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

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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
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
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
C4 photosynthetic carbon assimilation cycle, NADP-ME type
-
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
-
gluconeogenesis I
-
-
C4 and CAM-carbon fixation
-
-
gluconeogenesis
-
-
photosynthesis
-
-
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
COMMENTARY
LITERATURE
C4 NADP-malic enzyme
-
-
C4 photosynthetic NADP-malic enzyme
-
-
C4-NADP-malic enzyme
-
-
C4-NADP-ME
isoform involved in C4 photosynthesis
ChlME1
AF288899
-
ChlME1
AF288900
-
ChlME1
AF288904
-
ChlME1
AF288906
-
ChlME1
AF288911
-
ChlME2
AF288899
-
ChlME2
AF288900
-
ChlME2
AF288904
-
ChlME2
AF288906
-
ChlME2
AF288911
-
cytoNADPME
-
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)
-
MaeB
-
-
MaeB
Escherichia coli MG1655
-
-
malate dehydrogenase (decarboxylating, NADP)
-
-
-
-
malate dehydrogenase (NADP, decarboxylating)
-
-
-
-
malic enzyme
-
-
-
-
malic enzyme
-
-
malic enzyme
Aspergillus niger NRRL 2270
-
-
-
malic enzyme
-
-
malic enzyme
-
-
malic enzyme
Mnium undulatum
-
-
malic enzyme
-
-
malic enzyme
-
-
malic enzyme
-
-
malic enzyme
Sulfolobus solfataricus MT-4
-
-
-
malic enzyme
Trichomonas vaginalis TV 7-37
-
-
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
-
malic enzyme-NADP
Streptomyces coelicolor M145
-
-
ME-NADP
Streptomyces coelicolor M145
-
-
NAD(P)+-malic enzyme
-
-
NADP dependent malic enzyme
-
NADP malic enzyme
-
-
NADP+ dependent malic enzyme
-
-
-
-
NADP+-dependent malic enzyme
-
-
NADP+-dependent malic enzyme
-
NADP+-dependent malic enzyme
-
-
NADP+-dependent malic enzyme
-
-
NADP+-dependent malic enzyme 3
-
-
NADP+-ME
-
-
NADP-dependent malate dehydrogenase
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
-
NADP-dependent malic enzyme
Escherichia coli MG1655
-
-
NADP-dependent malic enzyme
-
-
NADP-dependent malic enzyme
-
NADP-dependent malic enzyme
-
NADP-dependent malic enzyme
Triticum aestivum Jinmai 47
-
-
NADP-dependent malic enzyme
-
NADP-linked decarboxylating malic enzyme
-
-
-
-
NADP-malic enzyme
-
-
-
-
NADP-malic enzyme
-
-
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
-
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
-
NADP-malic enzyme
-
NADP-malic enzyme
-
-
NADP-malic enzyme
Mnium undulatum
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
NADP-malic enzyme
-
NADP-malic enzyme
-
NADP-malic enzyme
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
-
NADP-malic enzyme
-
NADP-malic enzyme 2
-
-
NADP-ME
-
-
-
-
NADP-ME
-
-
NADP-ME
AF288899
-
NADP-ME
AF288900
-
NADP-ME
AF288904
-
NADP-ME
AF288906
-
NADP-ME
AF288911
-
NADP-ME
Mnium undulatum
-
-
NADP-ME
-
-
NADP-ME
-
-
NADP-ME
-
-
NADP-ME
Triticum aestivum Jinmai 47
-
-
NADP-ME
-
NADP-ME
-
NADP-ME1
-
-
NADP-ME1
isozyme
NADP-ME2
isozyme
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
UNIPROT
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
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
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
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
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
-
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
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
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
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
-
-
-
(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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
?
(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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
?
(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
-
-
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
-
-
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
-
-
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
-
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
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
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
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
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 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
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Trichomonas vaginalis TV 7-37
responsible for pyruvate and NADPH production
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
show the reaction diagram
Escherichia coli MG1655
-
-
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
-
-
r
(S)-malate + NADP+
?
show the reaction diagram
-
-
-
?
(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
-
-
-
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
?
-
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
?
-
regulation and physiological roles of the isozymes
-
-
-
additional information
?
-
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
?
-
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
?
-
-
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
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
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
-
-
-
?
(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
-
-
-
?
(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
-
-
-
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
?
-
-
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
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+
-
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+
absolute specific for
NADP+
-
binding site structure, Arg237 is important for cofactor binding and specificity
NADP+
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+
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+
-
-
NADP+
-
important role of Asp-351, Asp-350 and Glu-327 in the binding of Mg2+ and NADP+
NADP+
-
specific for
NADP+
-
no activity with NAD+
NADP+
-
preferred cofactor
NADP+
-
the enzyme is strictly NADP+-dependent
NADP+
dependent on
NADP+
-
dependent on
NADP+
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
-
cofactor
NADPH
-
specific for
NADPH
-
-
NADPH
-
dependent on
additional information
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
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+
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+
required
Mg2+
-
activates
Mg2+
-
required
Mg2+
-
activates at up to 4 mM, inhibition above, probably due to blockage of substrate binding
Mg2+
-
required
Mg2+
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+
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+
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+
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+
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
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
at high concentrations
(S)-malate
-
substrate inhibition
(S)-malate
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
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
acetyl-CoA
-
inhibits isozyme NADP-ME1
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
ATP
-
non-competitive versus L-malate
ATP
27% inhibition at 0.2 mM
ATP
-
83% inhibition at 2 mM
ATP
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
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
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+
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
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
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
D-Glucose-6-phosphate
;
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
EDTA
-
-
Fe2+-ascorbate
-
rapid inactivation
fumarate
-
at high concentration
fumarate
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
fumarate
-
inhibits isozymes NADP-ME1 , NADP-ME3 and NADP-ME4
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
-
no 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
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
-
competitive
oxaloacetic acid
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
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
sesamol
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
inhibition of isozyme NADP-ME2
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+
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
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
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
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
-
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
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
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
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
about 4fold increase of activity in the presence of 7.5 mM fumarate
fumarate
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
NH4+
-
activates
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
about 3fold increase of activity in the presence of 7.5 mM fumarate
succinate
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
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
the enzyme is induced by salt stress, NADP-ME activities in seedlings, leaves, and roots increase in response to NaCl
-
additional information
isozyme Hvme3 is not affected by light; the plastidic isozyme Hvme1 may perform housekeeping functions, but is upregulated as the photosynthetic decarboxylase
-
additional information
no activation of isozyme NADP-ME2 by aspartate
-
additional information
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
after PEG 6000 treatment, the levels of cytosolic NADP-ME transcripts are enhanced by approximately 2.5times
-
additional information
activity of the NADP-ME is mostly enhanced under various stresses
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
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
recombinant isozyme Hvme1
0.67
(S)-malate
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
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
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
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
recombinant NADP-ME2
3.3
(S)-malate
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
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
-
-
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+
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+
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+
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
0.0072
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
0.038
NADP+
-
-
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+
0.0721
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+
recombinant NADP-ME2
0.093
NADP+
recombinant NADP-ME2
0.1
NADP+
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
0.107
NADP+
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
-
-
0.69
pyruvate
pH 7.0, isozyme NADP-ME1
2.6
pyruvate
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
-
-
5.1
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
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
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
(S)-malate
Columba livia
-
pH 7.4, 25C, mutant enzyme D235A
0.005
(S)-malate
Columba livia
-
pH 7.4, 25C, mutant enzyme E234A
0.006
(S)-malate
Columba livia
-
pH 7.4, 25C, mutant enzyme D258A
0.3
(S)-malate
Columba livia
-
pH 7.4, 25C, Mg2+-activated, wild-type enzyme
0.9
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
1.1
(S)-malate
Columba livia
-
pH 7.4, 25C, mutant enzyme D257A
1.1
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
1.6
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
3.55
(S)-malate
Zea mays
-
pH 7.0, 30C, oxidized isozyme ZmC4-NADP-ME
5.6
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
8.35
(S)-malate
Zea mays
-
pH 7.0, 30C, reduced isozyme ZmC4-NADP-ME
12.6
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
13.6
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
15
(S)-malate
Columba livia
-
pH 7.4, 25C, Mn2+-activated, wild-type enzyme
15.7
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
19.1
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
23.2
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
31.34
(S)-malate
Columba livia
-
pH 7.4, 25C, Mn2+-activated, wild-type enzyme
34.83
(S)-malate
Columba livia
-
pH 7.4, 25C, Mg2+-activated, wild-type enzyme
38.7
(S)-malate
Arabidopsis thaliana
-
pH 7.5, 30C, isozyme NADP-ME1
46.44
(S)-malate
Columba livia
-
pH 7.4, 25C, mutant enzyme E234A
84.83
(S)-malate
Homo sapiens
-
mutant enzyme H51A/D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
91
(S)-malate
Zea mays
-
pH 8.0, 30C, oxidized isozyme ZmC4-NADP-ME
91.7
(S)-malate
Oryza sativa
Q6T5D1, Q9FRT2
recombinant NADP-ME2
94.57
(S)-malate
Homo sapiens
-
mutant enzyme D90A, in 50 mM Tris-HCl, pH 7.4, at 30C
95.53
(S)-malate
Homo sapiens
-
mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
96.7
(S)-malate
Oryza sativa
Q6T5D1, Q9FRT2
recombinant NADP-ME3
98.03
(S)-malate
Homo sapiens
-
mutant enzyme H142A/D568A, in 50 mM Tris-HCl, pH 7.4, at 30C
104.4
(S)-malate
Zea mays
-
pH 7.0, wild-type C4-NADP-ME isozyme
105.3
(S)-malate
Homo sapiens
-
mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30C
106
(S)-malate
Homo sapiens
-
mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30C
109.5
(S)-malate
Homo sapiens
-
mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30C
110.9
(S)-malate
Homo sapiens
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30C
122.7
(S)-malate
Homo sapiens
-
mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30C
136.9
(S)-malate
Homo sapiens
-
mutant enzyme D568A, in 50 mM Tris-HCl, pH 7.4, at 30C
140.1
(S)-malate
Columba sp.
-
pH 4.5, 25C, wild-type enzyme
151.3
(S)-malate
Arabidopsis thaliana
-
pH 7.5, 30C, isozyme NADP-ME4
151.7
(S)-malate
Zea mays
-
pH 7.0, wild-type non-C4-NADP-ME isozyme
154.3
(S)-malate
Nicotiana tabacum
Q006P9, Q006Q0
pH 7.3, isozyme NADP-ME1
177
(S)-malate
Nicotiana tabacum
Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME2
242
(S)-malate
Trypanosoma brucei
-
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
Arabidopsis thaliana
Q9LYG3, Q9XGZ0
pH 7.5
268.1
(S)-malate
Arabidopsis thaliana
-
pH 7.5, 30C, isozyme NADP-ME3
269
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME
324
(S)-malate
Arabidopsis thaliana
Q9LYG3, Q9XGZ0
pH 7.5
324.1
(S)-malate
Arabidopsis thaliana
-
pH 7.5, 30C, isozyme NADP-ME2
376
(S)-malate
Sulfolobus solfataricus
-
pH 8.0, 60C
518
(S)-malate
Trypanosoma cruzi
-
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
Trypanosoma cruzi
-
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
Trypanosoma brucei
-
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
Anas platyrhynchos
-
-
13.5
NAD+
Zea mays
-
wild-type enzyme, pH 8.0, 30C
13.5
NAD+
Zea mays
-
wild-type enzyme, pH 7.0
18.4
NAD+
Zea mays
-
mutant K435L/K436L, pH 8.0, 30C
22
NAD+
Homo sapiens
-
mutant S346K, pH 7.4, 30C
28.9
NAD+
Homo sapiens
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30C
34.18
NAD+
Homo sapiens
-
in 50 mM Tris-HCl (pH 7.4)
40
NAD+
Homo sapiens
-
mutant K347Y, pH 7.4, 30C
40.6
NAD+
Zea mays
-
mutant A392G, pH 7.0
51
NAD+
Homo sapiens
-
wild-type enzyme, pH 7.4, 30C
53
NAD+
Homo sapiens
-
mutant S347Y/K362Q, pH 7.4, 30C
60
NAD+
Homo sapiens
-
mutant K362Q, pH 7.4, 30C
65
NAD+
Homo sapiens
-
mutant S346K/K347Y, pH 7.4, 30C
108
NAD+
Homo sapiens
-
mutant K362H, pH 7.4, 30C
110
NAD+
Homo sapiens
-
mutant S346K/K362Q, pH 7.4, 30C
113
NAD+
Homo sapiens
-
mutant E314A, pH 7.4, 30C
124
NAD+
Homo sapiens
-
mutant S346K/K347Y/K362Q, pH 7.4, 30C
131
NAD+
Homo sapiens
-
mutant S346I/K347D/K362H, pH 7.4, 30C
145
NAD+
Homo sapiens
-
mutant E314A/S346K, pH 7.4, 30C
166
NAD+
Homo sapiens
-
mutant E314A/S346I/K347D/K362H, pH 7.4, 30C
208
NAD+
Homo sapiens
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30C
219
NAD+
Homo sapiens
-
mutant S346K/K347Y/K362H, pH 7.4, 30C
258
NAD+
Homo sapiens
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30C
0.38
NADP+
Zea mays
-
mutant R237L, pH 8.0, 30C
0.38
NADP+
Zea mays
-
mutant R237L, pH 7.0
0.8
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
1.1
NADP+
Zea mays
-
mutant K225I, pH 8.0, 30C
1.1
NADP+
Zea mays
-
pH 8.0, 30C, mutant C246A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
1.3
NADP+
Homo sapiens
-
mutant S346I/K347D/K362H, pH 7.4, 30C
1.6
NADP+
Zea mays
-
pH 8.0, 30C, mutant C270A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
3.55
NADP+
Zea mays
-
pH 7.0, 30C, oxidized isozyme ZmC4-NADP-ME; pH 7.0, 30C, wild-type, treated with diamide
4.2
NADP+
Zea mays
-
mutant A387G, pH 7.0
5.6
NADP+
Zea mays
-
pH 8.0, 30C, mutant C192A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
8
NADP+
Homo sapiens
-
mutant S346K/K347Y/K362H, pH 7.4, 30C
8.35
NADP+
Zea mays
-
pH 7.0, 30C, reduced isozyme ZmC4-NADP-ME; pH 7.0, 30C, wild-type, treated with dithiothreitol
13.2
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
14.2
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
15
NADP+
Homo sapiens
-
mutant E314A/S346I/K347D/K362H, pH 7.4, 30C; mutant S346K/K347Y/K362Q, pH 7.4, 30C
15.9
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
19.5
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
23.2
NADP+
Zea mays
-
pH 8.0, 30C, mutant C231A; pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
26
NADP+
Homo sapiens
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30C
30.8
NADP+
Zea mays
-
recombinant enzyme, pH 7.0
38.7
NADP+
Arabidopsis thaliana
-
pH 7.5, NADP-ME1
51
NADP+
Homo sapiens
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30C
66.6
NADP+
Escherichia coli
-
pH 7.5, recombinant MaeB
78
NADP+
Homo sapiens
-
mutant S347Y/K362Q, pH 7.4, 30C
88.3
NADP+
Oryza sativa
Q6T5D1, Q9FRT2
recombinant NADP-ME2
91
NADP+
Zea mays
-
pH 8.0, 30C, oxidized isozyme ZmC4-NADP-ME; pH 8.0, 30C, wild-type, treated with diamide
98.3
NADP+
Oryza sativa
Q6T5D1, Q9FRT2
recombinant NADP-ME3
102
NADP+
Homo sapiens
-
mutant S346K/K347Y, pH 7.4, 30C
110
NADP+
Homo sapiens
-
mutant E314A, pH 7.4, 30C
112
NADP+
Homo sapiens
-
mutant S346K/K362Q, pH 7.4, 30C
113.2
NADP+
Homo sapiens
-
in 50 mM Tris-HCl (pH 7.4)
121
NADP+
Homo sapiens
-
mutant K347Y, pH 7.4, 30C
126
NADP+
Homo sapiens
-
wild-type enzyme, pH 7.4, 30C
129
NADP+
Homo sapiens
-
mutant S346K, pH 7.4, 30C
132
NADP+
Homo sapiens
-
mutant K362Q, pH 7.4, 30C
135.8
NADP+
Homo sapiens
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30C
137
NADP+
Homo sapiens
-
mutant E314A/S346K, pH 7.4, 30C
149
NADP+
Homo sapiens
-
mutant K362H, pH 7.4, 30C
151.3
NADP+
Arabidopsis thaliana
-
pH 7.5, NADP-ME4
181.1
NADP+
Zea mays
-
mutant K435L/K436L, pH 8.0, 30C
200.3
NADP+
Zea mays
-
mutant A392G, pH 7.0
201.3
NADP+
Zea mays
-
wild-type enzyme, pH 8.0, 30C
201.3
NADP+
Zea mays
-
wild-type enzyme, pH 7.0
268.1
NADP+
Arabidopsis thaliana
-
pH 7.5, NADP-ME3
269
NADP+
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME; pH 8.0, 30C, wild-type, treated with dithiothreitol
284
NADP+
Trypanosoma brucei
-
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+
Arabidopsis thaliana
-
pH 7.5, NADP-ME2
504
NADP+
Trypanosoma cruzi
-
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+
Trypanosoma cruzi
-
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+
Trypanosoma brucei
-
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+
Arabidopsis thaliana
-
pH 7.5, NADP-ME2
8.3
pyruvate
Trypanosoma cruzi
-
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
Arabidopsis thaliana
-
pH 7.0, 30C, isozyme NADP-ME1
21.6
pyruvate
Nicotiana tabacum
Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME2
34
pyruvate
Trypanosoma brucei
-
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
Trypanosoma cruzi
-
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
Arabidopsis thaliana
-
pH 7.0, 30C, isozyme NADP-ME2
75
pyruvate
Arabidopsis thaliana
Q9LYG3, Q9XGZ0
pH 7.0
113
pyruvate
Trypanosoma brucei
-
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
Nicotiana tabacum
Q006P9, Q006Q0
pH 7.0, isozyme NADP-ME1
237
pyruvate
Arabidopsis thaliana
-
pH 7.0, 30C, isozyme NADP-ME3
237
pyruvate
Arabidopsis thaliana
Q9LYG3, Q9XGZ0
pH 7.0
284.1
pyruvate
Arabidopsis thaliana
-
pH 7.0, 30C, isozyme NADP-ME4
582
L-Malate
Sinorhizobium meliloti
-
assuming an octameric oligomerization state
additional information
additional information
Homo sapiens
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
200
0.37
(S)-malate
Zea mays
-
pH 8.0, 30C, mutant C270A
200
0.9
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
200
1.7
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
200
1.9
(S)-malate
Zea mays
-
pH 8.0, 30C, mutant C192A
200
3
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
200
4.3
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
200
4.3
(S)-malate
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
200
7.8
(S)-malate
Zea mays
-
pH 8.0, 30C, mutant C246A
200
9.1
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
200
11
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
200
13.6
(S)-malate
Zea mays
-
pH 8.0, 30C, mutant C231A
200
170
(S)-malate
Populus trichocarpa
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
200
297
(S)-malate
Trypanosoma cruzi
-
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
Trypanosoma brucei
-
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
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME
200
690
(S)-malate
Zea mays
-
pH 8.0, 30C, wild-type, treated with dithiothreitol
200
3536
(S)-malate
Trypanosoma brucei
-
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
Trypanosoma cruzi
-
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+
Homo sapiens
-
wild-type enzyme, pH 7.4, 30C
7
0.12
NADP+
Zea mays
-
pH 8.0, 30C, mutant C270A
10
0.21
NADP+
Zea mays
-
pH 8.0, 30C, mutant C246A
10
0.36
NADP+
Zea mays
-
pH 8.0, 30C, mutant C192A
10
0.37
NADP+
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C270A
10
1.5
NADP+
Zea mays
-
pH 8.0, 30C, mutant C231A
10
1.86
NADP+
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C192A
10
7.86
NADP+
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C246A
10
9.7
NADP+
Zea mays
-
pH 8.0, 30C, wild-type, treated with dithiothreitol
10
13.64
NADP+
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME, mutant C231A
10
22
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30C
10
110
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30C
10
140
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30C
10
210
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30C
10
650
NADP+
Populus trichocarpa
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30C
10
9746
NADP+
Zea mays
-
pH 8.0, 30C, reduced isozyme ZmC4-NADP-ME
10
17780
NADP+
Trypanosoma brucei
-
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+
Trypanosoma cruzi
-
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+
Trypanosoma cruzi
-
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+
Trypanosoma brucei
-
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+
Homo sapiens
-
wild-type enzyme, pH 7.4, 30C
10
1.1
pyruvate
Trypanosoma cruzi
-
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
Trypanosoma brucei
-
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
Trypanosoma cruzi
-
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
Trypanosoma brucei
-
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]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.008 - 0.89
-
enzyme activity in several recombinant strains, overview
0.01
-
below, wild-type strain W3110
0.048
enzyme extracts from flowers; enzyme extracts from flowers
0.069
enzyme extracts from stems; enzyme extracts from stems
0.072
enzyme extracts from leaves; enzyme extracts from leaves
0.16
root enzyme under salt stress after 24 h
0.2
leaf enzyme under salt stress after 24 h
0.571
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
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
recombinant NADP-ME3
85.1
recombinant NADP-ME2
90.9
-
mitochondrial enzyme
91.4
-
cytosolic enzyme
199
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
-
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
ORGANISM
UNIPROT
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
isozyme ZmChlMe2
7
-
carboxylation and decarboxylation, cytosolic enzyme
7
-
TES-NaOH buffer
7
-
assay at
7
-
reverse reaction
7
-
assay at
7
isozyme NADP-ME1, reverse reaction; isozyme NADP-ME2, forward and reverse reaction
7
-
assay at, reverse reaction
7
-
reductive carboxylation of pyruvate
7 - 8
-
assay at
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
7.3
-
carboxylation of pyruvate
7.3
-
carboxylation of pyruvate; NADP+-linked decarboxylation of malate, at 1 mM malate
7.3
-
isozyme 2
7.3
recombinant NADP-ME2
7.3
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
7.5
-
TES-NaOH buffer
7.5
-
carboxylation of pyruvate
7.5
-
assay at
7.5
-
assay at
7.5
assay at, forward reaction
7.5
-
forward reaction
7.5
recombinant isozyme Hvme3
7.5
-
assay at, forward reaction
7.5
-
assay at
7.5
-
assay at
7.5
-
oxidative decarboxylation of malate
7.6
-
cytosolic enzyme, decarboxylation
7.6 - 7.7
-
both reaction directions
7.7
recombinant NADP-ME2
7.8
-
oxidative decarboxylation of L-malate
7.8
-
assay at
7.8
recombinant isozyme Hvme1
8
-
decarboxylation of malate
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
approximately, isozyme ZmChlMe1
8
-
assay at
8.3
-
with 0.1 mM L-malate
8.5 - 9
Pigeon
-
in presence of 0.1 M malate
8.8
-
with 1 mM L-malate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
-
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
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
pH: about 65% of maximal activity, pH: about 65% of maximal activity, recombinant NADP-ME3
7.5 - 10.5
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
25
-
assay at, both reaction directions
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
isozyme ZmChlMe2
5.1
-
isoelectric focusing
5.5
-
isoelectric focusing
5.9
isozyme Hvme1, sequence calculation
6
isozyme ZmChlMe1
6
-
isozyme 1, isoelectric focusing; isozyme 2, isoelectric focusing
6.5
isozyme Hvme3, sequence calculation
7.1
-
recombinant enzyme, isoelectric focusing
8.9
isozyme Hvme2, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Trypanosoma cruzi CL Brener
-
-
-
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
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
-
insulinoma cells, high expression level of isozyme ME1
Manually annotated by BRENDA team
-
etiolated
Manually annotated by BRENDA team
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
AF288911, P36444
developing, expression pattern of the isozymes
Manually annotated by BRENDA team
AF288916, AF288917, Q8SAT3
-
Manually annotated by BRENDA team
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
; 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
; isozyme NADP-ME1 is leaf-abundant
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
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
-
isozyme NADP-ME1
Manually annotated by BRENDA team
emerging root
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
AF288898, AF288899
-
Manually annotated by BRENDA team
AF288900, AF288901, AF288902, Q93ZK8
-
Manually annotated by BRENDA team
AF288904, AF288905
-
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
-
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
-
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
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
AF288916, AF288917, Q8SAT3
both isozymes
Manually annotated by BRENDA team
isozyme Hvme1 possesses a putative transit peptide
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
isozyme Hvme2; isozyme Hvme3
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
-
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64000
mature monomer of recombinant enzyme after enterokinase digestion, SDS-PAGE
700772
65000
SDS-PAGE; SDS-PAGE
697911
68000
-
gel filtration
286716
70000
-
monomeric flower isozyme, native PAGE
686932
71600
calculated from amino acid sequence
700772
80000
gel filtration
655672
90000
-
sucrose density gradient centrifugation
286716
105000
-
-
286739
105000
-
gel filtration
680589
110000
-
recombinant dimeric enzyme, gel filtration at pH 7.0, minor peak
656120
140000
-
dimeric flower isozyme, native PAGE
686932
180000
-
gel filtration
286715
216000
-
cytosolic enzyme, density gradient centrifugation
286725
226000
-
recombinant tetrameric enzyme, gel filtration at pH 8.0, major peak
656120
227000
-
mitochondrial enzyme, density gradient centrifugation
286725
230000 - 240000
-
and a second molecular weight form of 460000-480000 Da, gel filtration
286728
240000
-
recombinant isozyme NADP-ME2, gel filtration
689596
243000
gel filtration
697911
248000
-
tetrameric isozymes from leaves, stem and roots, native PAGE, overview
686932
249000
gel filtration
697911
254000
-
gel filtration
654369
257000
-
gel filtration
286735
258000
-
gel filtration
286733
260000
native PAGE; native PAGE
689506
260000 - 265000
-
gel filtration
286737
264000
-
isozyme 2, gel filtration
657103
280000
-
tetrameric isozymes from flower, leaves, and stem, native PAGE, overview
686932
285000
-
gel filtration
286742
460000 - 480000
-
and a second molecular weight form of 230000-240000 Da, gel filtration
286728
SUBUNITS
ORGANISM
UNIPROT
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
?
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
?
x * 83000, SDS-PAGE
?
Escherichia coli MG1655
-
x * 83000, SDS-PAGE
-
dimer
-
2 * 42000, SDS-PAGE
dimer
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
-
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
4 * 64000, about, isozyme Hvme3, sequence calculation; 4 * 68000, about, isozyme Hvme2, sequence calculation; 4 * 72000, about, isozyme Hvme1, sequence calculation
tetramer
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
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
stable for 24 h
680589
7.5
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
697911
8
-
stable for at least one month
680589
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
stable for at least 120 min
286739
30
-
completely stable for at least 20 min
286740
33
-
120 min, 24% loss of activity
286739
40
-
120 min, 70% loss of activity
286739
44
-
stable for at least 10 min
654369
50
-
15 min, pH 8.0, irreversible thermal inactivation
687132
52 - 64
-
thermal denaturation of c-NADP-ME wild-type and the interface mutants, overview
723595
60
-
stable for at least 24 h
680589
60
-
12 h, in absence of solvent, stable
724897
75
-
stable for at least 12 h
680589
80
-
stable for at least 7 h
680589
85
-
stable for at least 5 h
680589
additional information
Pigeon
-
malic acid decreases heat stability at pH values above 5.0; Mg2+ or Mn2+ increase heat stability
286722
additional information
-
Mg2+ does not influence the thermal stability of the enzyme
723595
GENERAL STABILITY
ORGANISM
UNIPROT
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
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
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
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
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
separation of isozymes in native PAGE
-
recombinant fusion protein; recombinant fusion protein
-
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
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
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
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
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)
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
3'-UTR region, cloning, sequencing, and analysis
AF288906, P93139
3'-UTR region, cloning, sequencing, and analysis
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)
gene malE, DNA and amino acid sequence determination and analysis, genomic library construction, screening, and functional enzyme expression in Escherichia coli
gene malE, DNA and amino acid sequence determination and analysis, genomic library construction, screening, and functional enzyme expression in Escherichia coli
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
isozyme NADP-ME2, expression in Escherichia coli; nadp-me1, expression in Escherichia coli
expression in Arabidopsis thaliana under control of the 35S promoter
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
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
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)
preparation of a genomic library, DNA and amino acid sequence determination and analysis, detailed phylogenetic reconstruction of malic enzymes, overview
DNA and amino acid sequence determination and analysis
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
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
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
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
darkness does not affect enzyme expression in leves, no effect by salicylic acid or by salt stress
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
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