Information on EC 1.1.1.40 - malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
1.1.1.40
-
RECOMMENDED NAME
GeneOntology No.
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(S)-malate + NADP+ = pyruvate + CO2 + NADPH
show the reaction diagram
sequential ordered bi-ter kinetic mechanism with NADP+ as the leading substrate followed by L-malate. The products are released in the order of CO2, pyruvate and NADPH
-
(S)-malate + NADP+ = pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
(S)-malate + NADP+ = pyruvate + CO2 + NADPH
show the reaction diagram
the conserved residues Arg237 and Lys225 are involved in catalysis and substrate binding as proton acceptors
-
(S)-malate + NADP+ = pyruvate + CO2 + NADPH
show the reaction diagram
catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
C4 photosynthetic carbon assimilation cycle, NADP-ME type
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
gluconeogenesis I
-
Pyruvate metabolism
-
Carbon fixation in photosynthetic organisms
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating)
The enzyme catalyses the oxidative decarboxylation of (S)-malate in the presence of NADP+ and divalent metal ions, and the decarboxylation of oxaloacetate. cf. EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), and EC 1.1.1.39, malate dehydrogenase (decarboxylating).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C4 NADP-malic enzyme
-
-
C4 photosynthetic NADP-malic enzyme
-
-
C4-NADP-malic enzyme
-
-
C4-NADP-ME
P16243
isoform involved in C4 photosynthesis
ChlME1
Q8SAT4
-
ChlME1
AF288899
-
ChlME1
AF288900
-
ChlME1
AF288904
-
ChlME1
AF288906
-
ChlME1
AF288911
-
ChlME1
Q8SAT3
-
ChlME1
P22178
-
ChlME2
Q8SAT4
-
ChlME2
AF288899
-
ChlME2
AF288900
-
ChlME2
AF288904
-
ChlME2
AF288906
-
ChlME2
AF288911
-
ChlME2
Q8SAT3
-
ChlME2
P22178
-
cytoNADPME
Q6SZS7
-
cytosolic malic enzyme
-
-
cytosolic malic enzyme
-
-
cytosolic NADP+-dependent isoform
-
-
cytosolic NADP+-dependent malic enzyme
-
-
L-malate: NADP oxidoreductase [oxaloacetate decarboxylating]
-
-
L-malate:NADP oxidoreductase
-
-
-
-
L-malate:NADP oxidoreductase (oxaloacetate decarboxylating)
Q006P9, Q006Q0
-
MaeB
-
-
MaeB
P76558
-
MaeB
Escherichia coli MG1655
P76558
-
-
malate dehydrogenase (decarboxylating, NADP)
-
-
-
-
malate dehydrogenase (NADP, decarboxylating)
-
-
-
-
malic enzyme
-
-
-
-
malic enzyme
-
-
malic enzyme
Aspergillus niger NRRL 2270
-
-
-
malic enzyme
-
-
malic enzyme
Hieracium pilosella
-
-
malic enzyme
-
-
malic enzyme
Mnium undulatum
-
-
malic enzyme
-
-
malic enzyme
A6XP71
-
malic enzyme
A6XP72
-
malic enzyme
-
-
malic enzyme
-
-
malic enzyme
Sulfolobus solfataricus MT-4
-
-
-
malic enzyme
Q717I9
-
malic enzyme
Trichomonas vaginalis TV 7-37
Q717I9
-
-
malic enzyme
-
-
malic enzyme
Trypanosoma brucei 427, Trypanosoma brucei stock 427
-
-
-
malic enzyme
-
-
malic enzyme
Trypanosoma cruzi CL Brener
-
-
-
malic enzyme 1
-
-
malic enzyme 3
-
-
malic enzyme-NADP
Q9F3K4
-
malic enzyme-NADP
Streptomyces coelicolor M145
Q9F3K4
-
-
ME-NADP
Q9F3K4
-
ME-NADP
Streptomyces coelicolor M145
Q9F3K4
-
-
NAD(P)+-malic enzyme
-
-
NADP dependent malic enzyme
Q6T5D1, Q9FRT2
-
NADP malic enzyme
-
-
NADP+ dependent malic enzyme
-
-
-
-
NADP+-dependent malic enzyme
-
-
NADP+-dependent malic enzyme
Q27IE1, Q6PMI1, Q6PMI2
-
NADP+-dependent malic enzyme
-
-
NADP+-dependent malic enzyme
-
-
NADP+-dependent malic enzyme 3
-
-
NADP+-ME
-
-
NADP-dependent malate dehydrogenase
Q8H1E2
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
P76558
-
NADP-dependent malic enzyme
Escherichia coli MG1655
P76558
-
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
A9LIN4
-
NADP-dependent malic enzyme
B8PUQ5
-
NADP-dependent malic enzyme
Triticum aestivum Jinmai 47
B8PUQ5
-
-
NADP-dependent malic enzyme
Q8W000
-
NADP-linked decarboxylating malic enzyme
-
-
-
-
NADP-malic enzyme
-
-
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
Q9LYG3, Q9XGZ0
-
NADP-malic enzyme
Bothriochloa biloba
-
-
NADP-malic enzyme
Bothriochloa biloba Kuntze
-
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
Bothriochloa bladhii Kuntze
-
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
Cymbopogon ambiguus Spreng.
-
-
-
NADP-malic enzyme
Cymbopogon bombycinus
-
-
NADP-malic enzyme
Cymbopogon bombycinus Spreng.
-
-
-
NADP-malic enzyme
Dichanthium aristatum, Dichanthium sericeum, Digitaria brownii, Digitaria smutsi
-
-
NADP-malic enzyme
Q8SAT4
-
NADP-malic enzyme
-
-
NADP-malic enzyme
AF288899
-
NADP-malic enzyme
AF288900
-
NADP-malic enzyme
AF288904
-
NADP-malic enzyme
AF288906
-
NADP-malic enzyme
AF288911
-
NADP-malic enzyme
Q8SAT3
-
NADP-malic enzyme
P22178
-
NADP-malic enzyme
-
-
NADP-malic enzyme
Hieracium pilosella, Mnium undulatum
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
Q006P9, Q006Q0
-
NADP-malic enzyme
Q6SZS7
-
NADP-malic enzyme
Q6T5D1
-
NADP-malic enzyme
Q9FRT2
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
Q5G1U0
-
NADP-malic enzyme 2
-
-
NADP-MDH
Q8H1E2
-
NADP-ME
-
-
-
-
NADP-ME
-
-
NADP-ME
Q8SAT4
-
NADP-ME
AF288899
-
NADP-ME
AF288900
-
NADP-ME
AF288904
-
NADP-ME
AF288906
-
NADP-ME
AF288911
-
NADP-ME
Q8SAT3
-
NADP-ME
P22178
-
NADP-ME
Hieracium pilosella
-
-
NADP-ME
Q27IE1, Q6PMI1, Q6PMI2
-
NADP-ME
Mnium undulatum
-
-
NADP-ME
Q006P9, Q006Q0
-
NADP-ME
Q6SZS7
-
NADP-ME
Q9FRT2
-
NADP-ME
-
-
NADP-ME
-
-
NADP-ME
-
-
NADP-ME
B8PUQ5
-
NADP-ME
Triticum aestivum Jinmai 47
B8PUQ5
-
-
NADP-ME
Q5G1U0
-
NADP-ME
Q8W000
-
NADP-ME1
-
-
NADP-ME1
B8PUQ5
isozyme
NADP-ME2
Q9LYG3
isoform
NADP-ME2
Q9FRT2
-
NADP-ME2
A9LIN4
isozyme
NADP-ME3
Q9XGZ0
isoform
NADP-ME3
Q6T5D1
-
NADP-ME3
-
-
NADP-specific malate dehydrogenase
-
-
-
-
NADP-specific malic enzyme
-
-
-
-
NADP-specific ME
-
-
NADP-specific ME
-
-
pyruvic-malic carboxylase
-
-
-
-
TME
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-47-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
constitutive CAM plant, 2 isozymes
-
-
Manually annotated by BRENDA team
4 isozymes NADP-ME1-4
-
-
Manually annotated by BRENDA team
four malic isozymes, NADP-ME1, NADP-ME2, NADP-ME3, and NADP-ME4
-
-
Manually annotated by BRENDA team
isozymes NADP-ME1, NADP-ME2, and NADP-ME3
-
-
Manually annotated by BRENDA team
var. columbia
UniProt
Manually annotated by BRENDA team
strain NRRL 2270
-
-
Manually annotated by BRENDA team
Aspergillus niger NRRL 2270
strain NRRL 2270
-
-
Manually annotated by BRENDA team
Bothriochloa biloba
strain Kuntze
-
-
Manually annotated by BRENDA team
Bothriochloa biloba Kuntze
strain Kuntze
-
-
Manually annotated by BRENDA team
strain Kuntze
-
-
Manually annotated by BRENDA team
Bothriochloa bladhii Kuntze
strain Kuntze
-
-
Manually annotated by BRENDA team
cultivars Vergasa and Biela
-
-
Manually annotated by BRENDA team
Hochst. ex Chiov.
-
-
Manually annotated by BRENDA team
gene maeB encoding isozyme MaeB
-
-
Manually annotated by BRENDA team
Cymbopogon ambiguus
Spreng.
-
-
Manually annotated by BRENDA team
Cymbopogon ambiguus Spreng.
Spreng.
-
-
Manually annotated by BRENDA team
Cymbopogon bombycinus
Spreng.
-
-
Manually annotated by BRENDA team
Cymbopogon bombycinus Spreng.
Spreng.
-
-
Manually annotated by BRENDA team
Digitaria brownii
-
-
-
Manually annotated by BRENDA team
Digitaria smutsi
-
-
-
Manually annotated by BRENDA team
gene maeB
UniProt
Manually annotated by BRENDA team
gene maeB or ypfF, several isozymes
-
-
Manually annotated by BRENDA team
Escherichia coli MG1655
gene maeB
UniProt
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2; isozyme ChlME2, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
SwissProt
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C4 species, 2 isozymes ChlME1 and ChlME2, transgenic plant
AF288899
GenBank
Manually annotated by BRENDA team
isozyme ChlME2, nuclear encoded, 3'-untranslated region; C4 species, 2 isozymes ChlME1 and ChlME2
AF288898
GenBank
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
GenBank
Manually annotated by BRENDA team
isozyme ChlME2, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
AF288900
GenBank
Manually annotated by BRENDA team
isozyme ChlME2-2, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
AF288901
GenBank
Manually annotated by BRENDA team
isozyme ChlME2-3, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
AF288902
GenBank
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
AF288905
GenBank
Manually annotated by BRENDA team
isozyme ChlME2, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
AF288904
GenBank
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
GenBank
Manually annotated by BRENDA team
isozyme ChlME2, nuclear encoded, 3'-untranslated region; C3-C4 species, 2 isozymes ChlME1 and ChlME2
AF288906
GenBank
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2
AF288911
GenBank
Manually annotated by BRENDA team
isozyme ChlME1-2, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2; isozyme ChlME2-2, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2; isozyme ChlME2-3, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2; isozyme ChlME2, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2
GenBank
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2
AF288916
GenBank
Manually annotated by BRENDA team
isozyme ChlME1-2, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2
AF288917
GenBank
Manually annotated by BRENDA team
isozyme ChlME2-2, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2; isozyme ChlME2-3, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2; isozyme ChlME2, nuclear encoded, 3'-untranslated region; C3 species, 2 isozymes ChlME1 and ChlME2
SwissProt
Manually annotated by BRENDA team
isozyme ChlME1, nuclear encoded, 3'-untranslated region; C4 species, 2 isozymes ChlME1 and ChlME2; isozyme ChlME2, nuclear encoded, 3'-untranslated region; C4 species, 2 isozymes ChlME1 and ChlME2
GenBank
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Hieracium pilosella
-
-
-
Manually annotated by BRENDA team
isozyme Hvme1; gene hvme1
UniProt
Manually annotated by BRENDA team
isozyme Hvme2; gene hvme2
UniProt
Manually annotated by BRENDA team
isozyme Hvme3; gene hvme3
UniProt
Manually annotated by BRENDA team
Mnium undulatum
-
-
-
Manually annotated by BRENDA team
a commercially useful oil-producing fungus, strain CBS 696.70, gene malE
UniProt
Manually annotated by BRENDA team
an oleaginous fungus, strain CBS 696.70, at least seven isozymes A-G
-
-
Manually annotated by BRENDA team
a commercially useful oil-producing fungus, strain CBS 108.16, gene malE
UniProt
Manually annotated by BRENDA team
wild-type plants and transgenic plants, expressing potyviral helper component protease HC-pro or Potato virus Y strain NTN
-
-
Manually annotated by BRENDA team
gene nadp-me1; gene nadp-me1
UniProt
Manually annotated by BRENDA team
gene nadp-me2; gene nadp-me2
UniProt
Manually annotated by BRENDA team
isozyme NADP-ME2; cv. Nipponbare, isozyme NADP-ME2
SwissProt
Manually annotated by BRENDA team
var. indica, cv. Nipponbare
UniProt
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
five NADP-ME genes, PtNADP-ME1, PtNADP-ME2, PtNADP-ME3, PtNADP-ME4, and PtNADPME5
-
-
Manually annotated by BRENDA team
cv. Baker 296
-
-
Manually annotated by BRENDA team
salmon
-
-
-
Manually annotated by BRENDA team
seagull
-
-
-
Manually annotated by BRENDA team
cv. pop. sorghum
-
-
Manually annotated by BRENDA team
gene Sco5261
UniProt
Manually annotated by BRENDA team
Streptomyces coelicolor M145
gene Sco5261
UniProt
Manually annotated by BRENDA team
enzyme additionally catalyzes decarboxylation of oxalacetate
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus MT-4
-
-
-
Manually annotated by BRENDA team
strain TV 7-37
SwissProt
Manually annotated by BRENDA team
Trichomonas vaginalis TV 7-37
strain TV 7-37
SwissProt
Manually annotated by BRENDA team
hexaploid wheat
UniProt
Manually annotated by BRENDA team
Triticum aestivum Jinmai 47
hexaploid wheat
UniProt
Manually annotated by BRENDA team
; grown in male Wistar rats
-
-
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
-
-
Manually annotated by BRENDA team
Trypanosoma brucei stock 427
grown in male Wistar rats
-
-
Manually annotated by BRENDA team
Trypanosoma cruzi CL Brener
-
-
-
Manually annotated by BRENDA team
C4 NADP-ME and non-C4 NADP-ME isozymes, i.e. L and R isozymes
-
-
Manually annotated by BRENDA team
cv. VMH 404
-
-
Manually annotated by BRENDA team
inbred line AX882 (Nidera)
UniProt
Manually annotated by BRENDA team
isozyme ZmChlMe2; C4 plant, 2 isozymes, a C3-like isozyme, ZmChlMe2, and a C4-like isozyme, ZmChlMe1, most abundant form is the C4-like chloroplastic leaf isozyme
SwissProt
Manually annotated by BRENDA team
isozymes ZmC4-NADP-ME and ZmnonC4-NADP-ME
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the five PtNADP-ME isoforms cluster in a phylogenetic tree constructed with the whole set of plant NADP-ME sequences, classification into four groups. PtNADP-ME2 and PtNADPME3 cluster with the cytosolic dicot NADP-ME group (group II), while PtNADP-ME4 and PtNADP-ME5 are included in the plastidic dicot NADP-ME group (group III). The group IV comprises both monocot and dicot enzymes, including PtNADP-ME1. Neither of the PtNADP-ME isoforms is included in the monocot NADPMEs (group I)
malfunction
Q9F3K4
the double Sco2951 Sco5261 mutant, deficient in ME-NAD, EC 1.1.1.39, and ME-NADP activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglcerides during exponential growth
malfunction
-
loss of cytosolic NADP-malic enzyme 2 in Arabidopsis thaliana is associated with enhanced susceptibility to Colletotrichum higginsianum, transient apoplastic reactive oxygen species production after elicitation and callose papilla formation after infection are dampened in mutant nadp-me2
malfunction
-
antisense reduction of NADP-ME alters C3-C4 cycle coordination. Increase in Rubisco and phosphoenolpyruvate carboxylase activity and leaf nitrogen in low-NADP-ME antisense plants
malfunction
Streptomyces coelicolor M145
-
the double Sco2951 Sco5261 mutant, deficient in ME-NAD, EC 1.1.1.39, and ME-NADP activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglcerides during exponential growth
-
metabolism
-
the citrate-malate-pyruvate cycle serves to regenerate NAD+ and maintain glycolytic flux. Pyruvate cycles all lead to the exchange of reducing equivalents from mitochondrial NADH to cytosolic NADPH. Malic enzyme is integral to the coupling of metabolism with insulin secretion
metabolism
A6XP72
the enzyme is involved in the fatty acid biosynthesis
physiological function
-
some pyruvate cycling pathways require malate export from mitochondria and NADP+-dependent decarboxylation of malate to pyruvate by cytosolic malic enzyme ME1. Role of ME1 in glucose-stimulated insulin secretion and in methyl succinate-stimulated insulin secretion occuring occur via succinate entry into the mitochondria in exchange for malate and subsequent malate conversion to pyruvate, overview
physiological function
-
in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power; possibly, in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
physiological function
-
malate that is exported from the mitochondria to the cytosol is regenerated to pyruvate by cytosolic malic enzyme for cycling back to the mitochondria. Cytosolic malic enzyme, together with ATP citrate lyase and malate dehydrogenase, is also central to recycling of citrate back to pyruvate. Cytosolic malic enzyme in the beta-cell supports the concept that the mechanisms linking metabolism with insulin secretion may include a beta-cell pyruvate-malate cycle. siRNA knockdown and isotopic labeling strategies to evaluate the role of cytosolic and mitochondrial isozymes of malic enzyme in facilitating malate-pyruvate cycling in the context of fuel-stimulated insulin secretion, overview
physiological function
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
NADP-ME in the C3 plants contributes to a huge diversity of metabolic pathways in green and non-green tissues of these plants. Additionally, NADP-ME increases its activity in the plant response to stresses
physiological function
Q9F3K4
the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
physiological function
-
ADP-ME2 is an important player in plant basal defence, where it is involved in the generation of reactive oxygen species, NADP-ME2 is dispensable for later defence responses, overview
physiological function
-
one isozyme exclusively expressed in the bundle sheath cells and involved in C4 photosynthesis, i.e. ZmC4-NADP-ME, and the other, ZmnonC4-NADP-ME, with housekeeping roles
physiological function
-
NADP-malic enzyme is the primary enzyme decarboxylating malate in bundle sheath cells to supply CO2 to Rubisco
physiological function
Streptomyces coelicolor M145
-
the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
-
physiological function
Trypanosoma brucei 427, Trypanosoma brucei stock 427, Trypanosoma cruzi CL Brener
-
in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power; possibly, in those environments where glucose is very low or absent, the pathogen depends on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power
-
metabolism
-
isoform C4-NADP-ME involved in C4 photosynthesis is modulated by redox status, and its oxidation produces a conformational change limiting the catalytic process, although inducing higher affinity binding of the substrates. Residues Cys192, Cys246, Cys270 and Cys410 are directly or indirectly implicated in C4-NADP-ME redox modulation
additional information
-
analysis of transcriptional co-response patterns related NADP-ME2 to plant defence responses, overview
additional information
-
reversal of ZmC4-NADP-ME oxidation by chemical reductants, e.g. iodosobenzoate and CuCl2, doe to the presence of thiol groups able to form disulfide bonds. Residues Cys192, Cys246, Cys270, and Cys410 may be directly or indirectly implicated in ZmC4-NADP-ME redox modulation. Redox regulation plays a key role in many plastid functions. Isozyme specific redox regulation of ZmC4-NADP-ME activity, the modulation is not observed in the case of isozyme ZmnonC4-NADP-ME. The replacement of Cys246 with serine in ZmnonC4-NADP-ME may be responsible for the absence of redox modulation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
show the reaction diagram
P16243, -
-
-
-
?
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
show the reaction diagram
P16243, -
the unique and specialized C4-type enzyme has evolved fro the C3-type enzyme
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
-
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
-
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
P16243, -
-
-
-
-
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
at 39% of the activity with NADP+
-
ir
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
lower activity than with NADP+
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
NADP+ is preferred over NAD+
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
low activity with NAD+ as cofactor
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
ir
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
salmon
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q717I9, -
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q8SAT4
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-, P22178
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
AF288916, AF288917, Q8SAT3
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
AF288906, P93139
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
AF288904, AF288905
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
AF288900, AF288901, AF288902, Q93ZK8
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
AF288911, P36444
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
AF288898, AF288899
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q9FRT2
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
A6XP72
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
A6XP71
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q27IE1, Q6PMI1, Q6PMI2
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-, Q006P9, Q006Q0
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q8H1E2
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-, Q6SZS7
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q5G1U0, -
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
A9LIN4, B8PUQ5
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
B8PUQ5
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q9LYG3, Q9XGZ0
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q9F3K4
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
P76558
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
reaction velocity is 29times higher in the direction of decarboxylation than in the direction of the carboxylation
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Pigeon
-
Arg residue is involved in the binding of C-1 carboxyl group of malate
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the reverse reaction is catalyzed at 84% of the activity
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Pigeon
-
the singly-ionized species is the substrate, doubly-ionized malate is unreactive
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
carboxyl is replaced by hydrogen without net change of configuration
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
enzyme plays a specialized role in bundle sheath chloroplasts, where it provides CO2 for fixation by EC 4.1.1.39
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
major role of the enzyme is believed to be the supplier of NADPH for the reductive steps of lipogenesis
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
enzyme is involved in fatty acid biosynthesis in oil seed leucoplasts, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
no day/night regulation of the isozyme 2 in leaves via expression level but by metabolite inhibition, overview
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q717I9, -
responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
decarboxylation is favoured
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
NADP+ is preferred over NAD+
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
weak reaction
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
MEs are essential enzymes for growth on TCA cycle intermediates or on substrates that enter central metabolism via acetyl-coenzyme A, the reaction plays a role in the C4 metabolism, regulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q27IE1, Q6PMI1, Q6PMI2
NADP-ME provides a high CO2 concentration for Rubisco fixation in the C4 leaf chloroplasts, regulation of isozyme Hvme1, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q27IE1, Q6PMI1, Q6PMI2
regulation of isozyme Hvme3, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the C4 isozyme takes part in the C4 and CAM photosynthetic metabolisms, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the cycling of pyruvate by isozyme ME1 generates cytosolic NADPH
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the enzyme is involved in glucose-induced insulin secretion, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
A6XP72
the enzyme is rate-limiting step for fatty acid biosynthesis in oleaginous fungi in which the extent of lipid accumulation is below the maximum possible, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
A6XP71
the enzyme is rate-limiting step for fatty acid biosynthesis in oleaginous fungi in which the extent of lipid accumulation is below the maximum possible, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the only enzyme that can provide NADPH for fatty acid biosynthesis in oleaginous microorganisms, isozyme E, which arises from isoform D, is associated with lipid accumulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the reaction plays a role in the C4 metabolism, pathway regulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
during the catalytic process of malic enzyme, binding metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
NADP-ME2 is the isozyme with the highest catalytic efficiency for the reverse reaction, while NADP-ME4 presents higher kcat for the reverse reaction than for the forward reaction
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
via oxaloacetate, roles of Tyr91 and Lys162 in general acid-base catalysis in the pigeon NADP+-dependent malic enzyme, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Sulfolobus solfataricus MT-4
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trypanosoma cruzi CL Brener
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Triticum aestivum Jinmai 47
B8PUQ5
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trichomonas vaginalis TV 7-37
Q717I9
-, responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Escherichia coli MG1655
P76558
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trypanosoma brucei 427, Trypanosoma brucei stock 427
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Streptomyces coelicolor M145
Q9F3K4
-
-
-
r
(S)-malate + NADP+
?
show the reaction diagram
Q6T5D1, Q9FRT2
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Mnium undulatum
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Hieracium pilosella
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
oxaloacetate represents the intermediate resulting from dehydrogenation of malate during the first step of the catalytic cycle of MEs
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Trypanosoma cruzi CL Brener
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Trypanosoma cruzi CL Brener
-
oxaloacetate represents the intermediate resulting from dehydrogenation of malate during the first step of the catalytic cycle of MEs
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Trypanosoma brucei 427
-
-, oxaloacetate represents the intermediate resulting from dehydrogenation of malate during the first step of the catalytic cycle of MEs
-
-
r
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
Pigeon
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
no activity
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
at 1.3% of the rate of NADP+-linked oxidative decarboxylation
-
-
?
oxaloacetate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
?
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
Pigeon
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
-
?
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
6% of the activity of the NADP+-linked oxidative decarboxylation of malate
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
reaction velocity is 29times higher in the direction of decarboxylation than in the direction of the carboxylation
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
show the reaction diagram
-
at 84% of the activity of the NADP+-linked oxidative decarboxylation of malate
-
-
r
pyruvate + NADPH
?
show the reaction diagram
-
at 5.4% of the activity of NADP-dependent oxidative decarboxylation of malate
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Trypanosoma brucei stock 427
-
-, oxaloacetate represents the intermediate resulting from dehydrogenation of malate during the first step of the catalytic cycle of MEs
-
-
r
additional information
?
-
-
cell-specific regulation and transcription of the malic enzyme gene, cell-specific differences in T3 responsiveness of the malic enzyme gene are mediated in large part by by nonreceptor proteins that augment the transcriptional activity of the nuclear T3 receptor
-
-
-
additional information
?
-
-
the specific activity falls rapidly as the fruit ripens
-
-
-
additional information
?
-
-
one may speculate that in vivo the reaction catalyzed by cytosolic enzyme supplies dicarboxylic acids, anaplerotic function, for the formation of neurotransmitters while the mitochondrial enzyme regulates the flux rate via Krebs cycle by disposition of the tricarboxylic acid cycle intermediates, cataplerotic function
-
-
-
additional information
?
-
Q717I9, -
enzyme belongs to the prokaryotic small subunit-type family of malic enzymes being achieved by a horizontal gene transfer from an eubacterium to the ancestor of Trichomonas vaginalis, enzyme occurs besides the eukaryotic large subunit-type enzyme in the organism
-
-
-
additional information
?
-
-
enzyme is regulated by light and dithiols, such as dithioerythritol
-
-
-
additional information
?
-
Q8SAT4
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
-, P22178
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288916, AF288917, Q8SAT3
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288906, P93139
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288904, AF288905
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288900, AF288901, AF288902, Q93ZK8
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288911, P36444
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288898, AF288899
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
-
additional information
?
-
-
the enzyme plays a role in the mechanism of stomatal closure as well as in a potential mechanism for genetic altering plant water use
-
-
-
additional information
?
-
Q717I9, -
enzyme does not decarboxylate oxaloacetate
-
-
-
additional information
?
-
-
enzyme additionally catalyzes decarboxylation of oxalacetate
-
-
-
additional information
?
-
-
diurnal effects of an enhanced chloroplastic NADP-ME activity on metabolite levels, overview
-
-
-
additional information
?
-
-
TME is not capable of N2 fixation probably due to a constantly high ratio of NADPH + H+ to NADP+ in nitrogen-fixing bacteroids, overview
-
-
-
additional information
?
-
-
the isozyme pattern is similar in Nicotiana benthamiana wild-type plants and transgenic plants, expressing potyviral helper component protease HC-pro or Potato virus Y strain NTN, overview
-
-
-
additional information
?
-
Polytrichum commune, Polytrichum piliferum, Mnium undulatum, Hieracium pilosella
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
-
additional information
?
-
Aspergillus niger NRRL 2270
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
-
additional information
?
-
Trichomonas vaginalis TV 7-37
Q717I9
enzyme belongs to the prokaryotic small subunit-type family of malic enzymes being achieved by a horizontal gene transfer from an eubacterium to the ancestor of Trichomonas vaginalis, enzyme occurs besides the eukaryotic large subunit-type enzyme in the organism, enzyme does not decarboxylate oxaloacetate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
show the reaction diagram
P16243, -
the unique and specialized C4-type enzyme has evolved fro the C3-type enzyme
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q9FRT2
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q27IE1, Q6PMI1, Q6PMI2
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-, Q006P9, Q006Q0
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q8H1E2
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-, Q6SZS7
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
B8PUQ5
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q9F3K4
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
P76558
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
enzyme plays a specialized role in bundle sheath chloroplasts, where it provides CO2 for fixation by EC 4.1.1.39
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
major role of the enzyme is believed to be the supplier of NADPH for the reductive steps of lipogenesis
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
enzyme is involved in fatty acid biosynthesis in oil seed leucoplasts, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
no day/night regulation of the isozyme 2 in leaves via expression level but by metabolite inhibition, overview
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q717I9, -
responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
MEs are essential enzymes for growth on TCA cycle intermediates or on substrates that enter central metabolism via acetyl-coenzyme A, the reaction plays a role in the C4 metabolism, regulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q27IE1, Q6PMI1, Q6PMI2
NADP-ME provides a high CO2 concentration for Rubisco fixation in the C4 leaf chloroplasts, regulation of isozyme Hvme1, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Q27IE1, Q6PMI1, Q6PMI2
regulation of isozyme Hvme3, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the C4 isozyme takes part in the C4 and CAM photosynthetic metabolisms, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the cycling of pyruvate by isozyme ME1 generates cytosolic NADPH
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the enzyme is involved in glucose-induced insulin secretion, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
A6XP72
the enzyme is rate-limiting step for fatty acid biosynthesis in oleaginous fungi in which the extent of lipid accumulation is below the maximum possible, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
A6XP71
the enzyme is rate-limiting step for fatty acid biosynthesis in oleaginous fungi in which the extent of lipid accumulation is below the maximum possible, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the only enzyme that can provide NADPH for fatty acid biosynthesis in oleaginous microorganisms, isozyme E, which arises from isoform D, is associated with lipid accumulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
-
the reaction plays a role in the C4 metabolism, pathway regulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Mnium undulatum
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Hieracium pilosella
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trypanosoma cruzi CL Brener
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Trypanosoma cruzi CL Brener
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Triticum aestivum Jinmai 47
B8PUQ5
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trichomonas vaginalis TV 7-37
Q717I9
responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Escherichia coli MG1655
P76558
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trypanosoma brucei 427
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Trypanosoma brucei 427
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trypanosoma brucei stock 427
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
show the reaction diagram
Trypanosoma brucei stock 427
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Streptomyces coelicolor M145
Q9F3K4
-
-
-
r
additional information
?
-
-
cell-specific regulation and transcription of the malic enzyme gene, cell-specific differences in T3 responsiveness of the malic enzyme gene are mediated in large part by by nonreceptor proteins that augment the transcriptional activity of the nuclear T3 receptor
-
-
-
additional information
?
-
-
the specific activity falls rapidly as the fruit ripens
-
-
-
additional information
?
-
-
one may speculate that in vivo the reaction catalyzed by cytosolic enzyme supplies dicarboxylic acids, anaplerotic function, for the formation of neurotransmitters while the mitochondrial enzyme regulates the flux rate via Krebs cycle by disposition of the tricarboxylic acid cycle intermediates, cataplerotic function
-
-
-
additional information
?
-
Q717I9, -
enzyme belongs to the prokaryotic small subunit-type family of malic enzymes being achieved by a horizontal gene transfer from an eubacterium to the ancestor of Trichomonas vaginalis, enzyme occurs besides the eukaryotic large subunit-type enzyme in the organism
-
-
-
additional information
?
-
-
enzyme is regulated by light and dithiols, such as dithioerythritol
-
-
-
additional information
?
-
Q8SAT4
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
-, P22178
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288916, AF288917, Q8SAT3
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288906, P93139
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288904, AF288905
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288900, AF288901, AF288902, Q93ZK8
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288911, P36444
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
AF288898, AF288899
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
-
additional information
?
-
-
the enzyme plays a role in the mechanism of stomatal closure as well as in a potential mechanism for genetic altering plant water use
-
-
-
additional information
?
-
-
diurnal effects of an enhanced chloroplastic NADP-ME activity on metabolite levels, overview
-
-
-
additional information
?
-
-
TME is not capable of N2 fixation probably due to a constantly high ratio of NADPH + H+ to NADP+ in nitrogen-fixing bacteroids, overview
-
-
-
additional information
?
-
Polytrichum commune, Polytrichum piliferum, Mnium undulatum, Hieracium pilosella
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
-
additional information
?
-
Aspergillus niger NRRL 2270
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
-
additional information
?
-
Trichomonas vaginalis TV 7-37
Q717I9
enzyme belongs to the prokaryotic small subunit-type family of malic enzymes being achieved by a horizontal gene transfer from an eubacterium to the ancestor of Trichomonas vaginalis, enzyme occurs besides the eukaryotic large subunit-type enzyme in the organism
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
very low activity with
NAD+
-
the recombinant wild-type enzyme shows a low intrinsic activity with NAD+, best at pH 7.0, mutant A392G shows increased activity with NAD+ compared to the wild-type enzyme
NAD+
-
poor activity with NAD+ compared to NADP+
NADP+
Pigeon
-
cofactor; stimulation of decarboxylation of oxaloacetate
NADP+
-
cofactor
NADP+
-
cofactor
NADP+
-
cofactor
NADP+
-
cofactor
NADP+
Pigeon
-
cofactor
NADP+
-
cofactor
NADP+
-
absolutely specific for, no activity with NAD+
NADP+
-
cofactor specificity is determined by Lys435/Lys436 interacting with the 2'-phosphate group of the ribose ring
NADP+
Q717I9, -
absolute specific for
NADP+
-
binding site structure, Arg237 is important for cofactor binding and specificity
NADP+
Q8SAT4
specific for
NADP+
AF288898, AF288899
specific for
NADP+
AF288900, AF288901, AF288902, Q93ZK8
specific for
NADP+
AF288904, AF288905
specific for
NADP+
AF288906, P93139
specific for
NADP+
AF288911, P36444
specific for
NADP+
AF288916, AF288917, Q8SAT3
specific for
NADP+
P22178
specific for
NADP+
-
specific for, no activity with NAD+
NADP+
-
dependent on, 1 cofactor molecule per subunit, binding mode, structure around the binding site at the 2'-phosphate group helps to define the cofactor specificity of the enzyme, Lys362 and Ser346 are involved, molecular mechanism
NADP+
-
important role of Asp-351, Asp-350 and Glu-327 in the binding of Mg2+ and NADP+
NADP+
Q6T5D1, Q9FRT2
;
NADP+
-
specific for
NADP+
-
no activity with NAD+
NADP+
Q27IE1, Q6PMI1, Q6PMI2
-
NADP+
-, Q006P9, Q006Q0
;
NADP+
A9LIN4, B8PUQ5
;
NADP+
-
preferred cofactor
NADP+
Q9LYG3, Q9XGZ0
;
NADP+
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
NADP+
-
the enzyme is strictly NADP+-dependent
NADP+
Q9F3K4
dependent on
NADP+
A6XP72
dependent on
NADP+
-
dependent on
NADP+
P76558
dependent on
NADP+
-
dependent on
NADP+
-
Lys362 is the key residue contributing to binding the 2'-phosphate of NADP+
NADPH
Pigeon
-
cofactor
NADPH
-
cofactor
NADPH
-
cofactor
NADPH
-
cofactor
NADPH
-
specific for
NADPH
Q27IE1, Q6PMI1, Q6PMI2
-
NADPH
-, Q006P9, Q006Q0
;
NADPH
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
NADPH
-
dependent on
additional information
Q717I9, -
no activity with NAD+
-
additional information
-
nucleotide-binding site of c-NADP-ME, sequence comparisons, overview. A series of E314A-containing c-NADP-ME quadruple mutants are changed to NAD+-utilizing enzymes by abrogating NADP+ binding and increasing NAD+ binding
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
Pigeon
-
less effective activation than Mn2+
Cu2+
Pigeon
-
weak activation
K+
-
activates; Km: 0.7 mM
KCl
-
activates at 2 mM
Mg2+
-
requires low concentration of Mn2+ or Mg2+ for activity, Km: 0.24 mM
Mg2+
-
divalent metal ion required, Mn2+ is more effective than Mg2+, Km: 0.34 mM
Mg2+
Pigeon
-
promotes activity
Mg2+
-
activity of cytosolic enzyme and mitochondrial enzyme is strictly dependent on; optimal concentration: 6 mM for the decarboxylation of the mitochondrial enzyme, 20 mM for the cytosolic enzyme
Mg2+
-
divalent cation required, Mn2+ is more effective than Mg2+
Mg2+
-
Km: 0.00146 mM
Mg2+
-
Km: 0.005-0.16 mM
Mg2+
-
Km: 0.011-3.5 mM
Mg2+
-
Km: 0.006-0.2 mM
Mg2+
-
Km: 0.05-0.23 mM
Mg2+
-
Mg2+ and Mn2+ stabilize two structurally distinct forms of the enzyme which vary in catalytic and regulatory properties
Mg2+
-
absolute requirement for a divalent cation, Mn2+ or Mg2+; Km: 0.315 mM
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
enzyme requires either Mg2+ or Mn2+ for activity, no activity without divalent cation
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
Q717I9, -
strictly dependent on presence of Mg2+ or Mn2+
Mg2+
-
activates, KM: 0.16 mM for wild-type enzyme
Mg2+
-
required. Important role of Asp-351, Asp-350 and Glu-327 in the binding of Mg2+ and NADP+
Mg2+
-
may partly replace for Mn2+
Mg2+
Q6SZS7
required
Mg2+
-
activates
Mg2+
-
required
Mg2+
-
activates at up to 4 mM, inhibition above, probably due to blockage of substrate binding
Mg2+
-
required
Mg2+
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme1 requires Mg2+ or Mn2+ for activity; isozyme Hvme3 requires Mg2+ or Mn2+ for activity
Mg2+
-
required for activity
Mg2+
-
activates, kcat is 1280/s and Km 0.27 mM for ME1, and kcat is 208/s and Km 0.58 mM for ME2; can partially substitute for Mn2+, activates
Mg2+
-
can partially substitute for Mn2+, activates; highly activating, kcat is 461/s and Km 0.04 mM for ME1, and kcat is 864/s and Km 0.57 mM for ME2
Mg2+
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
activates
Mg2+
Q9F3K4
activates
Mg2+
P76558
activates, can partially substitute for Mn2+ to about 92% of the maximal activity
Mg2+
-
required
Mn2+
-
Km: 0.01 mM; requires low concentration of Mn2+ or Mg2+ for activity
Mn2+
-
divalent metal ion required, Mn2+ is more effective than Mg2+; Km: 0.004 mM
Mn2+
Pigeon
-
0.004 mM, 50% of the maximal activity of the malic activity. 0.2 mM, 50% of the maximal activity of oxaloacetic decarboxylase
Mn2+
-
activity of cytosolic enzyme and mitochondrial enzyme is strictly dependent on; optimal concentration is 15 mM for the cytosolic enzyme and 10 mM for the mitochondrial enzyme
Mn2+
-
required, Km: 0.008 mM
Mn2+
-
required for decarboxylation of malate and decarboxylation of pyruvate, KM: 0.0018 mM
Mn2+
-
divalent cation required, Mn2+ is more effective than Mg2+
Mn2+
-
at pH 7.1, Km: 0.0143; Mg2+ and Mn2+ stabilize two structurally distinct forms of the enzyme which vary in catalytic and regulatory properties
Mn2+
-
absolute requirement for a divalent cation, Mn2+ or Mg2+; Km: 0.210 mM
Mn2+
-
dependent on presence of divalent cations. Maximal activity in presence of 5 mM Mn2+
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
enzyme requires either Mg2+ or Mn2+ for activity, no activity without divalent cation
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
Q717I9, -
strictly dependent on presence of Mg2+ or Mn2+
Mn2+
-
-
Mn2+
-
activates, KM: 0.00378 mM for wild-type enzyme
Mn2+
-
most effective divalent cation
Mn2+
-
required for forward and reverse reaction, residues Tyr91 and Lys162 are not involved in metal ion binding
Mn2+
-
required for activity and protective against inactivation and degeneration by urea or digestion by trypsin, Trp252 is involved, overview, during the catalytic process of malic enzyme, binding of metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form
Mn2+
-
activates
Mn2+
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme1 requires Mg2+ or Mn2+ for activity; isozyme Hvme3 requires Mg2+ or Mn2+ for activity
Mn2+
-
activates
Mn2+
-
activates, required; highly activating, kcat is 905/s and Km 0.0024 mM for ME1, and kcat is 246/s and Km 0.0066 mM for ME2
Mn2+
-
activates, kcat is 518/s and Km 0.0043 mM for ME1, and kcat is 687/s and Km 0.0091 mM for ME2; activates, required
Mn2+
-
activates
Mn2+
-
activates
NH4+
-
activates
NH4Cl
-
activates
Ni2+
Pigeon
-
weak activation
Zn2+
Pigeon
-
weak activation
Mn2+
P76558
dependent on, best at 20 mM
additional information
-
absolute requirement for a divalent cation. Ca2+ is barely effective
additional information
-
Mg2+ does not influence the thermal stability of the enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
at high concentrations
(S)-malate
-
substrate inhibition
(S)-malate
Q27IE1, Q6PMI1, Q6PMI2
an increase to malate concentration of 10 mM decreases the specific activity of rHVME1 by almost 50%
2'-AMP
-
competitive
2,3-Butanedione
Pigeon
-
pseudo-first-order loss of oxidative decarboxylase activity
2-Ketoglutarate
-
34% inhibition at 2 mM
2-mercaptoethanol
-
inactivation in absence of Mg2+
2-oxoglutarate
-
strong
2-oxoglutarate
-
competitive
2-oxoglutarate
-
inhibition of isozyme NADP-ME2
5'-AMP
-
competitive
acetyl-CoA
-
inhibition is much more pronounced in the mitochondrial enzyme than in the cytosolic enzyme and occurs at physiological acetyl-CoA concentrations
acetyl-CoA
-, Q006P9, Q006Q0
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
acetyl-CoA
-
inhibits isozyme NADP-ME1
acetyl-CoA
Q9LYG3, Q9XGZ0
;
adenosine 2'-phosphate
Pigeon
-
-
ADP
Pigeon
-
-
ADP
-
83% inhibition at 2 mM
AMP
-
41% inhibition at 5 mM
AMP
-
75% inhibition at 2 mM
arsenite
Pigeon
-
weak
aspartate
Q9LYG3, Q9XGZ0
-
ATP
-
non-competitive versus L-malate
ATP
Q717I9, -
27% inhibition at 0.2 mM
ATP
-
83% inhibition at 2 mM
ATP
-, Q006P9, Q006Q0
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
ATP
Q9LYG3, Q9XGZ0
;
ATP
-
weak inhibitor
ATP
-
10% inhibition of the wild-type enzyme at 3.0 mM in presence of NAD+, no inhibition in presence of NADP+, inhibition of mutant enzymes by ATP inpresence of NAD+ or NADP+
cAMP
-
10% inhibition at 5 mM
citrate
-
competitive, 61% inhibition at 5 mM
citrate
-
competitive
Citric acid
-
inhibits all PtNADP-ME activities significantly
CO2
-
product inhibition, uncompetitive with respect to L-malate and NADP+, 39% inhibition at 25 mM
CoA
-, Q006P9, Q006Q0
30% inhibition of isozyme NADP-ME1 at 2 mM
CoA
-
activities of PtNADP-ME1, PtNADP-ME2 and PtNADPME4 proteins are inhibited
Cu2+
Pigeon
-
3 mM, weak
Cu2+
-
complete inhibition at 0.1 mM, competitive to Mg2+ and Mn2+, enzyme inhibition leads to reduced lipid biosynthesis and accumulation of citric acid, quantitative overview
Cu2+
P76558
strong inhibition
Cu2+-ascorbate
-
rapid inactivation by generation of reactive oxygen species at pH 5.0, Fe2+ can substitute for Cu2+, Cu2+ or ascorbate alone are not effective, azide, 1,4-diazabicyclo-(2.2.2.)octane, histidine and imidazole protect against inhibition, the substrates L-malate and NADP+ and EDTA protect almost completely, loss of activity is accompanied with cleavage of the protein into 4 fragments of 14-55 kDa
CuCl2
-
about 40% loss of activity within 60 min
D-fructose
-
PtNADP-ME1
D-fructose-1,6-bisphosphate
-
13% inhibition at 5 mM
D-fructose-1,6-bisphosphate
Q5G1U0
when assayed at malate concentrations of 0.2 mM, D-fructose-1,6-bisphosphate inhibits the enzyme by a 49% over the control activity
D-glucose 6-phosphate
-, Q006P9, Q006Q0
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
D-Glucose-6-phosphate
Q9LYG3, Q9XGZ0
;
Diamide
-
2 mM, time-dependent decrease in activity reaching about 40% of initial activity after 60 min. In presence of dithiothreitol, a complete recovery is observed after 90 min. Enzyme oxidation decreases the catalytic activity. No severe loss of protein secondary structure takes place after oxidation; about 40% loss of activity within 60 min
diphenyliodonium chloride
Pigeon
-
weak
Fe2+-ascorbate
-
rapid inactivation
fumarate
-
at high concentration
fumarate
-, Q006P9, Q006Q0
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
fumarate
-
inhibits isozymes NADP-ME1 , NADP-ME3 and NADP-ME4
fumarate
Q9LYG3, Q9XGZ0
-
GDP
-
13% inhibition at 5 mM
glutathione
-
strongly inactivates in absence of Mg2+
H2O2
-
83% inhibition at 0.25 mM, 91.1% inhibition at 0.5 mM
Hg2+
Pigeon
-
0.0005 mM, almost complete inhibition
iodoacetate
Pigeon
-
weak
Iodosobenzoate
-
1 mM, time-dependent decrease in activity reaching about 40% of initial activity after 60 min; about 40% loss of activity within 60 min
L-aspartate
-
competitive, 94% inhibition at 10 mM
L-Malate
-
pH 7.0, high concentration
malate
Pigeon
-
substrate inhibition
malate
-
no inhibition at pH 7.0
malate
-
inhibition at pH 7.0
malate
-
inhibition at pH 7.0
malate
-
excess of malate inhibits the oxidative decarboxylation catalyzed by the cytosolic enzyme at pH 7.0, and below, decarboxylation catalyzed by mitochondrial enzyme is unaffected by the substrate
malate
-
inhibition at high concentrations at pH 7.0, but not at pH 8.0
malate
-, Q006P9, Q006Q0
inhibition of isozyme NADP-ME1 at pH 7.0
Maleate
-
the cis isomer of fumarate, inhibition of isozyme NADP-ME2
malonate
-
inhibition of isozyme NADP-ME2
malonyl-CoA
-
inhibition of mitochondrial enzyme and cytosolic enzyme to a much lower extent than with acetyl-CoA
Mg2+
-
mitochondrial enzyme, decarboxylation reaction, above 6 mM
NaCl
-
at high concentrations
NAD+
Pigeon
-
weak
NADP+
-
substrate inhibition
NADPH
-
product inhibition, competitive with respect to L-malate and NADP+
o-Iodosobenzoate
Pigeon
-
strong
oxalate
-
51% inhibition at 1 mM
oxalate
-
inhibition is decreased by light exposure
oxaloacetate
-
strong
oxaloacetate
-
competitive, 70% inhibition at 2 mM
oxaloacetate
Q9LYG3, Q9XGZ0
;
oxaloacetic acid
-, Q006P9, Q006Q0
60% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
oxaloacetic acid
-
inhibits all PtNADP-ME activities significantly
p-mercuribenzoate
Pigeon
-
strong
Phenylglyoxal
Pigeon
-
pseudo-first-order loss of oxidative decarboxylase activity
phosphate
-
35% inhibition at 5 mM
phosphoenolpyruvate
-
39% inhibition at 5 mM
phosphoenolpyruvate
-
competitive, 82% inhibition at 2 mM
pyruvate
-
competitive
pyruvate
-
non-competitive inhibition
pyruvate
-
product inhibition, competitive with respect to L-malate, 16% inhibition at 5 mM
pyruvate
-
inhibition is decreased by light exposure
pyruvate
-
22% inhibition at 2 mM
pyruvate
-, Q006P9, Q006Q0
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
sesamol
A6XP72
a specific inhibitor of the enzyme
-
SO32-
-
in decarboxylation of malate: partially competitive with respect to malate, in carboxylation of pyruvate: fully competitive for CO2 or HCO3-
succinate
-
slight inhibition at high concentrations
succinate
-
competitive, 28% inhibition at 5 mM
succinate
-, Q006P9, Q006Q0
inhibition of isozyme NADP-ME2
succinate
Q9LYG3, Q9XGZ0
-
sulfite
-
-
Tartronate
-
noncompetitive inhibitor with respect to L-malate
Trypsin
-
digests the mutant enzymes, while the wild-type enzyme is protected in the presence of Mn2+, because a specific cutting site in the Lys352-Gly-Arg354 region is able to generate a unique polypeptide with Mr of 37 kDa, and this polypeptide is resistant to further digestion
-
Urea
-
inactivation at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, overview
Zn2+
P76558
strong inhibition
Mg2+
-
activates at up to 4 mM, inhibition above, probably due to blockage of substrate binding, Km is 0.19 mM
additional information
-
feedback inhibition is reduced by illumination
-
additional information
-
glutamine is a poor inhibitor
-
additional information
Q27IE1, Q6PMI1, Q6PMI2
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
-, Q006P9, Q006Q0
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
A9LIN4, B8PUQ5
the expression levels of isozyme NADP-ME1 in leaves clearly decreases to the lowest point at 6 h following application of abscisic acid (0.2 mM), when treated with 4C, NaCl, and PEG, NADP-ME1 is down-regulated and low temperature treatment is more distinct; with respect to isozyme NADP-ME2, the expression levels are reduced by abscisic acid and salicylic acid treatments, in the salicylic acid treatment, the expression amounts of NADP-ME2 decrease to least at 3 h treatment, then begin to ascend till 6 h and again start to descend till 24 h treatment
-
additional information
Q5G1U0
cytosolic NADP-ME expression in roots decreases with development, decreased levels of expression of cytosolic NADP-ME is observed in roots after incubating in solutions of Na2CO3 at pH 11.0 or NaHCO3 at pH 6.5; cytosolic NADP-ME is not inhibited by high malate concentrations at pH 7.0; NADP-ME is not affected by acetyl-CoA, CoA, pyruvate, L-alanine, alpha-ketoglutarate, glycerol-3-phosphate, 3-phospho-glycerate, and citrate
-
additional information
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
additional information
-
ZmnonC4-NADP-ME activity is not significantly modified by any chemical oxidant in 60 min
-
additional information
-
no inhibition of isozyme NADP-ME2 by tartrate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetyl carnitine
-
19% activation at 5 mM
acetyl-CoA
-
activates
acetyl-CoA
-
24% activation at 0.005 mM
acetyl-CoA
-
PtNADP-ME1, PtNADP-ME3, and PtNADP-ME4 are activated
aspartate
-, Q006P9, Q006Q0
2fold activation of isozyme NADP-ME1
aspartate
-
isozyme NADP-ME2 activity is highly stimulated at both low and high concentrations of 0.5 mM and 2 mM, respectively
ATP
-
18% activation at 5 mM
citrate
-
22% activation at 5 mM
citrate
-
activation is increased by light exposure
CoA
-
activates
CoA
-
29% activation at 0.005 mM
CoA
-, Q006P9, Q006Q0
slight activation of isozyme NADP-ME2
CoA
-
activates isozyme NADP-ME2
D-glucose 6-phosphate
-
activates PtNADP-ME3 and PtNADP-ME4
fumarate
-
increases activity of the mitochondrial enzyme at low malate concentrations, no effect on the activity of the cytosolic enzyme
fumarate
-
slight activation at low concentration
fumarate
-
isozyme NADP-ME2 activity is highly stimulated at both low and high concentrations of 0.5 mM and 2 mM, respectively, twofold activation of at 0.5 mM
fumarate
Q9LYG3, Q9XGZ0
about 4fold increase of activity in the presence of 7.5 mM fumarate
fumarate
Q5G1U0
when assayed at malate concentrations of 0.2 mM, fumarate activates the enzyme by 80% over the control activity
fumarate
-
fumarate activates the NADP-ME2 forward reaction by about 15fold at 0.05 mM NADP+, but only at about 1.5fold at 0.35 mM NADP+. The trans configuration of fumarate is crucial for the activating effect
L-aspartate
-
the cytosolic isozyme is 50% activated by L-aspartate
L-aspartate
-
10fold activation; the cytosolic isozyme is over 10fold activated by L-aspartate
L-glutamate
-
15% activation at 5 mM
malonyl-CoA
-
15% activation at 0.005 mM
palmitoyl-CoA
-
activates
palmitoyl-CoA
-
69% activation at 0.005 mM
succinate
-
increases activity of the mitochondrial enzyme at low malate concentrations, no effect on the activity of the cytosolic enzyme
succinate
-
slight activation up to 10 mM
succinate
-
activates
succinate
-
65% activation at 5 mM
succinate
-
activation is increased by light exposure
succinate
-
isozyme NADP-ME2 activity is highly stimulated at both low and high concentrations of 0.5 mM and 2 mM, respectively, partial activation of isozyme NADP-ME1 at 2 mM
succinate
Q9LYG3, Q9XGZ0
about 3fold increase of activity in the presence of 7.5 mM fumarate
succinate
Q5G1U0
when assayed at malate concentrations of 0.2 mM, succinate activates the enzyme by 121% over the control activity, at malate concentration of 1.2 mM, succinate activates the enzyme by 62% over the control activity
succinate
-
activates at 10 mM
UDP
-
10% activation at 5 mM
UDP-glucose
-
32% activation at 2 mM
methanol
-
activation is reversible and inversely related to the temperature
additional information
Q717I9, -
enzyme activity is not affected by oxaloacetate, fumarate, succinate, AMP, and NH4+
-
additional information
-
activation by light with 30% increased Vmax, activation by light is reduced by addition of dithiols
-
additional information
-
glutamate is a poor activator
-
additional information
Q6SZS7
the enzyme is induced by salt stress, NADP-ME activities in seedlings, leaves, and roots increase in response to NaCl
-
additional information
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme3 is not affected by light; the plastidic isozyme Hvme1 may perform housekeeping functions, but is upregulated as the photosynthetic decarboxylase
-
additional information
-, Q006P9, Q006Q0
no activation of isozyme NADP-ME2 by aspartate
-
additional information
Q9FRT2
expression of NADP-ME2 in roots is induced by stress from carbonates, NaHCO3 and Na2CO3, NaCl, and environmental pH changes in leaves and roots of seedlings, overview
-
additional information
Q5G1U0
after PEG 6000 treatment, the levels of cytosolic NADP-ME transcripts are enhanced by approximately 2.5times
-
additional information
B8PUQ5
activity of the NADP-ME is mostly enhanced under various stresses
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00014
-
(S)-malate
-
pH 8.0, 30C, mutant C246A
0.00015
-
(S)-malate
-
pH 7.0, 30C, wild-type, treated with dithiothreitol
0.00017
-
(S)-malate
-
pH 8.0, 30C, wild-type, treated with diamide
0.00039
-
(S)-malate
-
pH 8.0, 30C, wild-type, treated with dithiothreitol
0.0008
-
(S)-malate
-
pH 7.0, 30C, wild-type, treated with diamide
0.0017
-
(S)-malate
-
pH 8.0, 30C, mutant C231A
0.00296
-
(S)-malate
-
pH 7.5, NADP-ME1
0.003
-
(S)-malate
-
pH 8.0, 30C, mutant C192A
0.0033
-
(S)-malate
-
pH 7.5, NADP-ME2
0.0043
-
(S)-malate
-
pH 8.0, 30C, mutant C270A
0.018
-
(S)-malate
-
60C, pH 8.0, presence of Mn2+
0.04
-
(S)-malate
-
pH 7.0, wild-type C4-NADP-ME isozyme
0.05
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme D258A
0.065
-
(S)-malate
-
60C, pH 8.0, presence of Mg2+
0.071
-
(S)-malate
-
pH 7.0, 60C
0.08
-
(S)-malate
-
pH 7.4, 25C, Mn2+-activated, wild-type enzyme
0.08
-
(S)-malate
-
pH 7.0, 30C, oxidized isozyme ZmC4-NADP-ME
0.1
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme D235A; pH 7.4, 25C, mutant enzyme D257A
0.13
-
(S)-malate
-, Q006P9, Q006Q0
pH 7.3, isozyme NADP-ME1
0.13
-
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
0.14
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
0.15
-
(S)-malate
-
pH 7.0, 30C, reduced isozyme ZmC4-NADP-ME
0.17
-
(S)-malate
-
pH 8.0, 30C, oxidized isozyme ZmC4-NADP-ME
0.23
-
(S)-malate
-
pH 7.5, NADP-ME4
0.23
-
(S)-malate
-
pH 4.5, 25C, wild-type enzyme
0.23
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME4
0.24
-
(S)-malate
-
recombinant ME1, pH 7.4, temperature not specified in the publication
0.27
-
(S)-malate
-
pH 7.4, 25C, Mg2+-activated, wild-type enzyme
0.32
-
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
0.39
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME
0.4
-
(S)-malate
-
mutant E314A, with NADP+, pH 7.4, 30C
0.49
-
(S)-malate
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30C
0.49
-
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
0.51
-
(S)-malate
-
pH 7.0, wild-type non-C4-NADP-ME isozyme
0.6
-
(S)-malate
Q27IE1, Q6PMI1, Q6PMI2
recombinant isozyme Hvme1
0.67
-
(S)-malate
Q717I9, -
pH 7.6, 25C
0.68
-
(S)-malate
-
mutant enzyme D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.8
-
(S)-malate
Q9LYG3, Q9XGZ0
pH 7.5
0.83
-
(S)-malate
-
pH 7.5, NADP-ME3
0.83
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME3
0.84
-
(S)-malate
-
mutant enzyme H51A/D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.89
-
(S)-malate
-
mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.9
-
(S)-malate
-
mutant S346K, with NADP+, pH 7.4, 30C
0.92
-
(S)-malate
-
mutant enzyme H142A/D568A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.95
-
(S)-malate
-
mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.97
-
(S)-malate
-
mutant enzyme D568A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.98
-
(S)-malate
-
mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30C
1
-
(S)-malate
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
1
-
(S)-malate
-
mutant E314A/S346K/K347Y/K362H, with NAD+, pH 7.4, 30C; mutant S346K/K347Y, with NADP+, pH 7.4, 30C; with NADP+, wild-type enzyme, pH 7.4, 30C
1.03
-
(S)-malate
-
mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
1.1
-
(S)-malate
-
mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30C
1.1
-
(S)-malate
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
1.2
-
(S)-malate
-
mutant E314A/S346K, with NADP+, pH 7.4, 30C
1.4
-
(S)-malate
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
1.46
-
(S)-malate
-, Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME2
1.5
-
(S)-malate
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
1.7
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
1.8
-
(S)-malate
-
mutants K347Y and K362Q, with NADP+, pH 7.4, 30C
2
-
(S)-malate
-
mutant E314A/S346K/K347Y/K362Q, with NAD+, pH 7.4, 30C
2.3
-
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
2.6
-
(S)-malate
Q6T5D1, Q9FRT2
recombinant NADP-ME2
2.9
-
(S)-malate
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
2.96
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME1
3
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
3
-
(S)-malate
-
mutant E314A/S346I/K347D/K362H, with NAD+, pH 7.4, 30C
3.1
-
(S)-malate
Q6T5D1, Q9FRT2
recombinant NADP-ME2
3.3
-
(S)-malate
Q9LYG3, Q9XGZ0
pH 7.5
3.33
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME2
3.41
-
(S)-malate
-
pH 7.5, recombinant MaeB
3.7
-
(S)-malate
-
mutant S346K/K362Q, with NADP+, pH 7.4, 30C
4
-
(S)-malate
-
mutants E314A, S346K, E314A/S346K, S346K/K362Q, and S346K/K347Y/K362Q, with NAD+, pH 7.4, 30C
4.3
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
4.9
-
(S)-malate
-
mutant K362H, with NADP+, pH 7.4, 30C
5
-
(S)-malate
-
mutants K347Y, K362Q, and S346K/K347Y, with NAD+, pH 7.4, 30C; with NAD+, wild-type enzyme, pH 7.4, 30C
5.5
-
(S)-malate
-
mutant S347Y/K362Q, with NADP+, pH 7.4, 30C
5.6
-
(S)-malate
-
mutant E314A/S346K/K347Y/K362Q, with NADP+, pH 7.4, 30C
6
-
(S)-malate
-
mutants S346K/K347Y/K362H, with NAD+, pH 7.4, 30C
6.4
-
(S)-malate
Q9F3K4
pH 8.0, 30C, recombinant enzyme
7
-
(S)-malate
-
mutant S346I/K347D/K362H, with NAD+, pH 7.4, 30C
7.3
-
(S)-malate
-
mutant E314A/S346K/K347Y/K362H, with NADP+, pH 7.4, 30C
8
-
(S)-malate
-
mutants K362H and S347Y/K362Q, with NAD+, pH 7.4, 30C
10
-
(S)-malate
-
mutant S346K/K347Y/K362Q, with NADP+, pH 7.4, 30C
11
-
(S)-malate
-
mutant S346K/K347Y/K362H, with NADP+, pH 7.4, 30C
13.33
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme E234A
24
-
(S)-malate
-
mutant E314A/S346I/K347D/K362H, with NADP+, pH 7.4, 30C
36
-
(S)-malate
-
mutant S346I/K347D/K362H, with NADP+, pH 7.4, 30C
13.3
-
bicarbonate
-
-
27.9
-
bicarbonate
-
-
0.04
-
L-Malate
-
-
0.041
-
L-Malate
Pigeon
-
pH 6.5
0.073
-
L-Malate
-
-
0.08
-
L-Malate
-
-
0.09
-
L-Malate
-
-
0.12
-
L-Malate
-
with NADP+ as cosubstrate
0.14
-
L-Malate
-
cytosolic enzyme
0.19
-
L-Malate
-
-
0.19
-
L-Malate
-
recombinant enzyme, pH 7.0
0.216
-
L-Malate
-
-
0.22
-
L-Malate
-
pH 7.6-7.7, 25C
0.23
-
L-Malate
-
wild-type enzyme, pH 8.0, 30C
0.23
-
L-Malate
-
wild-type enzyme, pH 7.0
0.26
-
L-Malate
-
pH 8.0, 30C, light
0.28
-
L-Malate
-
pH 8.0, 30C, dark
0.31
-
L-Malate
-
mutant K435L/K436L, pH 8.0, 30C
0.39
-
L-Malate
Pigeon
-
pH 7.5
0.46
-
L-Malate
-
-
0.5
-
L-Malate
-
mutant A392G, pH 7.0
0.53
-
L-Malate
-
-
0.6
-
L-Malate
-
cytosolic enzyme
0.666
-
L-Malate
-
at 1.0 mM Mn2+
0.68
-
L-Malate
-
-
0.96
-
L-Malate
-
-
0.96
-
L-Malate
-
with NAD+ as cosubstrate
1.08
-
L-Malate
-
at 5.0 mM Mn2+
1.1
-
L-Malate
-
mutant A387G, pH 7.0
1.1
-
L-Malate
-
pH 7.3, 30C, isozyme 2
1.25
-
L-Malate
-
mitochondrial enzyme
2.6
-
L-Malate
-
mutant K225I, pH 8.0, 30C
2.9
-
L-Malate
-
mutant R237L, pH 8.0, 30C
2.9
-
L-Malate
-
mutant R237L, pH 7.0
3.3
-
L-Malate
Pigeon
-
pH 8.5
4.5
-
L-Malate
-
-
1.06
-
malate
-
activation by Mn2+
0.25
-
NAD+
-
60C, pH 8.0
0.9
-
NAD+
-
mutants E314A/S346K/K347Y/K362H and E314A/S346I/K347D/K362H, pH 7.4, 30C
1.5
-
NAD+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30C
1.6
-
NAD+
-
mutant E314A, pH 7.4, 30C
1.9
-
NAD+
-
mutant K435L/K436L, pH 8.0, 30C
4.6
-
NAD+
-
-
5
-
NAD+
-
mutant E314A/S346K, pH 7.4, 30C
6
-
NAD+
-
mutant A392G, pH 7.0
6.5
-
NAD+
-
mutant S346I/K347D/K362H, pH 7.4, 30C
7.1
-
NAD+
-
mutant S346K/K347Y/K362H, pH 7.4, 30C
8.1
-
NAD+
-
wild-type enzyme, pH 8.0, 30C
8.1
-
NAD+
-
wild-type enzyme, pH 7.0
10
-
NAD+
-
mutant S346K/K347Y/K362Q, pH 7.4, 30C
11
-
NAD+
-
mutant K347Y, pH 7.4, 30C
11.5
-
NAD+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30C
13
-
NAD+
-
mutant K362Q, pH 7.4, 30C
14
-
NAD+
-
mutant K362H, pH 7.4, 30C; mutant S346K/K362Q, pH 7.4, 30C
17
-
NAD+
-
mutant S346K, pH 7.4, 30C
18
-
NAD+
-
mutant S346K/K347Y, pH 7.4, 30C
18.35
-
NAD+
-
wild-type enzyme, pH 7.4, 30C
18.6
-
NAD+
-
in 50 mM Tris-HCl (pH 7.4)
20
-
NAD+
-
mutant S347Y/K362Q, pH 7.4, 30C
0.00118
-
NADP+
-
cytosolic enzyme
0.00139
-
NADP+
-
-
0.00171
-
NADP+
-, Q006P9, Q006Q0
pH 7.3, isozyme NADP-ME1
0.00179
-
NADP+
-
pH 7.4, 25C, mutant enzyme D235A
0.0018
-
NADP+
-
pH 7.4, 25C, mutant enzyme E234A
0.00188
-
NADP+
-
mitochondrial enzyme
0.002
-
NADP+
-
-
0.002
-
NADP+
-
mutant E314A, pH 7.4, 30C
0.00207
-
NADP+
-
pH 7.4, 25C, Mn2+-activated, wild-type enzyme
0.0026
-
NADP+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30C
0.0028
-
NADP+
Q717I9, -
pH 7.6, 25C
0.00283
-
NADP+
-
pH 7.4, 25C, mutant enzyme D257A
0.00296
-
NADP+
-
pH 7.4, 25C, mutant enzyme D258A
0.003
-
NADP+
-
60C, pH 8.0
0.003
-
NADP+
-
mutant E314A/S346K, pH 7.4, 30C
0.0031
-
NADP+
-
-
0.00315
-
NADP+
-
-
0.0034
-
NADP+
-
pH 4.5, 25C, wild-type enzyme
0.0036
-
NADP+
-
pH 7.0, 30C, oxidized isozyme ZmC4-NADP-ME; pH 7.0, 30C, wild-type, treated with diamide
0.0037
-
NADP+
-
mutant enzyme H51A/D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.0039
-
NADP+
-
mutant enzyme D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.004
-
NADP+
-
mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30C; mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.0042
-
NADP+
-
mutant enzyme H142A/D568A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.00429
-
NADP+
-, Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME2
0.0046
-
NADP+
-
-
0.0048
-
NADP+
-
mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.005
-
NADP+
-
mutant enzyme D568A, in 50 mM Tris-HCl, pH 7.4, at 30C; mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.005
-
NADP+
-
wild-type enzyme, pH 7.4, 30C
0.0053
-
NADP+
-
in 50 mM Tris-HCl (pH 7.4)
0.0053
-
NADP+
-
pH 8.0, 30C, mutant C246A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
0.0065
-
NADP+
-
pH 7.5, NADP-ME3
0.0065
-
NADP+
-
pH 7.5, 30C, isozyme NADP-ME3
0.0065
-
NADP+
Q9LYG3, Q9XGZ0
pH 7.5
0.0072
-
NADP+
-
mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30C
0.008
-
NADP+
-
wild-type enzyme, pH 8.0, 30C
0.008
-
NADP+
-
wild-type enzyme, pH 7.0
0.0082
-
NADP+
-
-
0.0086
-
NADP+
-
-
0.0086
-
NADP+
-
recombinant enzyme, pH 7.0
0.0088
-
NADP+
-
pH 8.0, 30C, oxidized isozyme ZmC4-NADP-ME; pH 8.0, 30C, wild-type, treated with diamide
0.009
-
NADP+
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30C
0.0092
-
NADP+
-
-
0.0102
-
NADP+
-
pH 7.5, NADP-ME4
0.0102
-
NADP+
-
pH 7.5, 30C, isozyme NADP-ME4
0.0103
-
NADP+
-
pH 7.6-7.7, 25C
0.012
-
NADP+
-
-
0.0125
-
NADP+
-
pH 7.0, 60C
0.013
-
NADP+
-
pH 7.3, 30C, isozyme 2
0.013
-
NADP+
-
mutant S346K, pH 7.4, 30C
0.0135
-
NADP+
-
pH 8.0, 30C, mutant C270A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
0.014
-
NADP+
-
activation by Mn2+
0.0147
-
NADP+
-
pH 7.0, 30C, reduced isozyme ZmC4-NADP-ME; pH 7.0, 30C, wild-type, treated with dithiothreitol
0.015
-
NADP+
-
-
0.015
-
NADP+
-
pH 8.0, 30C, mutant C231A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
0.0154
-
NADP+
-
pH 8.0, 30C, mutant C192A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
0.016
-
NADP+
Pigeon
-
pH 7.5
0.016
-
NADP+
-
-
0.016
-
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
0.025
-
NADP+
-
activation by Mg2+
0.027
-
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
0.0276
-
NADP+
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME; pH 8.0, 30C, wild-type, treated with dithiothreitol
0.03
-
NADP+
-
mutant A392G, pH 7.0
0.03
-
NADP+
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
0.03
-
NADP+
-
mutant K347Y, pH 7.4, 30C
0.032
-
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
0.036
-
NADP+
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
0.037
-
NADP+
-
-
0.037
-
NADP+
-
mutant A387G, pH 7.0
0.04
-
NADP+
-
pH 7.0, wild-type C4-NADP-ME isozyme
0.0415
-
NADP+
-
pH 7.5, recombinant MaeB
0.0472
-
NADP+
-
-
0.048
-
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
0.072
-
NADP+
Q9LYG3, Q9XGZ0
pH 7.5
0.0721
-
NADP+
-
pH 7.5, NADP-ME2
0.0721
-
NADP+
-
pH 7.5, 30C, isozyme NADP-ME2
0.073
-
NADP+
-
mutant K435L/K436L, pH 8.0, 30C
0.075
-
NADP+
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
0.079
-
NADP+
Q6T5D1, Q9FRT2
recombinant NADP-ME2
0.093
-
NADP+
Q6T5D1, Q9FRT2
recombinant NADP-ME2
0.1
-
NADP+
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
0.107
-
NADP+
Q9F3K4
pH 8.0, 30C, recombinant enzyme
0.12
-
NADP+
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
0.123
-
NADP+
-
mutant K225I, pH 8.0, 30C
0.14
-
NADP+
-
mutant S346K/K347Y, pH 7.4, 30C
0.205
-
NADP+
-
pH 7.5, NADP-ME1
0.205
-
NADP+
-
pH 7.5, 30C, isozyme NADP-ME1
0.29
-
NADP+
-
mutant R237L, pH 8.0, 30C
0.29
-
NADP+
-
mutant R237L, pH 7.0
0.36
-
NADP+
-
mutant K362H, pH 7.4, 30C
0.51
-
NADP+
-
pH 7.0, wild-type non-C4-NADP-ME isozyme
0.76
-
NADP+
-
mutant K362Q, pH 7.4, 30C
3
-
NADP+
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30C
5
-
NADP+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30C
6
-
NADP+
-
mutant S346K/K362Q, pH 7.4, 30C
8.2
-
NADP+
-
-
12
-
NADP+
-
mutant S347Y/K362Q, pH 7.4, 30C
17
-
NADP+
-
mutant S346K/K347Y/K362Q, pH 7.4, 30C
29
-
NADP+
-
mutants S346K/K347Y/K362H and E314A/S346I/K347D/K362H, pH 7.4, 30C
116
-
NADP+
-
mutant S346I/K347D/K362H, pH 7.4, 30C
0.002
-
NADPH
-
-
0.0053
-
NADPH
-
-
0.045
-
NADPH
-
-
23
-
NaHCO3
-
-
0.5
-
pyruvate
Q9LYG3, Q9XGZ0
pH 7.0
0.69
-
pyruvate
-, Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME1
2.6
-
pyruvate
-, Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME2
3
-
pyruvate
-
-
4.3
-
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
4.8
-
pyruvate
-
-
5
-
pyruvate
Q9LYG3, Q9XGZ0
pH 7.0
5.1
-
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
5.3
-
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
5.8
-
pyruvate
-
recombinant ME1, pH 7.4, temperature not specified in the publication
5.9
-
pyruvate
-
-
7.2
-
pyruvate
-
-
7.6
-
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
10
-
pyruvate
-
cytosolic enzyme
16.9
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME1
18.1
-
pyruvate
Q9F3K4
pH 8.0, 30C, recombinant enzyme
25
-
pyruvate
-
mitochondrial enzyme
26.3
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME4
48.2
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME3
138.9
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME2
3.63
-
malate
-
activation by Mg2+
additional information
-
additional information
-
kinetics of mutant enzymes, overview
-
additional information
-
additional information
-
with malate as the variable substrate the kinetics are nonhyperbolic, exhibiting a sigmoidal response with a positive Hill coefficient
-
additional information
-
additional information
-
kinetics of recombinant chimeric mutant enzymes, overview
-
additional information
-
additional information
Q27IE1, Q6PMI1, Q6PMI2
recombinant isozyme Hvme1, kinetics; recombinant isozyme Hvme3, kinetics
-
additional information
-
additional information
-
kinetics of isozymes at different pH, overview
-
additional information
-
additional information
-
among the five isoforms, PtNADP-ME5 has the highest affinities for NADP while PtNADP-ME2 exhibits the lowest affinities toward both malate and NADP+
-
additional information
-
additional information
-
kinetics of NADP+ and (S)-malate at different NADP+ and fumarate concentrations, overview
-
additional information
-
additional information
-
human m-NAD(P)-ME is a non-cooperative enzyme for substrate L-malate binding, steady-state kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.004
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme D235A
0.005
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme E234A
0.006
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme D258A
0.3
-
(S)-malate
-
pH 7.4, 25C, Mg2+-activated, wild-type enzyme
0.9
-
(S)-malate
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
1.1
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme D257A
1.1
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
1.6
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
3.55
-
(S)-malate
-
pH 7.0, 30C, oxidized isozyme ZmC4-NADP-ME
5.6
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
8.35
-
(S)-malate
-
pH 7.0, 30C, reduced isozyme ZmC4-NADP-ME
12.6
-
(S)-malate
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
13.6
-
(S)-malate
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
15
-
(S)-malate
-
pH 7.4, 25C, Mn2+-activated, wild-type enzyme
15.7
-
(S)-malate
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
19.1
-
(S)-malate
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
23.2
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
31.34
-
(S)-malate
-
pH 7.4, 25C, Mn2+-activated, wild-type enzyme
34.83
-
(S)-malate
-
pH 7.4, 25C, Mg2+-activated, wild-type enzyme
38.7
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME1
46.44
-
(S)-malate
-
pH 7.4, 25C, mutant enzyme E234A
84.83
-
(S)-malate
-
mutant enzyme H51A/D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
91
-
(S)-malate
-
pH 8.0, 30C, oxidized isozyme ZmC4-NADP-ME
91.7
-
(S)-malate
Q6T5D1, Q9FRT2
recombinant NADP-ME2
94.57
-
(S)-malate
-
mutant enzyme D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
95.53
-
(S)-malate
-
mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
96.7
-
(S)-malate
Q6T5D1, Q9FRT2
recombinant NADP-ME3
98.03
-
(S)-malate
-
mutant enzyme H142A/D568A, in 50 mM Tris-HCl, pH 7.4, at 30C
104.4
-
(S)-malate
-
pH 7.0, wild-type C4-NADP-ME isozyme
105.3
-
(S)-malate
-
mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
106
-
(S)-malate
-
mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30C
109.5
-
(S)-malate
-
mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30C
110.9
-
(S)-malate
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30C
122.7
-
(S)-malate
-
mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30C
136.9
-
(S)-malate
-
mutant enzyme D568A, in 50 mM Tris-HCl, pH 7.4, at 30C
140.1
-
(S)-malate
-
pH 4.5, 25C, wild-type enzyme
151.3
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME4
151.7
-
(S)-malate
-
pH 7.0, wild-type non-C4-NADP-ME isozyme
154.3
-
(S)-malate
-, Q006P9, Q006Q0
pH 7.3, isozyme NADP-ME1
177
-
(S)-malate
-, Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME2
242
-
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
268
-
(S)-malate
Q9LYG3, Q9XGZ0
pH 7.5
268.1
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME3
269
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME
324
-
(S)-malate
Q9LYG3, Q9XGZ0
pH 7.5
324.1
-
(S)-malate
-
pH 7.5, 30C, isozyme NADP-ME2
376
-
(S)-malate
-
pH 8.0, 60C
518
-
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
683
-
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
1132
-
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
160
-
L-Malate
-
-
13.5
-
NAD+
-
wild-type enzyme, pH 8.0, 30C
13.5
-
NAD+
-
wild-type enzyme, pH 7.0
18.4
-
NAD+
-
mutant K435L/K436L, pH 8.0, 30C
22
-
NAD+
-
mutant S346K, pH 7.4, 30C
28.9
-
NAD+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30C
34.18
-
NAD+
-
in 50 mM Tris-HCl (pH 7.4)
40
-
NAD+
-
mutant K347Y, pH 7.4, 30C
40.6
-
NAD+
-
mutant A392G, pH 7.0
51
-
NAD+
-
wild-type enzyme, pH 7.4, 30C
53
-
NAD+
-
mutant S347Y/K362Q, pH 7.4, 30C
60
-
NAD+
-
mutant K362Q, pH 7.4, 30C
65
-
NAD+
-
mutant S346K/K347Y, pH 7.4, 30C
108
-
NAD+
-
mutant K362H, pH 7.4, 30C
110
-
NAD+
-
mutant S346K/K362Q, pH 7.4, 30C
113
-
NAD+
-
mutant E314A, pH 7.4, 30C
124
-
NAD+
-
mutant S346K/K347Y/K362Q, pH 7.4, 30C
131
-
NAD+
-
mutant S346I/K347D/K362H, pH 7.4, 30C
145
-
NAD+
-
mutant E314A/S346K, pH 7.4, 30C
166
-
NAD+
-
mutant E314A/S346I/K347D/K362H, pH 7.4, 30C
208
-
NAD+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30C
219
-
NAD+
-
mutant S346K/K347Y/K362H, pH 7.4, 30C
258
-
NAD+
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30C
0.38
-
NADP+
-
mutant R237L, pH 8.0, 30C
0.38
-
NADP+
-
mutant R237L, pH 7.0
0.8
-
NADP+
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
1.1
-
NADP+
-
mutant K225I, pH 8.0, 30C
1.1
-
NADP+
-
pH 8.0, 30C, mutant C246A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
1.3
-
NADP+
-
mutant S346I/K347D/K362H, pH 7.4, 30C
1.6
-
NADP+
-
pH 8.0, 30C, mutant C270A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
3.55
-
NADP+
-
pH 7.0, 30C, oxidized isozyme ZmC4-NADP-ME; pH 7.0, 30C, wild-type, treated with diamide
4.2
-
NADP+
-
mutant A387G, pH 7.0
5.6
-
NADP+
-
pH 8.0, 30C, mutant C192A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
8
-
NADP+
-
mutant S346K/K347Y/K362H, pH 7.4, 30C
8.35
-
NADP+
-
pH 7.0, 30C, reduced isozyme ZmC4-NADP-ME; pH 7.0, 30C, wild-type, treated with dithiothreitol
13.2
-
NADP+
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
14.2
-
NADP+
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
15
-
NADP+
-
mutant E314A/S346I/K347D/K362H, pH 7.4, 30C; mutant S346K/K347Y/K362Q, pH 7.4, 30C
15.9
-
NADP+
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
19.5
-
NADP+
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
23.2
-
NADP+
-
pH 8.0, 30C, mutant C231A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
26
-
NADP+
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30C
30.8
-
NADP+
-
recombinant enzyme, pH 7.0
38.7
-
NADP+
-
pH 7.5, NADP-ME1
51
-
NADP+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30C
66.6
-
NADP+
-
pH 7.5, recombinant MaeB
78
-
NADP+
-
mutant S347Y/K362Q, pH 7.4, 30C
88.3
-
NADP+
Q6T5D1, Q9FRT2
recombinant NADP-ME2
91
-
NADP+
-
pH 8.0, 30C, oxidized isozyme ZmC4-NADP-ME; pH 8.0, 30C, wild-type, treated with diamide
98.3
-
NADP+
Q6T5D1, Q9FRT2
recombinant NADP-ME3
102
-
NADP+
-
mutant S346K/K347Y, pH 7.4, 30C
110
-
NADP+
-
mutant E314A, pH 7.4, 30C
112
-
NADP+
-
mutant S346K/K362Q, pH 7.4, 30C
113.2
-
NADP+
-
in 50 mM Tris-HCl (pH 7.4)
121
-
NADP+
-
mutant K347Y, pH 7.4, 30C
126
-
NADP+
-
wild-type enzyme, pH 7.4, 30C
129
-
NADP+
-
mutant S346K, pH 7.4, 30C
132
-
NADP+
-
mutant K362Q, pH 7.4, 30C
135.8
-
NADP+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30C
137
-
NADP+
-
mutant E314A/S346K, pH 7.4, 30C
149
-
NADP+
-
mutant K362H, pH 7.4, 30C
151.3
-
NADP+
-
pH 7.5, NADP-ME4
181.1
-
NADP+
-
mutant K435L/K436L, pH 8.0, 30C
200.3
-
NADP+
-
mutant A392G, pH 7.0
201.3
-
NADP+
-
wild-type enzyme, pH 8.0, 30C
201.3
-
NADP+
-
wild-type enzyme, pH 7.0
268.1
-
NADP+
-
pH 7.5, NADP-ME3
269
-
NADP+
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME; pH 8.0, 30C, wild-type, treated with dithiothreitol
284
-
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
324.1
-
NADP+
-
pH 7.5, NADP-ME2
504
-
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
691
-
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
1206
-
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
4670
-
NADP+
-
pH 7.5, NADP-ME2
8.3
-
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
16.5
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME1
21.6
-
pyruvate
-, Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME2
34
-
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
39
-
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
75
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME2
75
-
pyruvate
Q9LYG3, Q9XGZ0
pH 7.0
113
-
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
158.4
-
pyruvate
-, Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME1
237
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME3
237
-
pyruvate
Q9LYG3, Q9XGZ0
pH 7.0
284.1
-
pyruvate
-
pH 7.0, 30C, isozyme NADP-ME4
582
-
L-Malate
-
assuming an octameric oligomerization state
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.14
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
200
0.37
-
(S)-malate
-
pH 8.0, 30C, mutant C270A
200
0.9
-
(S)-malate
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
200
1.7
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
200
1.9
-
(S)-malate
-
pH 8.0, 30C, mutant C192A
200
3
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
200
4.3
-
(S)-malate
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
200
4.3
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
200
7.8
-
(S)-malate
-
pH 8.0, 30C, mutant C246A
200
9.1
-
(S)-malate
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
200
11
-
(S)-malate
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
200
13.6
-
(S)-malate
-
pH 8.0, 30C, mutant C231A
200
170
-
(S)-malate
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
200
297
-
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
200
494
-
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
200
689.7
-
(S)-malate
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME
200
690
-
(S)-malate
-
pH 8.0, 30C, wild-type, treated with dithiothreitol
200
3536
-
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
200
3981
-
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
200
2.8
-
NAD+
-
wild-type enzyme, pH 7.4, 30C
7
0.12
-
NADP+
-
pH 8.0, 30C, mutant C270A
10
0.21
-
NADP+
-
pH 8.0, 30C, mutant C246A
10
0.36
-
NADP+
-
pH 8.0, 30C, mutant C192A
10
0.37
-
NADP+
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
10
1.5
-
NADP+
-
pH 8.0, 30C, mutant C231A
10
1.86
-
NADP+
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
10
7.86
-
NADP+
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
10
9.7
-
NADP+
-
pH 8.0, 30C, wild-type, treated with dithiothreitol
10
13.64
-
NADP+
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
10
22
-
NADP+
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
10
110
-
NADP+
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
10
140
-
NADP+
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
10
210
-
NADP+
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
10
650
-
NADP+
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
10
9746
-
NADP+
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME
10
17780
-
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
10
18680
-
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
10
21600
-
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
10
25170
-
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
10
36000
-
NADP+
-
wild-type enzyme, pH 7.4, 30C
10
1.1
-
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
31
6
-
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
31
8
-
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
31
26
-
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication; pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
31
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.28
-
(S)-malate
-
pH 4.5, 25C, wild-type enzyme
0.105
-
2'-AMP
-
wild-type enzyme, pH 8.0, 30C
0.688
-
2'-AMP
-
mutant K435L/K436L, pH 8.0, 30C
0.256
-
5'-AMP
-
mutant K435L/K436L, pH 8.0, 30C
0.439
-
5'-AMP
-
wild-type enzyme, pH 8.0, 30C
0.73
-
ATP
-
mutants E314A and E314A/S346K, in presence of NAD+, pH 7.4, 30C
3.3
-
ATP
-
mutant E314A/S346K/K347Y/K362Q, in presence of NAD+, pH 7.4, 30C
3.9
-
ATP
-
mutant E314A/S346K/K347Y/K362Q, in presence of NADP+, pH 7.4, 30C
4.77
-
ATP
-
in the presence of NAD+, in 50 mM Tris-HCl (pH 7.4)
5.91
-
ATP
-
in the presence of NADP+, in 50 mM Tris-HCl (pH 7.4)
17.2
-
ATP
-
mutant E314A/S346K, in presence of NAPD+, pH 7.4, 30C
17.27
-
ATP
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30C
18.1
-
ATP
-
mutant E314A, in presence of NAPD+, pH 7.4, 30C
20.6
-
ATP
-
wild-type enzyme, in presence of NADP+, pH 7.4, 30C
23.2
-
ATP
-
wild-type enzyme, in presence of NAD+, pH 7.4, 30C
0.372
-
CO2
-
versus NADP+, pH 7.6-7.7, 25C
0.83
-
CO2
-
versus L-malate, pH 7.6-7.7, 25C
0.01
-
Cu2+
-
pH 7.4, 30C, with Mg2+
0.045
-
Cu2+
-
pH 7.4, 30C, with Mn2+
0.0089
-
NADP+
-
pH 4.5, 25C, wild-type enzyme
0.046
-
NADPH
-
versus NADP+, pH 7.6-7.7, 25C
0.492
-
NADPH
-
versus L-malate, pH 7.6-7.7, 25C
0.18
-
oxalate
-
pH 8.0, 30C, dark
0.3
-
oxalate
-
pH 8.0, 30C, light
0.016
-
pyruvate
-
pH 7.6-7.7, 25C
1.3
-
pyruvate
-
pH 8.0, 30C, dark
2.6
-
pyruvate
-
pH 8.0, 30C, light
4.7
-
L-Malate
-
recombinant enzyme, pH 7.0
additional information
-
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.008
0.89
-
enzyme activity in several recombinant strains, overview
0.01
-
-
below, wild-type strain W3110
0.048
-
-, Q006P9, Q006Q0
enzyme extracts from flowers; enzyme extracts from flowers
0.069
-
-, Q006P9, Q006Q0
enzyme extracts from stems; enzyme extracts from stems
0.072
-
-, Q006P9, Q006Q0
enzyme extracts from leaves; enzyme extracts from leaves
0.16
-
Q6SZS7
root enzyme under salt stress after 24 h
0.2
-
Q6SZS7
leaf enzyme under salt stress after 24 h
0.571
-
-, Q006P9, Q006Q0
enzyme extract from roots; enzyme extract from roots
1.69
-
-
MaeB overexpressed in an anaplerotic enzyme overexpressing strain
1.92
-
-
recombinant enzyme in INS-1 832/13 cells, reverse reaction, pH 7.4, temperature not specified in the publication
3.15
-
P76558
pH 7.8, 46C, purified recombinant enzyme
5.04
-
-
-
18.2
-
-
purified enzyme
30.14
-
-
partially purified leaf isozyme 2
36.6
-
-
60C, pH 8.0
56.35
-
-
-
78.6
-
Q6T5D1, Q9FRT2
recombinant NADP-ME3
85.1
-
Q6T5D1, Q9FRT2
recombinant NADP-ME2
90.9
-
-
mitochondrial enzyme
91.4
-
-
cytosolic enzyme
199
-
Q717I9, -
purified enzyme
additional information
-
Pigeon
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
wild-type and transgenic mutant
additional information
-
-
the enzyme activity is similar in Nicotiana benthamiana wild-type plants and transgenic plants, expressing potyviral helper component protease HC-pro or Potato virus Y strain NTN, overview
additional information
-
-
isozyme expression levels, pyruvate cycling and isozyme activity in pancreatic islets, overview
additional information
-
-
-
additional information
-
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
changes in NADPH contents in the leaves of plant species towards the end of the light or darkness periods, diurnal changes in malate and citrate contents in gametophores kept under control, hypoxia, high irradiance, drought stress, and CO2-free air conditions, comparison to other species, overiew
additional information
-
-
relative NADP-malic enzyme activity in rosette leaves of Arabidopsis thaliana wild-type, loss-of-function (nadp-me2.1 and -2.2), complemented (nadp-me2.1 ? ME2-1 and -2) and overexpressing (ME2-1 and -2) lines, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
assay at, forward reaction
5.2
-
-
decarboxylation of oxaloacetate
6.6
-
-
mitochondrial enzyme, carboxylation
6.8
-
-
MES-NaOH buffer
6.9
7.2
-
-
6.9
7.8
Q8W000
isozyme ZmChlMe2
7
8
-
assay at
7
-
-
carboxylation and decarboxylation, cytosolic enzyme
7
-
-
TES-NaOH buffer
7
-
-
assay at
7
-
-
reverse reaction
7
-
-
assay at
7
-
-, Q006P9, Q006Q0
isozyme NADP-ME1, reverse reaction; isozyme NADP-ME2, forward and reverse reaction
7
-
-
assay at, reverse reaction
7
-
Q5G1U0
-
7
-
-
assay at
7
-
-
reductive carboxylation of pyruvate
7.1
-
-
Tris-HCl buffer
7.1
-
-
NADP+-linked decarboxylation of malate, at 0.2 mM malate
7.2
-
Pigeon
-
in presence of 0.1 mM malate
7.2
-
-
-
7.3
-
-
carboxylation of pyruvate
7.3
-
-
carboxylation of pyruvate; NADP+-linked decarboxylation of malate, at 1 mM malate
7.3
-
-
isozyme 2
7.3
-
Q6T5D1, Q9FRT2
recombinant NADP-ME2
7.3
-
-, Q006P9, Q006Q0
isozyme NADP-ME1, forward reaction
7.4
-
-
carboxylation of pyruvate
7.4
-
-
cytosolic enzyme, NADPH-dependent reductive carboxylation of pyruvate
7.4
-
-
assay at
7.4
-
-
assay at, reverse reaction
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.5
8.5
Q717I9, -
-
7.5
-
-
TES-NaOH buffer
7.5
-
-
carboxylation of pyruvate
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
Q6SZS7
assay at, forward reaction
7.5
-
-
forward reaction
7.5
-
A6XP71
assay at
7.5
-
A6XP72
assay at
7.5
-
-
assay at
7.5
-
Q27IE1, Q6PMI1, Q6PMI2
recombinant isozyme Hvme3
7.5
-
-
assay at, forward reaction
7.5
-
B8PUQ5
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
oxidative decarboxylation of malate
7.6
7.7
-
both reaction directions
7.6
-
-
cytosolic enzyme, decarboxylation
7.7
-
Q6T5D1, Q9FRT2
recombinant NADP-ME2
7.8
-
-
oxidative decarboxylation of L-malate
7.8
-
-
assay at
7.8
-
Q27IE1, Q6PMI1, Q6PMI2
recombinant isozyme Hvme1
7.8
-
P76558
-
8
-
-
decarboxylation of malate
8
-
-
-
8
-
-
NADP+-dependent decarboxylation of malate, at 10 mM malate, mitochondrial enzyme and cytosolic enzyme
8
-
-
NADP+-linked decarboxylation of malate, at 10 mM malate
8
-
-
assay at
8
-
-
recombinant enzyme
8
-
-
assay at
8
-
Q8W000
approximately, isozyme ZmChlMe1
8
-
-
assay at
8
-
Q9F3K4
assay at
8.1
-
-
assay at
8.3
-
-
with 0.1 mM L-malate
8.3
-
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
assay at
8.5
9
Pigeon
-
in presence of 0.1 M malate
8.8
-
-
with 1 mM L-malate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
-
5.5
8.5
Q27IE1, Q6PMI1, Q6PMI2
-
6.5
7.5
-
pH 6.5: about 55% of maximal activity, pH 7.5: about 35% of maximal activity
6.8
8
-
pH 6.8: about 40% of maximal activity, pH 8.0: about 70% of maximal activity, cytosolic enzyme, NADPH-dependent reductive carboxylation of pyruvate
7
7.8
Q6T5D1, Q9FRT2
pH 7.0: about 65% of maximal activity, pH 7.8: about 70% of maximal activity, recombinant NADP-ME2
7
8.2
-
broad range, 80% of maximal activity at pH 7.0 and pH 8.2
7
9
-
pH 7.0: about 60% of maximal activity, pH 9.0: about 55% of maximal activity
7.1
8.6
-
pH 7.1: about 65% of maximal activity, pH 8.6: about 75% of maximal activity, NADP+-dependent decarboxylation of malate, at 10 mM malate, mitochondrial enzyme and cytosolic enzyme
7.3
8.3
Q6T5D1, Q9FRT2
pH: about 65% of maximal activity, pH: about 65% of maximal activity, recombinant NADP-ME3
7.5
10.5
P76558
activity range, profile overview
7.5
9
-
pH 7.5: about 50% of maximal activity, pH 9.0: about 85% of maximal activity
additional information
-
-
pH profiles of wild-type and mutant enzymes, overview
additional information
-
-
enzyme conformation at different pH values, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
25
-
-
assay at, both reaction directions
25
-
Q717I9, -
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
Q9F3K4
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
46
-
P76558
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
55
P76558
activity range, profile overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
Q8W000
isozyme ZmChlMe2
5.1
-
-
isoelectric focusing
5.5
-
-
isoelectric focusing
5.9
-
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme1, sequence calculation
6
-
Q717I9, -
calculated
6
-
Q8W000
isozyme ZmChlMe1
6
-
-
isozyme 1, isoelectric focusing; isozyme 2, isoelectric focusing
6.5
-
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme3, sequence calculation
7.1
-
-
recombinant enzyme, isoelectric focusing
8.9
-
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme2, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Trypanosoma cruzi CL Brener
-
-
-
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
-
isozyme ZmC4-NADP-ME
Manually annotated by BRENDA team
-
only two isozymes present in the fermenter-grown or bottle-grown cultures
Manually annotated by BRENDA team
AF288898, AF288899
-
Manually annotated by BRENDA team
AF288900, AF288901, AF288902, Q93ZK8
-
Manually annotated by BRENDA team
AF288904, AF288905
-
Manually annotated by BRENDA team
AF288906, P93139
-
Manually annotated by BRENDA team
AF288911, P36444
-
Manually annotated by BRENDA team
AF288916, AF288917, Q8SAT3
-
Manually annotated by BRENDA team
-
NADP-ME4 is found in guard cells of cotyledonous leaves
Manually annotated by BRENDA team
-
hepatocytes and fibroblasts
Manually annotated by BRENDA team
-
activity is detected in the central vasculature of the siliques; activity is detected in the embryo at all developmental stages, including the seed attachment point and the integuments, NADP-ME4; at the globular and heart stage, detected in the funiculus and vascular tissue of the siliques, NADP-ME2; expression of NADP-ME1 from the torpedo stage onward
Manually annotated by BRENDA team
-
developing, maximal at stage 7 of endosperm development, overview
Manually annotated by BRENDA team
Trypanosoma cruzi CL Brener
-
-
-
Manually annotated by BRENDA team
-
sepals and filaments of developed flowers, NADP-ME2
Manually annotated by BRENDA team
-
isozyme F1 and F2
Manually annotated by BRENDA team
-, Q006P9, Q006Q0
;
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
-
insulinoma cells, high expression level of isozyme ME1
Manually annotated by BRENDA team
-
etiolated
Manually annotated by BRENDA team
Q8W000
young and mature green leaves, in sheath, tass, tip, and husk of the latter
Manually annotated by BRENDA team
AF288898, AF288899
-
Manually annotated by BRENDA team
AF288900, AF288901, AF288902, Q93ZK8
-
Manually annotated by BRENDA team
AF288904, AF288905
-
Manually annotated by BRENDA team
AF288906, P93139
-
Manually annotated by BRENDA team
AF288911, P36444
developing, expression pattern of the isozymes
Manually annotated by BRENDA team
AF288916, AF288917, Q8SAT3
-
Manually annotated by BRENDA team
P22178
developing, expression pattern of the isozymes
Manually annotated by BRENDA team
-
isozymes 1 and 2
Manually annotated by BRENDA team
-
expression of NADP-ME2 in all cell types, being particularly strong in the trichome basal cells and hydatodes; expression of NADP-ME3 is restricted to the trichomes and trichome basal cells of leaves and stems; NADP-ME4
Manually annotated by BRENDA team
-
isozymes L2, L3 and L4 in older leaves, isozyme L1/R in younger leaves and roots, cell saround the midrib, as well as stomatal, epidermal, and mesophyll cells
Manually annotated by BRENDA team
Q27IE1, Q6PMI1, Q6PMI2
; isozyme Hvme1 is upregulated in the C4 leaves during the light period; isozyme Hvme3 is equally active in C4 and C3 leaves
Manually annotated by BRENDA team
-, Q006P9, Q006Q0
;
Manually annotated by BRENDA team
A9LIN4, B8PUQ5
; isozyme NADP-ME1 is leaf-abundant
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
Triticum aestivum Jinmai 47
-
-
-
Manually annotated by BRENDA team
-
no activity
Manually annotated by BRENDA team
-
musculus rectus, musculus soleus
Manually annotated by BRENDA team
-
flight muscle
Manually annotated by BRENDA team
-
musculus psoas, musculus semitendinosus
Manually annotated by BRENDA team
-
musculus rectus, musculus soleus
Manually annotated by BRENDA team
seagull
-
musculus pectoralis
Manually annotated by BRENDA team
-
abdominal muscle
Manually annotated by BRENDA team
-
expression of NADP-ME3 exclusively in pollen from the latest maturation stage up to its germination on the stigma; NADP-ME4
Manually annotated by BRENDA team
-
isozyme NADP-ME3
Manually annotated by BRENDA team
Trypanosoma brucei 427, Trypanosoma brucei stock 427
-
-
-
Manually annotated by BRENDA team
Q8W000
only isozyme ZmChlMe2
Manually annotated by BRENDA team
-
only isozyme 1, not isozyme 2
Manually annotated by BRENDA team
-
expression of NADP-ME2 throughout all the tissues, except for root tips; stele, mainly at emerging lateral roots and at root tips, NADP-ME4
Manually annotated by BRENDA team
-
isozyme L1/R in younger leaves and roots
Manually annotated by BRENDA team
-, Q006P9, Q006Q0
;
Manually annotated by BRENDA team
-
isozyme NADP-ME1
Manually annotated by BRENDA team
A9LIN4, B8PUQ5
;
Manually annotated by BRENDA team
Q5G1U0
emerging root
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
-
NADP-ME1 expression only in some secondary roots, where it is confined to the stele and excluded from the tips
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
AF288898, AF288899
-
Manually annotated by BRENDA team
AF288900, AF288901, AF288902, Q93ZK8
-
Manually annotated by BRENDA team
AF288904, AF288905
-
Manually annotated by BRENDA team
AF288906, P93139
-
Manually annotated by BRENDA team
AF288911, P36444
-
Manually annotated by BRENDA team
AF288916, AF288917, Q8SAT3
-
Manually annotated by BRENDA team
-
NADP-ME2; NADP-ME4
Manually annotated by BRENDA team
-
in developing siliques, NADP-ME2 activity is found at both ends, the stigmatic papillae and the abscission zone. Detected in the funiculus and vascular tissue of the siliques, NADP-ME2
Manually annotated by BRENDA team
-
expression of NADP-ME3 is restricted to the trichomes and trichome basal cells of leaves and stems; NADP-ME4
Manually annotated by BRENDA team
-
isozymes S1 and S2
Manually annotated by BRENDA team
-, Q006P9, Q006Q0
;
Manually annotated by BRENDA team
A9LIN4, B8PUQ5
;
Manually annotated by BRENDA team
-
isozyme NADP-ME3
Manually annotated by BRENDA team
-
parenchymal cell vessel
Manually annotated by BRENDA team
additional information
-
NADP-ME2 activity is detected in all reproductive organs; NADP-ME4 is detected in all vegetative organs; no activity of NADP-ME1 is detectable in leaves and stems throughout growth, not expressed in floral organs
Manually annotated by BRENDA team
additional information
-
tissue-specific isozyme patterns, overview
Manually annotated by BRENDA team
additional information
-
NADP-ME2 and 4 are constitutively expressed, while NADP-ME1 is restricted to secondary roots and NADP-ME3 to trichomes and pollen
Manually annotated by BRENDA team
additional information
-
both cytosolic and mitochondrial isozymes are more abundant in the insect stage, although they can be immunodetected in the bloodstream forms; both isozymes appear to be clearly more abundant in the insect stage, although they can be immunodetected in the bloodstream forms
Manually annotated by BRENDA team
additional information
-
expression of the mitochondrial ME is upregulated in amastigotes, while the cytosolic isoform is more abundant in the insect stages of the parasite; the expression of the mitochondrial isozyme seems to be clearly upregulated in amastigotes, whereas the cytosolic isoform appears to be more abundant in the insect stages of the parasite
Manually annotated by BRENDA team
additional information
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
expression also in etiolated tissue
Manually annotated by BRENDA team
additional information
-
transcription levels of PtNADP-ME1 in lignified stems and roots are clearly higher than in other tissues, and PtNADP-ME2, PtNADP-ME3, PtNADP-ME4 and PtNADPME5 are broadly expressed in various tissues
Manually annotated by BRENDA team
additional information
Trypanosoma brucei 427, Trypanosoma brucei stock 427
-
both cytosolic and mitochondrial isozymes are more abundant in the insect stage, although they can be immunodetected in the bloodstream forms; both isozymes appear to be clearly more abundant in the insect stage, although they can be immunodetected in the bloodstream forms
-
Manually annotated by BRENDA team
additional information
Trypanosoma cruzi CL Brener
-
expression of the mitochondrial ME is upregulated in amastigotes, while the cytosolic isoform is more abundant in the insect stages of the parasite; the expression of the mitochondrial isozyme seems to be clearly upregulated in amastigotes, whereas the cytosolic isoform appears to be more abundant in the insect stages of the parasite
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
AF288898, AF288899
both isozymes
Manually annotated by BRENDA team
AF288900, AF288901, AF288902, Q93ZK8
both isozymes
Manually annotated by BRENDA team
AF288904, AF288905
both isozymes
Manually annotated by BRENDA team
AF288906, P93139
both isozymes
Manually annotated by BRENDA team
AF288911, P36444
both isozymes
Manually annotated by BRENDA team
AF288916, AF288917, Q8SAT3
both isozymes
Manually annotated by BRENDA team
P22178
both isozymes
Manually annotated by BRENDA team
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme1 possesses a putative transit peptide
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
-
from bundle sheath cells or mesophyll cells. In all the C4 species, the chloroplasts of bundle sheath cells in control plants show a typical structure of NADP-ME type whose thylakoids are scarcely appressed and grana are rudimentary, while in bundle sheath cell chloroplasts in the salt-treated plants, almost no structural damage is observed, overview
Manually annotated by BRENDA team
-
putative plastidic isozymes PtNADP-ME4 and PtNADP-ME5
Manually annotated by BRENDA team
-
isozymes ZmC4-NADP-ME and ZmnonC4-NADP-ME
Manually annotated by BRENDA team
Triticum aestivum Jinmai 47
-
-
-
Manually annotated by BRENDA team
-
2 distinct enzyme forms are present in cytosol and in mitochondria
Manually annotated by BRENDA team
-
represents about 1% of total cytosolic enzyme
Manually annotated by BRENDA team
Q717I9, -
exclusively in
Manually annotated by BRENDA team
Q6SZS7
cytoNADPME
Manually annotated by BRENDA team
Q27IE1, Q6PMI1, Q6PMI2
isozyme Hvme2; isozyme Hvme3
Manually annotated by BRENDA team
-, Q006P9, Q006Q0
-
Manually annotated by BRENDA team
-
isozymes NADP-ME1-3
Manually annotated by BRENDA team
-
both cytosolic and mitochondrial isozymes are more abundant in the insect stage, although they can be immunodetected in the bloodstream forms; cytosolic isozyme, appears to be clearly more abundant in the insect stage, although it can be immunodetected in the bloodstream form
Manually annotated by BRENDA team
-
cytosolic isozyme, the cytosolic isoform appears to be more abundant in the insect stages of the parasite; the cytosolic isoform is more abundant in the insect stages of the parasite
Manually annotated by BRENDA team
-
cytosolic malic enzyme ME1
Manually annotated by BRENDA team
Hieracium pilosella, Mnium undulatum, Polytrichum commune, Polytrichum piliferum
-
-
Manually annotated by BRENDA team
-
isozymes PtNADP-ME2 and PtNADPME3
Manually annotated by BRENDA team
-
NADP-malic enzyme 2
Manually annotated by BRENDA team
Trichomonas vaginalis TV 7-37
-
exclusively in
-
Manually annotated by BRENDA team
Trypanosoma brucei 427, Trypanosoma brucei stock 427
-
both cytosolic and mitochondrial isozymes are more abundant in the insect stage, although they can be immunodetected in the bloodstream forms; cytosolic isozyme, appears to be clearly more abundant in the insect stage, although it can be immunodetected in the bloodstream form
-
Manually annotated by BRENDA team
Trypanosoma cruzi CL Brener
-
cytosolic isozyme, the cytosolic isoform appears to be more abundant in the insect stages of the parasite; the cytosolic isoform is more abundant in the insect stages of the parasite
-
Manually annotated by BRENDA team
-
2 distinct enzyme forms are present in cytosol and in mitochondria
Manually annotated by BRENDA team
-
both cytosolic and mitochondrial isozymes are more abundant in the insect stage, although they can be immunodetected in the bloodstream forms; mitochondrial isozyme, appears to be clearly more abundant in the insect stage, although it can be immunodetected in the bloodstream form
Manually annotated by BRENDA team
-
expression of the mitochondrial ME is upregulated in amastigotes; mitochondrial isozyme, the expression of the mitochondrial isozyme seems to be clearly upregulated in amastigotes
Manually annotated by BRENDA team
-
mitochondrial malic enzyme ME3
Manually annotated by BRENDA team
Trypanosoma brucei 427, Trypanosoma brucei stock 427
-
both cytosolic and mitochondrial isozymes are more abundant in the insect stage, although they can be immunodetected in the bloodstream forms; mitochondrial isozyme, appears to be clearly more abundant in the insect stage, although it can be immunodetected in the bloodstream form
-
Manually annotated by BRENDA team
-
NADP-ME4 is localized to plastids
Manually annotated by BRENDA team
Trypanosoma cruzi CL Brener
-
expression of the mitochondrial ME is upregulated in amastigotes; mitochondrial isozyme, the expression of the mitochondrial isozyme seems to be clearly upregulated in amastigotes
-
Manually annotated by BRENDA team
additional information
-
the recombinant enzyme is imported into chloroplasts of Spinacia oleracea
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
64000
-
Q5G1U0
mature monomer of recombinant enzyme after enterokinase digestion, SDS-PAGE
65000
-
Q9LYG3, Q9XGZ0
SDS-PAGE; SDS-PAGE
68000
-
-
gel filtration
70000
-
-
monomeric flower isozyme, native PAGE
71600
-
Q5G1U0
calculated from amino acid sequence
80000
-
Q717I9, -
gel filtration
90000
-
-
sucrose density gradient centrifugation
105000
-
-
gel filtration
110000
-
-
recombinant dimeric enzyme, gel filtration at pH 7.0, minor peak
140000
-
-
dimeric flower isozyme, native PAGE
180000
-
-
gel filtration
216000
-
-
cytosolic enzyme, density gradient centrifugation
226000
-
-
recombinant tetrameric enzyme, gel filtration at pH 8.0, major peak
227000
-
-
mitochondrial enzyme, density gradient centrifugation
230000
240000
-
and a second molecular weight form of 460000-480000 Da, gel filtration
240000
-
-
recombinant isozyme NADP-ME2, gel filtration
243000
-
Q9LYG3, Q9XGZ0
gel filtration
248000
-
-
tetrameric isozymes from leaves, stem and roots, native PAGE, overview
249000
-
Q9LYG3, Q9XGZ0
gel filtration
254000
-
-
gel filtration
257000
-
-
gel filtration
258000
-
-
gel filtration
260000
265000
-
gel filtration
260000
-
-, Q006P9, Q006Q0
native PAGE; native PAGE
264000
-
-
isozyme 2, gel filtration
280000
-
-
tetrameric isozymes from flower, leaves, and stem, native PAGE, overview
285000
-
-
gel filtration
460000
480000
-
and a second molecular weight form of 230000-240000 Da, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 82000, SDS-PAGE
?
-
x * 72000, SDS-PAGE
?
-
x * 62000, SDS-PAGE
?
-
x * 67000, SDS-PAGE
?
-
x * 64000, SDS-PAGE
?
-
x * 72000, SDS-PAGE
?
-
x * 62000, SDS-PAGE
?
Q8W000
x * 62000, isozyme ZmChlMe1, x * 72000, isozyme ZmChlMe2
?
-
x * 72000, isozyme 1, SDS-PAGE
?
-
x * 62000-66000, recombinant chimeric enzymes, SDS-PAGE
?
-
x * 65000, SDS-PAGE
?
P76558
x * 83000, SDS-PAGE
?
Escherichia coli MG1655
-
x * 83000, SDS-PAGE
-
dimer
-
2 * 42000, SDS-PAGE
dimer
Q717I9, -
2 * 42500, SDS-PAGE
dimer
-
2 * 49000, SDS-PAGE
dimer
-
2 * 70000, SDS-PAGE
dimer
-
2 * 72000, SDS-PAGE
dimer
-
2 * 61300, about, DNA sequence calculation
dimer
-
the dimeric form of c-NADP-ME is as active as tetramers, analytical ultracentrifugation
dimer
Trichomonas vaginalis TV 7-37
-
2 * 42500, SDS-PAGE
-
hexamer or octamer
Q5G1U0
-
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 72000, SDS-PAGE
oligomer
-
x * 62000, detagged recombinant wild-type enzyme
oligomer
-
the cytosolic PtNADP-ME2 aggregates as octamers and hexadecamers while the plastidic PtNADP-ME4 resembles hexamers and octamers. Different PtNADP-ME family members present different oligomeric states in vitro
tetramer
-
4 * 64900, SDS-PAGE
tetramer
-
4 * 64000, SDS-PAGE
tetramer
-
4 * 64000-65000, SDS-PAGE
tetramer
-
4 * 63000, SDS-PAGE
tetramer
-
4 * 65000, SDS-PAGE
tetramer
-
4 * 72000, SDS-PAGE
tetramer
-
4 * 63000, approximately, SDS-PAGE
tetramer
-
4 * 62000, SDS-PAGE
tetramer
-
4 * 72000, isozyme 2, SDS-PAGE
tetramer
-
subunit structure and organisation, crystal structure
tetramer
-
structure analysis from crystal structure, the enzyme is a tetrameric protein with double dimer quaternary structure, pH dependence of enzyme structure, overview
tetramer
-
4 * 62000, tissue specific isozymes, SDS-PAGE, 4 * 70000, tissue specific isozymes, SDS-PAGE
tetramer
-
4 * 72000, SDS-PAGE
tetramer
-
4 * 61300, about, DNA sequence calculation
tetramer
Q27IE1, Q6PMI1, Q6PMI2
4 * 64000, about, isozyme Hvme3, sequence calculation; 4 * 68000, about, isozyme Hvme2, sequence calculation; 4 * 72000, about, isozyme Hvme1, sequence calculation
tetramer
-, Q006P9, Q006Q0
4 * 63000, plastidic isozyme, SDS-PAGE; 4 * 65000, cytosolic isozyme, SDS-PAGE
tetramer
-
4 * 62000, recombinant mature isozyme NADP-ME2, SDS-PAGE
tetramer
-
c-NADP-ME exists mainly as a tetramer, analytical ultracentrifugation
tetramer
-
4 * 64000, SDS-PAGE
tetramer
-
recombinant ZmC4-NADP-ME wild-type and mutants
tetramer
-
c-NADP-ME has a dimer-dimer quaternary structure in which the dimer interface associates more tightly than the tetramer interface
tetramer
Trypanosoma brucei 427, Trypanosoma brucei stock 427, Trypanosoma cruzi CL Brener
-
-
-
monomer
-
1 * 61300, about, DNA sequence calculation
additional information
-
extent of oligomerization is pH-dependent, 3D-structure analysis
additional information
-
circular dichroism structure analysis of wild-type and mutant enzymes, overview
additional information
-
at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, aggregation of the enzyme is attributable to the Trp572 side chain, overview
additional information
-
the enzyme exists in several different oligomeric states depending on the metabolite concentrations, light status, ionic strength as well as pH, conformational changes of guanidine hydrochloride-denatured NADP-malic enzyme studied by quenching of protein native fluorescence with KI and acrylamide, overview
additional information
-
MaeB possesses a multimodular structure, it is composed of two distinct domains, MWs of the different isozymes, overview
additional information
-
the enzyme is first dissociated from a tetramer to dimers before the 2 M urea treatment, and the dimers then dissociated into monomers before the 2.5 M urea treatment
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
10 mg/ml purified enzyme in quarternary complex with NADP+, Mn2+, and oxalate, closed enzyme form, hanging drop vapour diffusion method, 4C, from 20 mM Tris, pH 7.4, 10 mM oxalate, 5 mM MnCl2, 0.23 mM NADP+, and 2 mM DTT, with a reservoir solution containing 100 mM sodium citrate, pH 5.5, 8% PEG 6000, and 1 M LiCl, 3-4 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, atomic model
-
recombinant His-tagged cytosolic and mitochondrial isozymes from Escherichia coli by nickel affinity chromatography
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
stable for 24 h
7.5
-
Q9LYG3, Q9XGZ0
at pH 7.5 isoenzyme NADP-ME2 retains 95% of the maximal activity; at pH 7.5 isoenzyme NADP-ME3 retains 95% of the maximal activity
8
-
-
stable for at least one month
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
stable for at least 120 min
30
-
-
completely stable for at least 20 min
33
-
-
120 min, 24% loss of activity
40
-
-
120 min, 70% loss of activity
44
-
-
stable for at least 10 min
50
-
-
15 min, pH 8.0, irreversible thermal inactivation
52
64
-
thermal denaturation of c-NADP-ME wild-type and the interface mutants, overview
60
-
-
stable for at least 24 h
60
-
-
12 h, in absence of solvent, stable
75
-
-
stable for at least 12 h
80
-
-
stable for at least 7 h
85
-
-
stable for at least 5 h
additional information
-
Pigeon
-
malic acid decreases heat stability at pH values above 5.0; Mg2+ or Mn2+ increase heat stability
additional information
-
-
Mg2+ does not influence the thermal stability of the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
malic acid decreases heat stability at pH values above 5.0
Pigeon
-
Mg2+ or Mn2+ increase heat stability
Pigeon
-
loss of activity upon repeated freezing and thawing
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimethylformamide
-
25C, after a 24-h incubation in 50% dimethylformamide, the enzyme is completely active
dimethylformamide
Sulfolobus solfataricus MT-4
-
25C, after a 24-h incubation in 50% dimethylformamide, the enzyme is completely active
-
Ethanol
-
15%, 25C, 24 h, 15% loss of activity. Half-life is 8 h in 50% ethanol
Ethanol
Sulfolobus solfataricus MT-4
-
15%, 25C, 24 h, 15% loss of activity. Half-life is 8 h in 50% ethanol
-
guanidine-HCl
-
25C, half-life is 30 min in 6 M guanidine hydrochloride
Methanol
-
50%, 25C, 24 h, 15% loss of activity. Half-life of 50% methanol is 16 h at 45C and 3 min at 60C
Methanol
Sulfolobus solfataricus MT-4
-
50%, 25C, 24 h, 15% loss of activity. Half-life of 50% methanol is 16 h at 45C and 3 min at 60C
-
SDS
-
25C, the enzyme is not inactivated in 0.05% SDS over 24 h. Half-life is 5 h in 0.075% SDS
SDS
Sulfolobus solfataricus MT-4
-
25C, the enzyme is not inactivated in 0.05% SDS over 24 h. Half-life is 5 h in 0.075% SDS
-
tetrahydrofuran
-
half-life is 30 min in 50% tetrahydrofuran
urea
-
25C, the enzyme is not inactivated in 4 M urea over 24 h. Half-life is 10 h in 7.5 M urea
urea
Sulfolobus solfataricus MT-4
-
25C, the enzyme is not inactivated in 4 M urea over 24 h. Half-life is 10 h in 7.5 M urea
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
during the storage of the whole cells at -20C, isozyme E is gradually converted to isozyme G
-
-20C, stable for several weeks
-
4C, loss of activity upon prolonged storage
-
25C, pH 8.0, stable for at least one month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isozyme 2, partially from leaves, 513fold
-
native enzyme by anion exchange and affinity chromatography
-
recombinant mutant enzymes
-
recombinant enzyme from Escherichia coli by pecipitation with streptomycin sulfate, DEAE ion exchange, affinity and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 by anion exchange chromatography and 2',5'-ADP affinity chromatography to over 95% purity
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
P76558
recombinant His-tagged MaeB from strain BL21(DE3) by nickel affinity chromatography
-
Ni-NTA-Sepharose column chromatography
-
nickel affinity gel column chromatography
-
recombinant ME1 2229fold from INS-1 832/13 cell cytosolic fractions by 2',5'-ADP affinity chromatography
-
recombinant His-tagged isozyme Hvme1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, native enzyme partially by chloroplast isolation; recombinant His-tagged isozyme Hvme3 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Q27IE1, Q6PMI1, Q6PMI2
separation of isozymes in native PAGE
-
recombinant fusion protein; recombinant fusion protein
Q6T5D1, Q9FRT2
-
Pigeon
-
recombinant isozymes PtNADP-ME1, PtNADP-ME2, PtNADP-ME3, PtNADP-ME4, and PtNADPME5 from Escherichia coli by glutathione affinity chromatography
-
5160fold from oil seed
-
2 distinct enzyme forms
-
331fold to homogeneity by a 4-step chromatographical procedure
Q717I9, -
recombinant His-tagged isozymes ME1 and ME2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged cytosolic and mitochondrial isozymes from Escherichia coli by nickel affinity chromatography; recombinant His-tagged isozymes ME1 and ME2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Ni-NTA column chromatography
Q5G1U0
recombinant His-tagged chimeric NADP-ME mutants from Escherichia coli strain BL21(DE3) by two different steps of affinity chromatography to homogeneity
-
recombinant His-tagged mutant enzyme to homogeneity from Escherichia coli by metal affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) to homogeneity
-
recombinant wild-type and mutants from Escherichia coli to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli TH-2 cells as a fusion protein including a 15-residue N-terminal leader from beta-galactosidase coded by the lacZ gene
-
expression in Escherichia coli, NADP-ME1; expression in Escherichia coli, NADP-ME2; expression in Escherichia coli, NADP-ME3; expression in Escherichia coli, NADP-ME4
-
expression of isozyme NADP-ME2 in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant isozymes NADP-ME2 in Escherichia coli
-
genes NADP-ME1, NADP-ME2, and NADP-ME3, quantitative RT-PCR expression analysis
-
NADP-MDH gene, cDNA library screening, promoter analysis and DNA and amino acid sequence determination and analysis, genetic structure and sequence comparison with Brassicaceae plant sequences, overview, expression oof NADP-MDH-HIS3 fusion genes in the yeast two-hybrid system, Saccharomyces cerevisiae strain YM4271, identifying interaction with DNA binding proteins, overview
Q8H1E2
mutant enzymes expressed in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
overexpression in Escherichia coli
-
co-expression in strain W3110 with 5-aminolevulinate synthase, EC 2.3.1.37, from Rhodobacter sphaeroides, hemA gene, for reconstruction of the 5-aminolevulinic acid biosynthesis, subcloning in strain DH5alpha, increased C4 metabolism via NADP-dependent malic enzyme expression results in increased 5-aminolevulinate production by 5-aminolevulinate synthase in Escherichia coli
-
gene maeB, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
P76558
gene maeB, overexpression in wild-type strain W3110, and in strains deficient for pyruvate formate lyase, lactate dehydrogenase, and glucose phosphotransferase, overview
-
subcloning in strain K-12, expression of the His-tagged enzyme in strain BL21(DE3)
-
3'-UTR region, cloning, sequencing, and analysis
Q8SAT4
3'-UTR region, cloning, sequencing, and analysis
AF288906, P93139
3'-UTR region, cloning, sequencing, and analysis
P22178
expressed in Escherichia coli BL21 (DE3) cells
-
functional expression of ME1, under the control of cytomegalovirus, which also directs the transcription of GFP from an internal ribosome entry site, in Rattus norvegicus INS-1 832/13 cells and in Mus musculus islets
-
gene hvme1, DNA and amino acid sequence determintion and analysis, isozyme expression analysis, hvme1 promoter analysis, expression of His-tagged isozyme Hvme1 in Escherichia coli strain BL21(DE3); gene hvme2, DNA and amino acid sequence determintion and analysis, isozyme expression analysis, hvme1 promoter analysis; gene hvme3, DNA and amino acid sequence determintion and analysis, isozyme expression analysis, expression of His-tagged isozyme Hvme3 in Escherichia coli strain BL21(DE3)
Q27IE1, Q6PMI1, Q6PMI2
gene malE, DNA and amino acid sequence determination and analysis, genomic library construction, screening, and functional enzyme expression in Escherichia coli
A6XP71
gene malE, DNA and amino acid sequence determination and analysis, genomic library construction, screening, and functional enzyme expression in Escherichia coli
A6XP72
ME gene, DNA and amino acid sequence determination and analysis, recombinant enzyme expression of the enzyme in Rhodotorula glutinis strain GM4 using the PGK1 promoter, a strong constitutive promoter of yeast PGK1 gene, co-expression with the PGK1 gene from Saccharomyces cerevisiae
A6XP72
isozyme NADP-ME2, expression in Escherichia coli; nadp-me1, expression in Escherichia coli
-, Q006P9, Q006Q0
expression in Arabidopsis thaliana under control of the 35S promoter
Q6SZS7
expression of a glutathione S-transferase fusion proteins NADP-ME2 in Escherichia coli; expression of a glutathione S-transferase fusion proteins NADP-ME3 in Escherichia coli
Q6T5D1, Q9FRT2
isozyme NADP-ME2, DNA and amino acid sequence determination and analysis by screening of a root cDNA library, expressionin transgenic Arabidopsis thaliana plants using Agrobacterium tumefaciens strain EHA105-mediated transformation
Q9FRT2
five NADP-ME genes PtNADP-ME1, PtNADP-ME2, PtNADP-ME3, PtNADP-ME4, and PtNADPME5, DNA and amino acid sequence determination and analysis, phylogenetic analysis, individual expression of GST-tagged isozymes in Escherichia coli
-
isozymes expression analysis, overview
-
ME1 and ME3, quantitative real time PCR expression analysis
-
gene tme, subcloning in Escherichia coli, expression in bacteroids deficient for the NAD+-dependent malic enzyme encoded by gene dme, EC 1.1.1.39
-
gene Sco5261, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expressionin Escherichia coli strain BL21(DE3)
Q9F3K4
preparation of a genomic library, DNA and amino acid sequence determination and analysis, detailed phylogenetic reconstruction of malic enzymes, overview
Q717I9, -
DNA and amino acid sequence determination and analysis
B8PUQ5
cytosolic and mitochondrial isozymes, expression in of His-tagged isozymes ME1 and ME2 Escherichia coli Rosetta (DE3)pLysS; expression of His-tagged isozymes ME1 and ME2 in Escherichia coli strain BL21(DE3)
-
cytosolic and mitochondrial isozymes, expression of His-tagged ME2 in Escherichia coli Rosetta (DE3)pLysS and of His-tagged ME1 in Escherichia coli BL(DE3); expression of His-tagged isozymes ME1 and ME2 in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21 (DE3) cells
Q5G1U0
expression in Escherichia coli
-
expression in tobacco plants via infection with Agrobacterium tumefaciens
-
expression of His-tagged chimeric NADP-ME mutants in Escherichia coli strain BL21(DE3)
-
expression of the maize enzyme in Arabidopsis thaliana under control of the cauliflower mosaic virus 35S promoter
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutants in Escherichia coli BL21(DE3)
-
isozyme DNA and amino acid sequence determination and analysis, phylogenetic analysis, overview
Q8W000
overexpression of His-tagged wild-type and mutants in Escherichia coli strain DH5alpha, functional complementation of the enzyme deficient Escherichia coli triple mutant strain EJ1321
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
significant decrease of PtNADP-ME2 and PtNADP-ME3 in mRNA levels, but only a slight change in other PtNADP-ME genes, during the dark
-
NaCl salt stress upregulates the transcripts of putative plastidic isozymes PtNADP-ME4 and PtNADP-ME5 significantly. Expression of PtNADP-ME2 and PtNADP-ME3 increases during the course of leaf wounding, PtNADP-ME3 transcript levels peak at 6 h under NaCl and mannitol stresses. Expression of PtNADP-ME1 gene is induced slightly by mannitol and PEG osmotic stresses, but not by salt stress
-
abscisic acid and PEG reduce enzyme expression, under cold condition the enzyme expression is sligtly reduced
B8PUQ5
darkness does not affect enzyme expression in leves, no effect by salicylic acid or by salt stress
B8PUQ5
abscisic acid and PEG reduce enzyme expression, under cold condition the enzyme expression is sligtly reduced
Triticum aestivum Jinmai 47
-
-
darkness does not affect enzyme expression in leves, no effect by salicylic acid or by salt stress
Triticum aestivum Jinmai 47
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C99S
-
turnover number decreases 3fold and Km for malate increases 4fold
R115A
-
site-directed mutagenesis, mutation of isozyme NADP-ME2, the mutant shows similar kinetics as the wild-type isozyme NADP-ME2, but loses the activation ability of fumarate
R115A
-
site-directed mutagenesis of isozyme NADP-ME2, the mutant displays a marked inhibition in the presence of all the organic acids tested, also fumarate
D235A
-
turnover number is 783.5fold lower than wild-type value
D257A
-
turnover number is 28.5fold lower than wild-type value
D258A
-
turnover number is 522fold lower than wild-type value
E234A
-
turnover number is 1.3fold higher than wild-type value
K162A
-
site-directed mutagenesis, the mutation does not affect Mn2+ binding of the mutant enzyme, but kcat is 27000fold reduced compared to the wild-type enzyme, NH4Cl shows no rescue of the pyruvate reduction in the K162A mutant, while for oxaloacetate decarboxylation, ammonium chloride demonstrated a maximum restoration of 3.5fold at 1 mM, and its rescue efficiency decreases with increasing concentration
K162Q
-
site-directed mutagenesis, the mutation does not affect Mn2+ binding of the mutant enzyme, but kcat is 3500fold reduced compared to the wild-type enzyme
K162R
-
site-directed mutagenesis,the mutation does not affect Mn2+ binding of the mutant enzyme, but kcat is 125fold reduced compared to the wild-type enzyme
K362A
-
site-directed mutagenesis, 70fold increased Km for NADP+ compared to the wild-type enzyme
W252A
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252F
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252H
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252I
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252S
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
D139A
-
dimeric mutant enzyme with reduced activity compared to the wild type enzyme
D568A
-
dimeric or tetrameric mutant enzyme with increased activity compared to the wild type enzyme
D90A
-
dimeric or tetrameric mutant enzyme with reduced activity compared to the wild type enzyme
E314A
-
site-directed mutagenesis
E314A/S346I/K347D/K362H
-
site-directed mutagenesis, the quadruple mutant enzyme is a mainly NAD+-utilizing enzyme by a considerable increase in catalysis using NAD+ as the cofactor, shows increased inibition by ATP compared to the wild-type enzyme
E314A/S346K
-
site-directed mutagenesis
E314A/S346K/K347Y/K362H
-
site-directed mutagenesis, the quadruple mutant enzyme is a mainly NAD+-utilizing enzyme by a considerable increase in catalysis using NAD+ as the cofactor, shows increased inibition by ATP compared to the wild-type enzyme
E314A/S346K/K347Y/K362Q
-
site-directed mutagenesis, the quadruple mutant enzyme is a mainly NAD+-utilizing enzyme by a considerable increase in catalysis using NAD+ as the cofactor, shows increased inibition by ATP compared to the wild-type enzyme
H142A
-
dimeric mutant enzyme with increased activity compared to the wild type enzyme
H142A
-
site-directed mutagenesis, a dimeric tetramer interface mutant
H142A/D568A
-
dimeric mutant enzyme with reduced activity compared to the wild type enzyme
H142A/D568A
-
site-directed mutagenesis, a dimeric tetramer interface mutant. The mutant dimer completely dissociates into monomers after a 2.5 M urea treatment
H51A
-
dimeric or tetrameric mutant enzyme with wild type activity
H51A/D139A
-
dimeric or tetrameric mutant enzyme with reduced activity compared to the wild type enzyme
H51A/D139A
-
site-directed mutagenesis, a dimeric dimer interface mutant
H51A/D90A
-
dimeric or tetrameric mutant enzyme with reduced activity compared to the wild type enzyme
H51A/D90A
-
site-directed mutagenesis, a dimeric dimer interface mutant. The mutant dimer completely dissociates into monomers after a 1.5 M urea treatment
K347Y
-
site-directed mutagenesis, the mutant enzyme shows a 5fold increased Km for NADP+ compared to the wild-type enzyme
K347Y/K362Q
-
site-directed mutagenesis
K362H
-
site-directed mutagenesis
S346I/K347D/K362H
-
site-directed mutagenesis, the triple c-NADP-ME mutant does not show significant reduction in its Km,NAD values. This mutant exclusively utilizes NAD+ as its cofactor
S346K
-
site-directed mutagenesis, site-directed mutagenesis, the mutant enzyme shows a 3fold increased Km for NADP+ compared to the wild-type enzyme
S346K/K347Y
-
site-directed mutagenesis, the double mutant enzyme shows a 30fold increased Km for NADP+ compared to the wild-type enzyme
S346K/K347Y/K362H
-
site-directed mutagenesis, the triple c-NADP-ME mutant does not show significant reduction in its Km,NAD values, but displays an enhanced value for kcat,NAD
S346K/K347Y/K362Q
-
site-directed mutagenesis, the triple c-NADP-ME mutant does not show significant reduction in its Km,NAD values
S346K/K362Q
-
site-directed mutagenesis
W572A
-
dimeric mutant enzyme with slightly reduced activity compared to the wild type enzyme
A387G
-
site directed mutagenesis, mutation at the NADP+ binding site, mutant shows 48fold decreased kcat and 4.3 and 5.8fold increased Km for NADP+ and L-malate, respectively, compared to the wild-type enzyme, no activity with NAD+
A392G
-
site directed mutagenesis, mutation at the NADP+ binding site, mutant shows unaltered kcat, but 3.5 and 2.6fold increased Km for NADP+ and L-malate, respectively, and increased activity with NAD+ compared to the wild-type enzyme
C192A
-
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Unlike wild-type, activity is not significantly changed in presence of oxidant iodosobenzoate; site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, the mutant displays lower malate affinity than the wild-type enzyme
C231A
-
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Similar to wild-type, activity decreases in presence of oxidant iodosobenzoate; site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, the mutant displays lower malate affinity than the wild-type enzyme
C246A
-
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Unlike wild-type, activity is not significantly changed in presence of oxidant iodosobenzoate; site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, C246A exhibits a nearly 5fold increase in its affinity towards NADP+ and a 3fold decrease for malate compared to the wild-tpe enzyme
C270A
-
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Unlike wild-type, activity is not significantly changed in presence of oxidant iodosobenzoate; site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, the mutant displays lower malate affinity than the wild-type enzyme
K225I
-
site-directed mutagenesis, mutation of a conserved residue involved in catalysis and substrate binding, mutant shows highly reduced activity and a 10fold higher partitioning ratio of oxaloacetate and malate compared to the wild-type enzyme, preference for reduction of oxaloacetate instead of decarboxylation
R237L
-
site-directed mutagenesis, mutation of a conserved residue involved in catalysis and substrate binding, mutant shows and an over 100fold higher partitioning ratio of oxaloacetate and malate compared to the wild-type enzyme, preference for reduction of oxaloacetate instead of decarboxylation
R237L
-
site directed mutagenesis, mutation at the NADP+ binding site, mutant shows 530fold decreased kcat and 36.3 and 15.3fold increased Km for NADP+ and L-malate, respectively, compared to the wild-type enzyme, no activity with NAD+
R70Q
-
kinetic parameters are similar except for a slightly lower turnover number and higher Km for L-malate
additional information
Q8H1E2
expression of NADP-MDH is not affected in knock-out plants, knock-out mutant lines At5g58340::tDNA-1, SALK_053119, and At5g58340::tDNA-2, SALK_018118, carrying a DNA insert in the 5' region
additional information
-
construction of deletion mutants of isozyme NADP-ME2
additional information
-
generation of knock-out mutants nadp-me2.1 and -2.2 by Agrobacterium tumefaciens strain GV3101-mediated transformation using the vacuum infiltration method
Y91F
-
site-directed mutagenesis, the mutation does not affect Mn2+ binding of the mutant enzyme, the mutant shows a 25fold increase and a 3fold decrease in the Km values for (S)-malate and NADP+ respectively, and its kcat value is decreased by 200fold compared to wild-type enzyme
additional information
-
effects of enzyme overexpression on the concentration of CO2 and the C4 metabolsim in wild-type strain and strains overexpressing other anaeplerotic enzymes, phenotypes, overview
additional information
P76558
deletion of gene maeB by chromosomal homologous recombination
additional information
Escherichia coli MG1655
-
deletion of gene maeB by chromosomal homologous recombination
-
additional information
AF288898, AF288899
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression pattern and regulation, overview; construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression patterns and regulation, overview
additional information
-
generation of an antisense construct targeting the C4 isoform of NADP-malic enzyme, transformation of Flaveria bidentis via Agrobacterium tumefaciens, transgenic Flaveria bidentis plants exhibit a 34% to 75% reduction in NADP-ME activity relative to the wild-type with no visible growth phenotype. In transgenic plants, CO2 assimilation rates at high intercellular CO2 are significantly reduced, whereas the in vitro activities of both phosphoenolpyruvate carboxylase and Rubisco are increased
additional information
AF288911, P36444
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs bearing parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei; construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
P22178
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
K362Q
-
site-directed mutagenesis, the mutant enzyme displays a significant, over 140fold elevation in Km,NADP value compared with that of wild-type c-NADP-ME but no significant changes in the kcat,NADP value
additional information
-
ME1 overexpression results in an increased glucose-dependent rise in malate and citrate levels in INS-1 832/13 cells. Introduction of ME1 activity alters glucose-stimulated insulin secretion to a lesser degree in mouse islets than in INS-1 832/13 cells, overview. In contrast to rat, mouse beta-cells lack ME1 activity, which is suggested to explain their lack of methyl succinate-stimulated insulin secretion. Metabolic phenotypes of transfected cells, overview
additional information
-
a series of E314A-containing c-NADP-ME quadruple mutants are changed to NAD+-utilizing enzymes by abrogating NADP+ binding and increasing NAD+ binding. Abolishing the repulsive effect of Glu314 in the quadruple mutants increases the binding affinity of NAD+
W572A
-
site-directed mutagenesis, a dimeric tetramer interface mutant
additional information
A6XP72
expression of the enzyme from Mucor circinelloides as a strategy to improve lipid content inside the Rhodotorula glutinis yeast cells, overview. Heterologous expression of NADP+-dependent ME involved in fatty acid biosynthesis increases the lipid accumulation in the oleaginous yeast Rhodotorula glutinis
additional information
-
construction of transgenic tobacco plants by expression of the maize enzyme, recombinant expression leads to plants with altered malate metabolism in guard cells and stomatal function which are more drought tolerant than the wild-type tobacco, overview
additional information
Q6SZS7
transgenic Arabidopsis thaliana plants overexpressing rice cytosolic NADP-ME have a greater salt tolerance at the seedling stage than wild-type plants in MS medium-supplemented with different levels of NaCl, no obvious morphological or developmental differences between the transgenic and wild-type plants
additional information
Q9FRT2
overexpression of rice isozyme NADP-ME2 in Arabidopsis thaliana enhances tolerance to salt and osmotic stresses in transgenic seedlings, overview
moe
-
enzyme inactivation by shRNA, ME1 activity is reduced by 62% and glucose-induced insulin secretion is decreased
additional information
-
siRNA knockdown of cytosolic ME1 by 89% of mRNA expression and enzyme activity significantly reduces glucose and decreases the flux of both pools of pyruvate through pyruvate carboxylase affecting the anaplerotic pathways, insulin secretion in response to membrane depolarization using potassium chloride is unaffected by siRNA knockdown of malic enzyme, overview
additional information
-
siRNA knockout of ME1 in INS-1 832/13 beta-cells, siRNA knockdown and isotopic labeling strategies, method optimization, overview
additional information
-
the tme gene is placed under the control of the dme promoter, and despite elevated levels of TME within bacteroids, no symbiotic nitrogen fixation occurred in dme mutant strains, the dme mutant cells fail to fix N2 in alfalfa root nodules, overview, no TME in the tme mutant RmG994
K435L/K436L
-
site-directed mutagenesis, mutation of residues which are important in cofactor binding, over 6fold increased Ki for 2'-AMP, and 1.7fold decreased Ki for 5'-AMP, and increased activity with NAD+ compared to the wild-type enzyme
additional information
-
construction of the Gsite5V and Gsite2V mutants, mutation at the NADP+ binding site
additional information
-
construction of transgenic tobacco plants by expression of the maize enzyme, recombinant expression leads to plants with altered malate metabolism in guard cells and stomatal function which are more drought tolerant than the wild-type tobacco
additional information
-
construction of chimerical NADP-ME sequences obtained from C4 and non-C4 isozymes
additional information
-
transgenic Arabidopsis thaliana plants overexpressing the maize C4 NADP-malic enzyme show 6-33fold increase enzyme activity and a more rapid progression of dark-induced senescence compared to the wild type plants, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
presence of 2 mM diamide leads to a time-dependent decrease in activity, reaching about 40% of initial activity after 60 min. After addition of dithiothreitol, a complete recovery is observed after 90 min
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
squential fluorometric quantification of malic acid enantiomers in a single line flow-injection system using immobilized-enzyme reactors. An immobilized D -malate dehydrogenase (EC 1.1.1.83) reactor and an immobilized L-malate dehydrogenase (EC 1.1.1.40) reactor are introduced into the flowline in series. Sample and coenzyme (NAD+ or NADP+) are injected into the flow line by an open sandwich method. D -Malate is selectively oxidized by EC 1.1.1.83 when NAD+ is injected with a sample. When NADP+ is injected with a sample, L -malate is oxidized only by 1.1.1.40. NADH or NADPH produced by the immobilized-enzyme reactors is monitored fluorometrically at 455 nm