Any feedback?
Information on EC 1.1.1.40 - malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) and Organism(s) Arabidopsis thaliana and UniProt Accession Q8H1E2
for references in articles please use BRENDA:EC1.1.1.40Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.40 malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)IUBMB Comments
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).
Specify your search results
Word Map
- 1.1.1.40
- chloroplast
- co2
- carboxylase
- phosphoenolpyruvate
- maize
- bundle
- sheath
- glucose-6-phosphate
- mesophyll
-
carboxykinase
- thioredoxins
- dikinase
- chlorophyll
- grass
- rubisco
-
photosystems
- sorghum
-
nad-malic
- 6-phosphogluconate
-
lipogenesis
-
lipogenic
- flaveria
- fructose-1,6-bisphosphatase
- orthophosphate
- ribulose-1,5-bisphosphate
-
kranz
-
nadp-isocitrate
- pck
-
crassulacean
-
photorespiration
-
nadph-generating
-
4.1.3.8
-
calvin
- trinervia
- phosphoribulokinase
-
non-photosynthetic
-
ferredoxin-thioredoxin
-
c4-like
-
bundle-sheath
-
photorespiratory
-
6.4.1.2
- bidentis
- crystallinum
-
3.1.3.11
-
4.1.1.31
- fbpase
-
water-use
- panicum
- mesembryanthemum
- nadp-icdh
- analysis
- biotechnology
- medicine
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nadp-me, nadp-malate dehydrogenase, nadp-malic enzyme, nadp-mdh, nadp-dependent malic enzyme, nadp-dependent malate dehydrogenase, nadp-me2, malic enzyme 1, nadp malic enzyme, nadp-me1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-malate:NADP oxidoreductase
-
-
-
-
malate dehydrogenase (decarboxylating, NADP)
-
-
-
-
malate dehydrogenase (NADP, decarboxylating)
-
-
-
-
malic enzyme
-
-
-
-
NADP+ dependent malic enzyme
-
-
-
-
NADP-linked decarboxylating malic enzyme
-
-
-
-
NADP-malic enzyme
NADP-ME
NADP-ME1
NADP-ME2
NADP-ME3
NADP-specific malate dehydrogenase
-
-
-
-
NADP-specific malic enzyme
-
-
-
-
pyruvic-malic carboxylase
-
-
-
-
TME
-
-
-
-
NADP-malic enzyme
-
-
-
-
NADP-ME
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
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).
CAS REGISTRY NUMBER
COMMENTARY
9028-47-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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 + H+
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
peroxynitrite
-
peroxynitrite inhibits cytosolic NADP-ME2 activity due to tyrosine nitration at Tyr-73 to 3-nitrotyrosine
additional information
-
no inhibition of isozyme NADP-ME2 by tartrate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aspartate
-
isozyme NADP-ME2 activity is highly stimulated at both low and high concentrations of 0.5 mM and 2 mM, respectively
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
-
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of isozymes at different pH, overview
-
additional information
additional information
-
kinetics of NADP+ and (S)-malate at different NADP+ and fumarate concentrations, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
NADP-ME1 expression only in some secondary roots, where it is confined to the stele and excluded from the tips
-
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
additional information
-
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-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
-
expression of NADP-ME3 exclusively in pollen from the latest maturation stage up to its germination on the stigma
-
expression of NADP-ME2 throughout all the tissues, except for root tips
-
stele, mainly at emerging lateral roots and at root tips, NADP-ME4
-
expression of NADP-ME3 is restricted to the trichomes and trichome basal cells of leaves and stems
additional information
-
NADP-ME2 activity is detected in all reproductive organs
additional information
-
no activity of NADP-ME1 is detectable in leaves and stems throughout growth, not expressed in floral organs
additional information
-
NADP-ME2 and 4 are constitutively expressed, while NADP-ME1 is restricted to secondary roots and NADP-ME3 to trichomes and pollen
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
the enzyme metabolizes malate, which is important for stabilizing cytoplasmic pH, controlling stomatal aperture, increasing resistance to aluminum excess and pathogens. Pyruvate, another product of the enzyme reaction, participates in the synthesis of defense compounds such as flavonoids and lignin, which are involved in stresses tolerance such as mechanical wounding and pathogen invasion. Moreover, the enzyme provides essential reductive coenzyme NADPH in the biosynthesis of flavonoids and lignin. On the other hand, NADPH is crucial for reactive oxygen species metabolizing systems such as the ascorbate-glutathione pathway and NADPH-dependent thioredoxin reductase, and is also required by apoplastic oxidative burst in most plant-pathogen interactions
physiological function
additional information
-
analysis of transcriptional co-response patterns related NADP-ME2 to plant defence responses, overview
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
-
seeds of Arabidopsis thaliana lacking a functional enzyme isoform NADP-ME1 have reduced seed viability relative to the wild type. Seeds of the loss-of-function mutant display higher levels of protein carbonylation than those of the wild type
malfunction
-
seeds of isoform nadp-me1 mutant are less sensitive to the abscisic acid repression of germination and loss viability more rapidly than wild type
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
-
isoform NADP-ME1 activity is required for protecting seeds against oxidation during seed dry storage
physiological function
-
isoform NADP-ME1 plays a specialized role, linked to abscisic acid signalling during the seed development as well as in the response to water deficit stress
physiological function
-
the enzyme plays important roles in diverse stress responses (pathogen infection, ozone stress, drought stress, salt stress, metal excess, temperature stress, wounding and UV radiation)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nitration
-
Tyr-73 of the enzyme is exclusively nitrated to 3-nitrotyrosine by peroxynitrite
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R115A
additional information
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
additional information
expression of NADP-MDH is not affected in knock-out plants, knock-out mutant lines At5g58340::tDNA-1, SALK_053119, and At5g58340::tDNA-2, SALK_018118, carrying a DNA insert in the 5' region
additional information
-
construction of deletion mutants of isozyme NADP-ME2
additional information
-
generation of knock-out mutants nadp-me2.1 and -2.2 by Agrobacterium tumefaciens strain GV3101-mediated transformation using the vacuum infiltration method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
at pH 7.5 isoenzyme NADP-ME2 retains 95% of the maximal activity
697911
7.5
at pH 7.5 isoenzyme NADP-ME3 retains 95% of the maximal activity
697911
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
25% diminished cytosolic enzyme activity is found in Arabidopsis thaliana seedlings exposed to short-term low temperature (4°C for 48 h)
-
enzyme isoform NADP-ME1 expression is increased in imbibed aged as compared with non-aged seeds
-
isoform NADP-ME1 transcript and protein are almost undetectable during normal vegetative growth, but gradually increase and reach levels higher than those of the other isoforms in the latest stages of seed development (reaching a value 136fold higher at 18 days after pollination). The treatment with 0.01 mM abscisic acid, 100 mM NaCl and 225 mM mannitol specifically induces the accumulation of isoform NADP-ME1 in seedlings and roots
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wheeler, M.C.; Tronconi, M.A.; Drincovich, M.F.; Andreo, C.S.; Fluegge, U.I.; Maurino, V.G.
A comprehensive analysis of the NADP-malic enzyme gene family of Arabidopsis
Plant Physiol.
139
39-51
2005
Arabidopsis thaliana
Hameister, S.; Becker, B.; Holtgrefe, S.; Strodtkoetter, I.; Linke, V.; Backhausen, J.E.; Scheibe, R.
Transcriptional regulation of NADP-dependent malate dehydrogenase: comparative genetics and identification of DNA-binding proteins
J. Mol. Evol.
65
437-455
2007
Arabidopsis thaliana (Q8H1E2)
Gerrard Wheeler, M.C.; Arias, C.L.; Tronconi, M.A.; Maurino, V.G.; Andreo, C.S.; Drincovich, M.F.
Arabidopsis thaliana NADP-malic enzyme isoforms: high degree of identity but clearly distinct properties
Plant Mol. Biol.
67
231-242
2008
Arabidopsis thaliana
Gerrard Wheeler, M.C.; Arias, C.L.; Maurino, V.G.; Andreo, C.S.; Drincovich, M.F.
Identification of domains involved in the allosteric regulation of cytosolic Arabidopsis thaliana NADP-malic enzymes
FEBS J.
276
5665-5677
2009
Arabidopsis thaliana (Q9LYG3), Arabidopsis thaliana (Q9XGZ0), Arabidopsis thaliana
Voll, L.; Zell, M.; Engelsdorf, T.; Saur, A.; Wheeler, M.; Drincovich, M.; Weber, A.; Maurino, V.
Loss of cytosolic NADP-malic enzyme 2 in Arabidopsis thaliana is associated with enhanced susceptibility to Colletotrichum higginsianum
New Phytol.
195
189-202
2012
Arabidopsis thaliana
Arias, C.; Andreo, C.; Drincovich, M.; Gerrard Wheeler, M.
Fumarate and cytosolic pH as modulators of the synthesis or consumption of C4 organic acids through NADP-malic enzyme in Arabidopsis thaliana
Plant Mol. Biol.
81
297-307
2013
Arabidopsis thaliana
Begara-Morales, J.C.; Sanchez-Calvo, B.; Gomez-Rodriguez, M.V.; Chaki, M.; Valderrama, R.; Mata-Perez, C.; Lopez-Jaramillo, J.; Corpas, F.J.; Barroso, J.B.
Short-term low temperature induces nitro-oxidative stress that deregulates the NADP-Malic enzyme function by tyrosine nitration in Arabidopsis thaliana
Antioxidants (Basel)
8
448
2019
Arabidopsis thaliana
Arias, C.L.; Pavlovic, T.; Torcolese, G.; Badia, M.B.; Gismondi, M.; Maurino, V.G.; Andreo, C.S.; Drincovich, M.F.; Gerrard Wheeler, M.C.; Saigo, M.
NADP-dependent malic enzyme 1 participates in the abscisic acid response in Arabidopsis thaliana
Front. Plant Sci.
9
1637
2018
Arabidopsis thaliana
Tronconi, M.A.; Andreo, C.S.; Drincovich, M.F.
Chimeric structure of plant malic enzyme family Different evolutionary scenarios for NAD- and NADP-dependent isoforms
Front. Plant Sci.
9
565
2018
Arabidopsis thaliana
Yazdanpanah, F.; Maurino, V.G.; Mettler-Altmann, T.; Buijs, G.; Bailly, M.N.; Karimi Jashni, M.; Willems, L.; Sergeeva, L.I.; Rajjou, L.C.; Hilhorst, H.W.M.; Bentsink, L.N.
NADP-malic enzyme 1 affects germination after seed storage in Arabidopsis thaliana
Plant Cell Physiol.
60
318-328
2019
Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 1.1.1.40)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
