diagnostics
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drug development
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biotechnology
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analysis
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subnucleus
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quinoproteins
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medicine
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agriculture
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shsps
- 1.1.1.37
- succinate
- isocitrate
- citrate
- isoenzymes
- oxaloacetate
- isozyme
- glucose-6-phosphate
-
tricarboxylic
- aminotransferase
- phosphoenolpyruvate
- carboxylase
- hexokinase
- dismutase
- esterase
- tca
- alpha-ketoglutarate
- creatine
- fumarase
- aldolase
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carboxykinase
- transaminase
-
krebs
- phosphoglucomutase
- aconitase
- gpi
-
horn
-
citric
-
medullary
-
phosphofructokinase
- 6-phosphogluconate
-
nadp-dependent
-
trigeminal
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1.1.1.27
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allozyme
- meloidogyne
- glyoxysomal
- groes
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nadp-malate
- alpha-glycerophosphate
- watermelon
-
phosphoglucose
- pqq
-
monomorphic
-
second-stage
-
isoenzymatic
-
root-knot
-
perineal
- diagnostics
- drug development
- biotechnology
- analysis
-
subnucleus
-
quinoproteins
- medicine
- agriculture
-
shsps
Reaction
Synonyms
(R)-2-hydroxyacid dehydrogenase, (S)-malate dehydrogenase, A8B73_11505, CaMDH, cMDH, cMDH -S, cMDH-L, cyMDH, cyMDH1, cyMDH2, cyMDH3, cytMDH, cytMDH1, cytosolic malate dehydrogenase, cytosolic malate dehydrogenase 1, cytosolic MDH, cytosolic NAD-dependent malate dehydrogenase, flo16, floury endosperm16, halophilic malate dehydrogenase, HmMalDH, L-malate dehydrogenase, L-malate dehydrogenases, L-malate-NAD oxidoreductase, L-malate-NAD-oxidoreductase, L-malate: NAD oxidoreductase, L-malate: NAD+ oxidoreductase, L-malate:NAD oxidoreductase, L-malate:NAD-oxidoreductase, L-MDH, LDH-like malate dehydrogenase, ldh0076, LEUM_0076, m-MDH, malate (NAD) dehydrogenase, malate dehydrogenase, malate dehydrogenase (NAD), malate dehydrogenase 1, malate dehydrogenase 2, malate: NAD oxidoreductase, MalDH, malic acid dehydrogenase, malic dehydrogenase, mbNAD-MDH, MDH, MDH A, MDH B1, MDH B2, Mdh1, MDH2, Mdh2a, Mdh2b, Mdh3, mitochondrial malate dehydrogenase, mitochondrial MDH, mMDH, mNAD-MDH, More, NAD+ malate dehydrogenase, NAD+-dependent malate dehydrogenase, NAD+-dependent MDH, NAD+-MDH enzymes, NAD-dependent cytosolic malate dehydrogenase, NAD-dependent malate dehydrogenase, NAD-dependent MalDH, NAD-dependent malic dehydrogenase, NAD-dependent MDH, NAD-L-malate dehydrogenase, NAD-linked malate dehydrogenase, NAD-malate dehydrogenase, NAD-malic dehydrogenase, NAD-MDH, NAD-specific malate dehydrogenase, NADP+-dependent malate dehydrogenase, Pcal_1699, pdNAD-MDH, peroxisomal malate dehydrogenase, peroxisomal NAD+-malate dehydrogenase 1, peroxisomal NAD+-malate dehydrogenase 2, plastid-localized NAD-dependent MDH, plastidial NAD+-dependent malate dehydrogenase, plastidial NAD-dependent malate dehydrogenase, plastidial NAD-dependent malate dehydrogenase 1, plNAD-MDH, PMDH, PMDH1, PMDH2, regulatory subunit of nucleic acid-conducting channel, s-MDH, SrMalDH, TaMDH, VEG69, Vegetative protein 69, YlMdh2p, [LDH-like] MDH
ECTree
1.1.1.37 malate dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.1.1.37 - malate dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C125S
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the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C131S
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the mutant of isoform cyMDH3 shows decreased activity compared to the wild type enzyme
C155S
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the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C161S
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the mutant of isoform cyMDH3 shows decreased activity compared to the wild type enzyme
C252S
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the mutant of isoform cyMDH1 shows strongly decreased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C258S
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the mutant of isoform cyMDH3 shows decreased activity compared to the wild type enzyme
C292S
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the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C2S
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the mutant of isoform cyMDH3 shows strongly increased activity compared to the wild type enzyme
C330S
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the mutant of isoform cyMDH1 shows slightly decreased activity compared to the wild type enzyme and is not inhibited by diamide. The mutant of isoform cyMDH2 shows decreased activity compared to the wild type enzyme and is not inhibited by diamide
C79S
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the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
C85S
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the mutant of isoform cyMDH3 shows slightly decreased activity compared to the wild type enzyme
E165K
increase in temperature-optimum to 65°C, compared to 60°C for the wild-type enzyme. Maximal specific activity at temperature optimum is increased by about 30% compared to wild-type enzyme. Melting temperature at pH 4.4 is by 4.6°C, melting temperature at pH 6.0 is increased by 12.0°C and melting temperature at pH 7.5 is increased by 23.9°C compared to wild-type enzyme, mutation stabilizes to such an extent that disruption of the inter-dimer electrostatic network around residue 165 no longer limits kinetic thermal stability
E165Q
increase in temperature-optimum to 65°C, compared to 60°C for the wild-type enzyme. Maximal specific activity at temperature optimum is increased by about 30% compared to wild-type enzyme. Melting temperature at pH 4.4 is by 5.4°C, melting temperature at pH 6.0 is increased by 11.2°C and melting temperature at pH 7.5 is increased by 23.6°C compared to wild-type enzyme, mutation stabilizes to such an extent that disruption of the inter-dimer electrostatic network around residue 165 no longer limits kinetic thermal stability
G210A
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme
G210A/V214I
site-directed mutagenesis, the double mutant shows a 2.2fold increase in lacatate dehydrogenase activity compared to the wild-type enzyme
I12V/R81Q/M85E/G210A/V214I
construction of a pentamutant by site-directed mutagenesis, whose substrate specificity is switched from malate dehydrogenase to that of lactate dehydrogenase, EC 1.1.1.27, the mutant shows highly reduced activity compared to the wild-type enzyme, overview
R81Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V214I
site-directed mutagenesis, the mutant's activity is not affected
G210A
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site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme
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I12V/R81Q/M85E/G210A/V214I
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construction of a pentamutant by site-directed mutagenesis, whose substrate specificity is switched from malate dehydrogenase to that of lactate dehydrogenase, EC 1.1.1.27, the mutant shows highly reduced activity compared to the wild-type enzyme, overview
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R81Q
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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E243R
mutation does not affect enzyme activity. The mutant enzyme is more halophilic than the wild-type protein. It is more sensitive to temperature and requires significantly higher concentrations of NaCl or KCl for equivalent stability
E267R
the numbering is not equivalent to the numbering of UniProt. The E267R mutation points into a central ordered water cavity, disrupting protein-solvent interactions. The mutant enzyme requires higher concentrations of the solvent salt for stability similar to that of the wild type
K205A
site-directed mutagenesis, the oligomeric state of the mutant changes with the nature of the anion bound, the mutant is dimeric or tetrameric, overview
R100Q
the mutant enzyme has considerably higher specificity for pyruvate than for oxaloacetate. Whereas the Km value for pyruvate is increased about 2fold, that for oxaloacetate increases 30fold. The R100Q mutant is not subjected to substrate inhibition, at least not at substrate concentrations up to 30 mM, and the highest kcat value is obtained at the lowest salt concentration used (0.15 M NaCl)
R207S/R292S
E243R
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mutation does not affect enzyme activity. The mutant enzyme is more halophilic than the wild-type protein. It is more sensitive to temperature and requires significantly higher concentrations of NaCl or KCl for equivalent stability
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E267R
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the numbering is not equivalent to the numbering of UniProt. The E267R mutation points into a central ordered water cavity, disrupting protein-solvent interactions. The mutant enzyme requires higher concentrations of the solvent salt for stability similar to that of the wild type
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R100Q
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the mutant enzyme has considerably higher specificity for pyruvate than for oxaloacetate. Whereas the Km value for pyruvate is increased about 2fold, that for oxaloacetate increases 30fold. The R100Q mutant is not subjected to substrate inhibition, at least not at substrate concentrations up to 30 mM, and the highest kcat value is obtained at the lowest salt concentration used (0.15 M NaCl)
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R207S/R292S
E145A
the mutant shows severely reduced activity compared to the wild type enzyme
H172A
the mutant shows severely reduced activity compared to the wild type enzyme
N120A
the mutant shows severely reduced activity compared to the wild type enzyme
R148A
the mutant shows severely reduced activity compared to the wild type enzyme
R82A
the mutant shows severely reduced activity compared to the wild type enzyme
R88A
the mutant shows severely reduced activity compared to the wild type enzyme
T218A
the mutant shows severely reduced activity compared to the wild type enzyme
H229Q
mutant enzyme is less resistant to heat denaturation than the wild-type enzyme
Q229H
mutant enzyme is more resistant to heat denaturation than the wild-type enzyme
H229Q
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mutant enzyme is less resistant to heat denaturation than the wild-type enzyme
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Q229H
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mutant enzyme is more resistant to heat denaturation than the wild-type enzyme
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additional information
R207S/R292S
site-directed mutagenesis, the oligomeric state of the mutant changes with the nature of the anion bound, the mutant is dimeric or tetrameric, overview
R207S/R292S
the numbering is not equivalent to the numbering of UniProt. The active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. The mutant enzyme requires higher salt concentrations than the wild type for stability. Thermal inactivation starts at 35°C, whereas the wild type is stable up to 60°C. At 4 M NaCl (pH 8) the kinetics of unfolding of the mutant is measured by following the fluorescence emission during incubation at various temperatures. The process is biphasic between 35 and 48 °C, while the thermal deactivation kinetics of the wild type protein is first-order
R207S/R292S
the numbering is not equivalent to the numbering of UniProt. The mutations, located at the dimer-dimer interface, disrupt two inter-dimeric salt bridge clusters that are essential for wild-type tetramer stabilisation. Association of active dimers into tetramers is weakened
R207S/R292S
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the numbering is not equivalent to the numbering of UniProt. The active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. The mutant enzyme requires higher salt concentrations than the wild type for stability. Thermal inactivation starts at 35°C, whereas the wild type is stable up to 60°C. At 4 M NaCl (pH 8) the kinetics of unfolding of the mutant is measured by following the fluorescence emission during incubation at various temperatures. The process is biphasic between 35 and 48 °C, while the thermal deactivation kinetics of the wild type protein is first-order
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R207S/R292S
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the numbering is not equivalent to the numbering of UniProt. The mutations, located at the dimer-dimer interface, disrupt two inter-dimeric salt bridge clusters that are essential for wild-type tetramer stabilisation. Association of active dimers into tetramers is weakened
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additional information
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construction of enzyme-deficient mutants by pmdh1 and pmdh2 genes disruption by T-DNA insertion, mutant seedlings mobilize their triacylglycerol very slowly and growth are insensitive to 2,4-dichlorophenoxybutyric acid, phenotype, overview
additional information
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
additional information
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
additional information
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characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
additional information
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
additional information
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characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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additional information
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characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
-
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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additional information
MdcyMDH overexpression contributed to malate accumulation in the apple callus and tomato
additional information
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MdcyMDH overexpression contributed to malate accumulation in the apple callus and tomato
additional information
MdcyMDH overexpression favourably contributes to cell and plant growth and confers stress tolerance both in the apple callus and tomato
additional information
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MdcyMDH overexpression favourably contributes to cell and plant growth and confers stress tolerance both in the apple callus and tomato
additional information
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isozyme Mdh1 overexpression in yeast extends life span of the organism requiring respiration and the Sir2 family, while the mdh1DELTAaat1DELTA double mutation blocks CR-mediated life span extension and also prevents the characteristic decrease in the NADH levels in the cytosolic/nuclear pool, overview
additional information
isozyme Mdh1 overexpression in yeast extends life span of the organism requiring respiration and the Sir2 family, while the mdh1DELTAaat1DELTA double mutation blocks CR-mediated life span extension and also prevents the characteristic decrease in the NADH levels in the cytosolic/nuclear pool, overview
additional information
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adsorption of the enzyme in 30 nm diameter Au nanoparticles for synthesis of bioconjugates, MDH:Au stoichiometry and kinetic parameters determined for MDH:Au, citrate synthase CS:Au, and three types of dual-activity MDH/CS:Au bioconjugates, method development, overview. The number of enzyme molecules adsorbed per particle is dependent upon the enzyme concentration in solution, with multilayers forming at high enzyme:Au solution ratios. The specific activity of adsorbed enzyme increases with increasing number adsorbed per particle for CS:Au, but is less sensitive to stoichiometry for MDH:Au
additional information
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construction of a bienzymatic biosensor for malic acid based on malate dehydrogenase and transaminase immobilized onto a glassy carbon powder/carbon nanotubes/NAD+ composite electrode. In order to shift the conversion of malate to oxaloacetate, a reaction to convert oxaloacetate to L-aspartate is coupled to the main reaction, by reacting it with glutamic acid in the presence of glutamate oxaloacetate transaminase, GOT. The main reaction shifts to products, thus promoting the conversion of malate, thereby generating NADH, pH 10.0. Method overview
