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1.1.1.40: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
This is an abbreviated version, for detailed information about malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+), go to the full flat file.
Reaction
Synonyms
ADP-malic enzyme2, c-NADP-ME, C4 NADP-malic enzyme, C4 photosynthetic NADP-malic enzyme, C4-NADP-malic enzyme, C4-NADP-ME, ChlME1, ChlME2, cytoNADPME, cytosolic malic enzyme, cytosolic NADP+-dependent isoform, cytosolic NADP+-dependent malic enzyme, L-malate: NADP oxidoreductase (decarboxylating), L-malate: NADP oxidoreductase [OAA decarboxylating], L-malate: NADP oxidoreductase [oxaloacetate decarboxylating], L-malate:NADP oxidoreductase, L-malate:NADP oxidoreductase (oxaloacetate decarboxylating), MaeB, MalA, malate dehydrogenase (decarboxylating, NADP), malate dehydrogenase (NADP, decarboxylating), malE1, malic enzyme, malic enzyme 1, malic enzyme 2, malic enzyme 3, malic enzyme-NADP, ME, ME-NADP, ME1, ME2, ME3, mitochondrial NADP malic enzyme, NAD(P)+-malic enzyme, NADP dependent malic enzyme, NADP malic enzyme, NADP(H)-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-linked decarboxylating malic enzyme, NADP-malate enzyme, NADP-malic enzyme, NADP-malic enzyme 2, NADP-MDH, NADP-ME, NADP-ME1, NADP-ME2, NADP-ME3, NADP-ME4, NADP-specific malate dehydrogenase, NADP-specific malic enzyme, NADP-specific ME, pyruvic-malic carboxylase, TME
ECTree
1.1.1.40 malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)Advanced search results
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Please login to have access to the AMENDA and FRENDA dataResults
in table
55
4129
142
104
160
202
13
23
100
15
10
68
276
Subunits
Subunits on EC 1.1.1.40 - malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
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SUBUNITS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
monomer
oligomer
tetramer
additional information
dimer
-
the dimeric form of c-NADP-ME is as active as tetramers, analytical ultracentrifugation
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
-
structure analysis from crystal structure, the enzyme is a tetrameric protein with double dimer quaternary structure, pH dependence of enzyme structure, overview
tetramer
-
c-NADP-ME exists mainly as a tetramer, analytical ultracentrifugation
tetramer
-
c-NADP-ME has a dimer-dimer quaternary structure in which the dimer interface associates more tightly than the tetramer interface
tetramer
a dimer of dimers. The c-NADP-ME monomer is composed of four domains. Domain A (residues 23-130) is predominantly helical and confers the ability to bind fumarate. Domain B (residues 131-277 and 464-535) contains a central five-stranded parallel beta-sheet surrounded by helices on both sides. Domain C (residues 278-463) exhibits a dinucleotide-binding Rossmann fold with a modification: strand beta3 is replaced by a short antiparallel beta-strand. Domain D (residues 536-579) contains one helix followed by a long extended random coil structure protruding away from the ordered portion of the ME monomer. The active site of ME is located at the interface of domains B and C, whereas residues in domains A and D primarily participate in the formation of dimers and tetramers
tetramer
4 * 64000, about, isozyme Hvme3, sequence calculation; 4 * 68000, about, isozyme Hvme2, sequence calculation; 4 * 72000, about, isozyme Hvme1, sequence calculation
tetramer
-
4 * 62000, tissue specific isozymes, SDS-PAGE, 4 * 70000, tissue specific isozymes, SDS-PAGE
tetramer
4 * 63000, plastidic isozyme, SDS-PAGE; 4 * 65000, cytosolic isozyme, SDS-PAGE
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
-
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
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
-
extent of oligomerization is pH-dependent, 3D-structure analysis
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
Information
