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(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
(S)-malate + NAD+
pyruvate + CO2 + NADH
(S)-malate + NADP+
?
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
pyruvate + NADPH + CO2
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
Oxaloacetate
Pyruvate + CO2
oxaloacetate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
Pyruvate + CO2
Oxaloacetate
-
-
-
-
r
pyruvate + CO2 + NADPH
(S)-malate + NADP+
pyruvate + CO2 + NADPH
L-malate + NADP+
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
pyruvate + NADPH
?
-
at 5.4% of the activity of NADP-dependent oxidative decarboxylation of malate
-
-
?
additional information
?
-
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
-
-
-
?
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
the unique and specialized C4-type enzyme has evolved fro the C3-type enzyme
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
at 39% of the activity with NADP+
-
ir
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
lower activity than with NADP+
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
low activity with NAD+ as cofactor
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
NADP+ is preferred over NAD+
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
when the R221G/K228R/I310V mutant is used with NADH, the mutant gives 1.2 and 2.7 times higher malate concentration than the wild-type with NADPH and NADH, respectively. These results can be partly explained by the alteration of the cofactor preference of the mutant enzyme, since the half-life of NADH is approximately 1.3times longer than that of NADPH at 50°C. However, the Km of the triple mutant for NAD+ remains 190times higher than that of the wild-type for NADP+
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(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
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?, r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
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
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
the reaction plays a role in the C4 metabolism, pathway regulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
AF288898, AF288899
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
AF288900, AF288901, AF288902, Q93ZK8 -
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
AF288904, AF288905
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
carboxyl is replaced by hydrogen without net change of configuration
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
the reverse reaction is catalyzed at 84% of the activity
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
weak reaction
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
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
regulation of isozyme Hvme3, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
no day/night regulation of the isozyme 2 in leaves via expression level but by metabolite inhibition, overview
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
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
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
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
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
Pigeon
-
Arg residue is involved in the binding of C-1 carboxyl group of malate
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
Pigeon
-
the singly-ionized species is the substrate, doubly-ionized malate is unreactive
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
the cycling of pyruvate by isozyme ME1 generates cytosolic NADPH
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
the enzyme is involved in glucose-induced insulin secretion, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
reaction velocity is 29times higher in the direction of decarboxylation than in the direction of the carboxylation
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
enzyme is involved in fatty acid biosynthesis in oil seed leucoplasts, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
decarboxylation is favoured
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
NADP+ is preferred over NAD+
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
salmon
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
ir
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
the C4 isozyme takes part in the C4 and CAM photosynthetic metabolisms, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
the enzyme probably operates in the direction of pyruvate and NADPH production under physiological conditions
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
the enzyme probably operates in the direction of pyruvate and NADPH production under physiological conditions
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
the enzyme demonstrates 4.7fold higher activity in the direction of malate decarboxylation compared with pyruvate carboxylation
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
Mnium undulatum
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
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
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
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
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
oxaloacetate represents the intermediate resulting from dehydrogenation of malate during the first step of the catalytic cycle of MEs
-
-
r
Oxaloacetate
Pyruvate + CO2
-
-
-
-
r
Oxaloacetate
Pyruvate + CO2
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
-
at 1.3% of the rate of NADP+-linked oxidative decarboxylation
-
-
?
Oxaloacetate
Pyruvate + CO2
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
Pigeon
-
-
-
?
Oxaloacetate
Pyruvate + CO2
-
no activity
-
-
?
Oxaloacetate
Pyruvate + CO2
-
-
-
?
Oxaloacetate
Pyruvate + CO2
-
-
-
-
?
pyruvate + CO2 + NADPH
(S)-malate + NADP+
-
-
-
?
pyruvate + CO2 + NADPH
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
at 84% of the activity of the NADP+-linked oxidative decarboxylation of malate
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
6% of the activity of the NADP+-linked oxidative decarboxylation of malate
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
-
?
pyruvate + CO2 + NADPH
L-malate + NADP+
Pigeon
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
reaction velocity is 29times higher in the direction of decarboxylation than in the direction of the carboxylation
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
?
pyruvate + CO2 + NADPH
L-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
the reverse reaction is very slow
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
the reverse reaction is very slow
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
additional information
?
-
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
?
additional information
?
-
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288898
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288899
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288900
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288901
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288902
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288904
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288905
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288906
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288911
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288916
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288917
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
-
regulation and physiological roles of the isozymes
-
-
?
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
?
-
-
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
?
-
-
no activity with NAD+
-
-
-
additional information
?
-
-
no activity with NAD+
-
-
-
additional information
?
-
-
the enzyme does not use NAD+ and does not show activity of oxaloacetate decarboxylation. NaHCO3 does not serve as a CO2 donor for carboxylation of pyruvate
-
-
-
additional information
?
-
Mnium undulatum
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, 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
?
-
-
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
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, 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
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
-
no activity with NAD+
-
-
-
additional information
?
-
-
no activity with NAD+
-
-
-
additional information
?
-
-
no activity with NAD+
-
-
-
additional information
?
-
-
no activity with NAD+
-
-
-
additional information
?
-
-
no activity with NAD+
-
-
-
additional information
?
-
-
enzyme additionally catalyzes decarboxylation of oxalacetate
-
-
?
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 specific activity falls rapidly as the fruit ripens
-
-
?
additional information
?
-
malic enzymes can reversibly catalyze the NAD(P)H-dependent reductive carboxylation of pyruvate to malate
-
-
?
additional information
?
-
-
malic enzymes can reversibly catalyze the NAD(P)H-dependent reductive carboxylation of pyruvate to malate
-
-
?
additional information
?
-
when the R221G/K228R/I310V mutant is used with NADH, the mutant gives 1.2 and 2.7 times higher malate concentration than the wild-type with NADPH and NADH, respectively. These results can be partly explained by the alteration of the cofactor preference of the mutant enzyme, since the half-life of NADH is approximately 1.3times longer than that of NADPH at 50°C. However, the Km of the triple mutant for NAD+ remains 190times higher than that of the wild-type for NADP+
-
-
?
additional information
?
-
-
when the R221G/K228R/I310V mutant is used with NADH, the mutant gives 1.2 and 2.7 times higher malate concentration than the wild-type with NADPH and NADH, respectively. These results can be partly explained by the alteration of the cofactor preference of the mutant enzyme, since the half-life of NADH is approximately 1.3times longer than that of NADPH at 50°C. However, the Km of the triple mutant for NAD+ remains 190times higher than that of the wild-type for NADP+
-
-
?
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 does not decarboxylate oxaloacetate
-
-
?
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 does not decarboxylate oxaloacetate
-
-
?
additional information
?
-
-
enzyme is regulated by light and dithiols, such as dithioerythritol
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
the unique and specialized C4-type enzyme has evolved fro the C3-type enzyme
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
when the R221G/K228R/I310V mutant is used with NADH, the mutant gives 1.2 and 2.7 times higher malate concentration than the wild-type with NADPH and NADH, respectively. These results can be partly explained by the alteration of the cofactor preference of the mutant enzyme, since the half-life of NADH is approximately 1.3times longer than that of NADPH at 50°C. However, the Km of the triple mutant for NAD+ remains 190times higher than that of the wild-type for NADP+
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
Oxaloacetate
Pyruvate + CO2
-
-
-
-
r
Pyruvate + CO2
Oxaloacetate
-
-
-
-
r
pyruvate + CO2 + NADPH
(S)-malate + NADP+
-
-
-
?
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
additional information
?
-
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?, r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
the reaction plays a role in the C4 metabolism, pathway regulation, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
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
regulation of isozyme Hvme3, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
no day/night regulation of the isozyme 2 in leaves via expression level but by metabolite inhibition, overview
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
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
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
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
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
the cycling of pyruvate by isozyme ME1 generates cytosolic NADPH
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
the enzyme is involved in glucose-induced insulin secretion, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
enzyme is involved in fatty acid biosynthesis in oil seed leucoplasts, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
responsible for pyruvate and NADPH production
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
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
-
the C4 isozyme takes part in the C4 and CAM photosynthetic metabolisms, overview
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
the enzyme probably operates in the direction of pyruvate and NADPH production under physiological conditions
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
the enzyme probably operates in the direction of pyruvate and NADPH production under physiological conditions
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
the enzyme demonstrates 4.7fold higher activity in the direction of malate decarboxylation compared with pyruvate carboxylation
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
Mnium undulatum
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
r
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
-
-
-
-
?
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
r
pyruvate + CO2 + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
additional information
?
-
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
?
additional information
?
-
-
the enzyme is a supplier of reducing power in form of reduced NADPH for lipid biosynthesis
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288898
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288899
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288900
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288901
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288902
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288904
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288905
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288906
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288911
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288916
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
AF288917
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
regulation and physiological roles of the isozymes
-
-
?
additional information
?
-
-
regulation and physiological roles of the isozymes
-
-
?
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
?
-
-
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
?
-
Mnium undulatum
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
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
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, 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
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, 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 specific activity falls rapidly as the fruit ripens
-
-
?
additional information
?
-
malic enzymes can reversibly catalyze the NAD(P)H-dependent reductive carboxylation of pyruvate to malate
-
-
?
additional information
?
-
-
malic enzymes can reversibly catalyze the NAD(P)H-dependent reductive carboxylation of pyruvate to malate
-
-
?
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 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
?
-
-
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
-
-
?
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(NH4)2SO4
-
at high concentrations
1-methylenecyclopropan-trans-2,3-dicarboxylic acid
-
1-methylenecyclopropane
inhibits at 10 mM
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+
3-(pyridin-2-yl)-6-[(5,6,7,8-tetrahydronaphthalen-2-yl)methyl][1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
ATR7-010
acetyl phosphate
-
slight inhibition at 2 mM
adenosine 2'-phosphate
Pigeon
-
-
Cd2+
-
in the presence of Mn2+, Cd2+ ions almost completely inhibit the enzyme activity (5.9% residual activity)
Citric acid
-
inhibits all PtNADP-ME activities significantly
CO2
-
product inhibition, uncompetitive with respect to L-malate and NADP+, 39% inhibition at 25 mM
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-1,6-bisphosphate
D-glucose 6-phosphate
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
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
Diethylamine NONOate
-
35% inhibition at 5 mM
diphenyliodonium chloride
Pigeon
-
weak
diphosphate
-
diphosphate at 2 mM inhibits the enzyme by 50%, but the activity is completely recovered if Mg2+ concentration increases to 5 mM
Fe2+-ascorbate
-
rapid inactivation
GDP
-
13% inhibition at 5 mM
glutamine
-
slight inhibition at 5 mM
Glutarate
inhibits at 10 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
Hydroxypyruvate
-
hydroxypyruvate at 1 mM inhibits the enzyme activity by 45%
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
Magnaporthe oryzae effector AVR-Pii
-
-
-
Maleate
-
the cis isomer of fumarate, inhibition of isozyme NADP-ME2
malonyl-CoA
-
inhibition of mitochondrial enzyme and cytosolic enzyme to a much lower extent than with acetyl-CoA
Na2S
-
the enzyme activity is inhibited by up to 29-32% using 2 and 5 mM Na2S as H2S donor
NADP+
-
substrate inhibition
NADPH
-
product inhibition, competitive with respect to L-malate and NADP+
Ni2+
-
about 50% activity at 0.5 mM
o-Iodosobenzoate
Pigeon
-
strong
p-mercuribenzoate
Pigeon
-
strong
peroxynitrite
-
peroxynitrite inhibits cytosolic NADP-ME2 activity due to tyrosine nitration at Tyr-73 to 3-nitrotyrosine
Phenylglyoxal
Pigeon
-
pseudo-first-order loss of oxidative decarboxylase activity
phosphate
-
35% inhibition at 5 mM
S-nitrosocysteine
-
35% inhibition at 5 mM
Sn2+
-
1 mM Sn2+ ions reduce the enzyme activity by 31%
SO32-
-
in decarboxylation of malate: partially competitive with respect to malate, in carboxylation of pyruvate: fully competitive for CO2 or HCO3-
Tartrate
inhibits at 10 mM
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
(S)-malate
-
substrate inhibition
(S)-malate
an increase to malate concentration of 10 mM decreases the specific activity of rHVME1 by almost 50%
2-oxoglutarate
-
inhibition of isozyme NADP-ME2
2-oxoglutarate
-
slight inhibition at 2 mM
2-oxoglutarate
-
competitive
acetyl-CoA
-
inhibits isozyme NADP-ME1
acetyl-CoA
-
enzyme inhibition by acetyl-CoA is relieved by increasing CoASH concentrations
acetyl-CoA
-
acetyl-CoA (0.1 mM) exerts the greatest inhibitory effect leading to a residual activity of 24%
acetyl-CoA
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
acetyl-CoA
-
inhibition is much more pronounced in the mitochondrial enzyme than in the cytosolic enzyme and occurs at physiological acetyl-CoA concentrations
ADP
-
slight inhibition at 2 mM
ADP
-
83% inhibition at 2 mM
AMP
-
75% inhibition at 2 mM
AMP
-
41% inhibition at 5 mM
ATP
-
ATP
-
slight inhibition at 2 mM
ATP
-
non-competitive versus L-malate
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+
ATP
-
83% inhibition at 2 mM
ATP
-
ATP at 2 mM inhibits the enzyme by 50%, but the activity is completely recovered if Mg2+ concentration increases to 5 mM
ATP
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
ATP
27% inhibition at 0.2 mM
Ca2+
-
Ca2+
-
complete inhibition at 5 mM
cAMP
-
slight inhibition at 1 mM
cAMP
-
10% inhibition at 5 mM
citrate
-
competitive, 61% inhibition at 5 mM
Co2+
-
Co2+
-
about 90% activity at 0.5 mM
CoA
-
slight inhibition at 1 mM
CoA
30% inhibition of isozyme NADP-ME1 at 2 mM
CoA
-
activities of PtNADP-ME1, PtNADP-ME2 and PtNADPME4 proteins are inhibited
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+
-
complete inhibition at 5 mM
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
fumarate
-
inhibits isozymes NADP-ME1 , NADP-ME3 and NADP-ME4
fumarate
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
fumarate
-
at high concentration
glyoxylate
-
competitive inhibition, about 60% activity at 2 mM
glyoxylate
competitive inhibition
malate
-
no 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
-
no inhibition at pH 7.0
malate
inhibition of isozyme NADP-ME1 at pH 7.0
malate
-
the enzyme is inhibited by high malate concentration at pH 7.0
malate
Pigeon
-
substrate inhibition
malate
-
the enzyme is inhibited by high malate concentration at pH 7.0
malate
-
no inhibition at pH 7.0
malate
-
inhibition at pH 7.0
malate
-
inhibition at high concentrations at pH 7.0, but not at pH 8.0
malate
-
the enzyme is inhibited by high malate concentration at pH 7.0
malonate
-
inhibition of isozyme NADP-ME2
Mg2+
-
activates at up to 4 mM, inhibition above, probably due to blockage of substrate binding, Km is 0.19 mM
Mg2+
-
about 80% activity at 0.5 mM
Mg2+
-
mitochondrial enzyme, decarboxylation reaction, above 6 mM
NaCl
-
at high concentrations
NaCl
-
in the presence of 50 mM KCl, 50 mM NaCl inhibits the enzyme activity by 40%
oxalate
-
-
oxalate
-
51% inhibition at 1 mM
oxalate
-
inhibition is decreased by light exposure
oxaloacetate
-
oxaloacetate
-
competitive, 70% inhibition at 2 mM
oxaloacetate
-
competitive inhibition, about 25% activity at 2 mM
oxaloacetate
feedback inhibition
oxaloacetate
-
competitive
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
phosphoenolpyruvate
-
slight inhibition at 1 mM
phosphoenolpyruvate
-
competitive, 82% inhibition at 2 mM
phosphoenolpyruvate
-
39% inhibition at 5 mM
pyruvate
-
-
pyruvate
-
22% inhibition at 2 mM
pyruvate
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
pyruvate
-
product inhibition, competitive with respect to L-malate, 16% inhibition at 5 mM
pyruvate
-
non-competitive inhibition
pyruvate
-
inhibition is decreased by light exposure
sesamol
added to the medium, inhibits best at 9 mM; a specific inhibitor of the enzyme; strong inhibition at 10 mM
succinate
-
succinate
-
competitive, 28% inhibition at 5 mM
succinate
inhibition of isozyme NADP-ME2
succinate
-
slight inhibition at high concentrations
Tartronate
-
noncompetitive inhibitor with respect to L-malate
Zn2+
-
-
Zn2+
-
about 10% activity at 5 mM
additional information
-
no inhibition of isozyme NADP-ME2 by tartrate
-
additional information
-
peroxynitrite does not affect the enzyme even at a high concentration of 5 mM 3-morpholinosydnonimine
-
additional information
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
-
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
-
ATR4-003 (3-(4-methoxyphenyl)-2-methyl-5-([(4-methylpyrimidin-2-yl)sulfanyl]methyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one) and ATR6-001 ([1-amino-5-(morpholin-4-yl)-6,7,8,9-tetrahydrothieno[2,3-c]isoquinolin-2-yl](piperidin-1-yl)methanone) do not inhibitenzyme activity up to a concentration of 0.02 mM
-
additional information
-
glutamine is a poor inhibitor
-
additional information
Mnium undulatum
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
additional information
-
not inhibited by ATP, ADP, AMP, propionyl-COA, acetyl-CoA, CoA, succinate, L-glutamate, L-aspartate, isocitrate, citrate, pyruvate, D-fructose 6-phosphate, D-glucose 6-phosphate, and 2-oxoglutarate
-
additional information
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
-
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
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 4°C, 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
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 4°C, 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
-
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 4°C, 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
-
feedback inhibition is reduced by illumination
-
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
-
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
-
ZmnonC4-NADP-ME activity is not significantly modified by any chemical oxidant in 60 min
-
additional information
ZmnonC4-NADP-ME activity is not significantly modified by any chemical oxidant in 60 min
-
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Adenocarcinoma
Arginine Methylation of MDH1 by CARM1 Inhibits Glutamine Metabolism and Suppresses Pancreatic Cancer.
Adenocarcinoma
[Oxidoreductase activity in the cells of stomach cancer]
Breast Neoplasms
Identification of genes with altered expression in medullary breast cancer vs. ductal breast cancer and normal breast epithelia.
Breast Neoplasms
Malic Enzyme 1 Indicates Worse Prognosis in Breast Cancer and Promotes Metastasis by Manipulating Reactive Oxygen Species.
Carcinogenesis
MicroRNA-30a attenuates mutant KRAS-driven colorectal tumorigenesis via direct suppression of ME1.
Carcinoma
Down-regulation of malic enzyme 1 and 2: Sensitizing head and neck squamous cell carcinoma cells to therapy-induced senescence.
Carcinoma
Malic Enzyme 1 Is Associated with Tumor Budding in Oral Squamous Cell Carcinomas.
Carcinoma, Hepatocellular
Hydroperoxide-stimulated release of calcium from rat liver and AS-30D hepatoma mitochondria.
Carcinoma, Hepatocellular
Malic enzyme 1 induces epithelial-mesenchymal transition and indicates poor prognosis in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Proportional activities of glycerol kinase and glycerol 3-phosphate dehydrogenase in rat hepatomas.
Carcinoma, Non-Small-Cell Lung
Mutant KRAS associated malic enzyme 1 expression is a predictive marker for radiation therapy response in non-small cell lung cancer.
Carcinoma, Squamous Cell
Down-regulation of malic enzyme 1 and 2: Sensitizing head and neck squamous cell carcinoma cells to therapy-induced senescence.
Cholangiocarcinoma
Malic enzyme 1 is a potential marker of combined hepatocellular cholangiocarcinoma, subtype with stem-cell features, intermediate-cell type.
Colonic Neoplasms
The HMGB1 protein induces a metabolic type of tumour cell death by blocking aerobic respiration.
Dehydration
Implications of terminal oxidase function in regulation of salicylic acid on soybean seedling photosynthetic performance under water stress.
Dehydration
Induced expression of the gene for NADP-malic enzyme in leaves of Aloe vera L. under salt stress.
Dehydration
Photosynthetic and anatomical characteristics in the C4crassulacean acid metabolism-cycling plant Portulaca grandiflora.
Dehydration
The activities of PEP carboxylase and the C(4) acid decarboxylases are little changed by drought stress in three C(4) grasses of different subtypes.
Diabetes Mellitus, Experimental
[Activity of NAD- and NADP-dependent malate dehydrogenase isoenzymes in the myocardium of rabbits with alloxan diabetes]
Diabetes Mellitus, Experimental
[Antagonism in the action of hydrocortisone and insulin in vivo on enzymes of pyruvate and malate metabolism in adipose tissue]
Dwarfism
Plastidial NAD-dependent malate dehydrogenase is critical for embryo development and heterotrophic metabolism in Arabidopsis.
Friedreich Ataxia
Skeletal muscle NAD+(P) and NADP+-dependent malic enzyme in Friedreich's ataxia.
Hypertriglyceridemia
Regulation of gene expression and activity of malic enzyme in liver of hereditary hypertriglyceridemic (hHTG) insulin resistant rat: effect of dietary sucrose and marine fish oil.
Hypokinesia
[Oxidative enzyme activity of the tricarboxylic acid cycle in rat skeletal muscles in hypokinesia]
Hypothyroidism
Changes of activity and kinetics of certain liver and heart enzymes of hypothyroid and T(3)-treated rats.
Infections
Activities of key enzymes in the C4 pathway and anatomy of sugarcane infected by Leifsoniaxyli subsp. xyli.
Infections
Iron- and Reactive Oxygen Species-Dependent Ferroptotic Cell Death in Rice-Magnaporthe oryzae Interactions.
Infections
Loss of cytosolic NADP-malic enzyme 2 in Arabidopsis thaliana is associated with enhanced susceptibility to Colletotrichum higginsianum.
Intestinal Volvulus
Inhibition of NADP-linked malic enzyme from Onchocerca volvulus and Dirofilaria immitis by suramin.
Lung Neoplasms
Mutant KRAS associated malic enzyme 1 expression is a predictive marker for radiation therapy response in non-small cell lung cancer.
malate dehydrogenase deficiency
Plastidial NAD-dependent malate dehydrogenase is critical for embryo development and heterotrophic metabolism in Arabidopsis.
Melanoma
Gene Expression Profiles of Adult Peripheral and Cord Blood Mononuclear Cells Altered by Lipopolysaccharide.
Nasopharyngeal Carcinoma
Repressing malic enzyme 1 redirects glucose metabolism, unbalances the redox state, and attenuates migratory and invasive abilities in nasopharyngeal carcinoma cell lines.
Neoplasm Metastasis
Malic Enzyme 1 Indicates Worse Prognosis in Breast Cancer and Promotes Metastasis by Manipulating Reactive Oxygen Species.
Neoplasm Metastasis
miR-885-5p Inhibits Invasion and Metastasis in Gastric Cancer by Targeting Malic Enzyme 1.
Neoplasms
Caffeic Acid Targets AMPK Signaling and Regulates Tricarboxylic Acid Cycle Anaplerosis while Metformin Downregulates HIF-1?-Induced Glycolytic Enzymes in Human Cervical Squamous Cell Carcinoma Lines.
Neoplasms
Dynamic Description of the Catalytic Cycle of Malate Enzyme?Stereoselective Recognition of Substrate, Chemical Reaction and Ligand Release.
Neoplasms
Effects of ME3 on the proliferation, invasion and metastasis of pancreatic cancer cells through epithelial-mesenchymal transition.
Neoplasms
Gene Expression Profiles of Adult Peripheral and Cord Blood Mononuclear Cells Altered by Lipopolysaccharide.
Neoplasms
Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli.
Neoplasms
Inhibition of malic enzyme 1 disrupts cellular metabolism and leads to vulnerability in cancer cells in glucose-restricted conditions.
Neoplasms
Interleukin-12 administration is more effective for preventing metastasis than for inhibiting primary established tumors in a murine model of spontaneous hepatic metastasis.
Neoplasms
Malic enzyme 1 (ME1) in the biology of cancer: it is not just intermediary metabolism.
Neoplasms
Malic enzyme 1 (ME1) is a potential oncogene in gastric cancer cells and is associated with poor survival of gastric cancer patients.
Neoplasms
Malic Enzyme 1 Is Associated with Tumor Budding in Oral Squamous Cell Carcinomas.
Neoplasms
Metformin and caffeic acid regulate metabolic reprogramming in human cervical carcinoma SiHa/HTB-35 cells and augment anticancer activity of Cisplatin via cell cycle regulation.
Neoplasms
Mutant KRAS associated malic enzyme 1 expression is a predictive marker for radiation therapy response in non-small cell lung cancer.
Neoplasms
[Oxidoreductase activity in the cells of stomach cancer]
Obesity
[Obesity, malic enzyme and aging--an animal experiment study]
Pancreatic Neoplasms
Dissecting cell-type-specific metabolism in pancreatic ductal adenocarcinoma.
Squamous Cell Carcinoma of Head and Neck
Down-regulation of malic enzyme 1 and 2: Sensitizing head and neck squamous cell carcinoma cells to therapy-induced senescence.
Squamous Cell Carcinoma of Head and Neck
Malic Enzyme 1 Is Associated with Tumor Budding in Oral Squamous Cell Carcinomas.
Starvation
The effect of starvation and refeeding on lipogenic enzymes in mammary glands and livers of lactating rats.
Stomach Neoplasms
Malic enzyme 1 (ME1) is a potential oncogene in gastric cancer cells and is associated with poor survival of gastric cancer patients.
Stomach Neoplasms
miR-885-5p Inhibits Invasion and Metastasis in Gastric Cancer by Targeting Malic Enzyme 1.
Thiamine Deficiency
Lipogenesis in the brain of thiamine-deficient rat pups.
Urinary Bladder Neoplasms
Tumor-suppressing effects of microRNA-612 in bladder cancer cells by targeting malic enzyme 1 expression.
Virus Diseases
Effect of Potato Virus Y on the NADP-Malic Enzyme from Nicotiana tabacum L.: mRNA, Expressed Protein and Activity.
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additional information
additional information
-
0.00014
(S)-malate
pH 8.0, 30°C, mutant C246A
0.00015
(S)-malate
pH 7.0, 30°C, wild-type, treated with dithiothreitol
0.00017
(S)-malate
pH 8.0, 30°C, wild-type, treated with diamide
0.00039
(S)-malate
pH 8.0, 30°C, wild-type, treated with dithiothreitol
0.0008
(S)-malate
pH 7.0, 30°C, wild-type, treated with diamide
0.0017
(S)-malate
pH 8.0, 30°C, mutant C231A
0.00296
(S)-malate
-
pH 7.5, NADP-ME1
0.003
(S)-malate
pH 8.0, 30°C, mutant C192A
0.0033
(S)-malate
-
pH 7.5, NADP-ME2
0.0043
(S)-malate
pH 8.0, 30°C, mutant C270A
0.018
(S)-malate
-
60°C, 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, 25°C, mutant enzyme D258A
0.065
(S)-malate
-
60°C, pH 8.0, presence of Mg2+
0.071
(S)-malate
-
pH 7.0, 60°C
0.08
(S)-malate
-
pH 7.4, 25°C, Mn2+-activated, wild-type enzyme
0.08
(S)-malate
pH 7.0, 30°C, oxidized isozyme ZmC4-NADP-ME
0.1
(S)-malate
-
pH 7.4, 25°C, mutant enzyme D235A
0.1
(S)-malate
-
pH 7.4, 25°C, 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
0.13
(S)-malate
-
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, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C246A
0.15
(S)-malate
pH 7.0, 30°C, reduced isozyme ZmC4-NADP-ME
0.17
(S)-malate
pH 8.0, 30°C, oxidized isozyme ZmC4-NADP-ME
0.19
(S)-malate
wild type enzyme, at pH 8.0 and 25°C
0.19
(S)-malate
-
at pH 8.0, temperature not specified in the publication
0.23
(S)-malate
-
pH 4.5, 25°C, wild-type enzyme
0.23
(S)-malate
-
pH 7.5, NADP-ME4
0.23
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME4
0.23
(S)-malate
-
wild type isoform C4-NADP-ME, at pH 7.0 and 25°C
0.24
(S)-malate
-
recombinant ME1, pH 7.4, temperature not specified in the publication
0.27
(S)-malate
-
pH 7.4, 25°C, Mg2+-activated, wild-type enzyme
0.27
(S)-malate
-
mutant A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.32
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication
0.32
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
0.36
(S)-malate
-
at pH 8.0, temperature not specified in the publication
0.39
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME
0.4
(S)-malate
-
mutant E314A, with NADP+, pH 7.4, 30°C
0.4
(S)-malate
-
mutant DelN/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.43
(S)-malate
-
wild type isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.44
(S)-malate
-
at pH 7.4 and 37°C
0.46
(S)-malate
-
mutant Q503E of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.47
(S)-malate
-
mutant E339A of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.47
(S)-malate
mutant enzyme S419A, at pH 8.0 and 25°C
0.47
(S)-malate
-
mutant F140I of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.49
(S)-malate
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.49
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication
0.49
(S)-malate
-
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
0.58
(S)-malate
-
mutant L544F of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.6
(S)-malate
recombinant isozyme Hvme1
0.65
(S)-malate
-
at pH 7.4 and 37°C
0.67
(S)-malate
pH 7.6, 25°C
0.68
(S)-malate
-
mutant enzyme D90A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.8
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G, at pH 7.4 and 30°C
0.8
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H, at pH 7.4 and 30°C
0.8
(S)-malate
pH 7.4, 30°C, recombinant mutant 57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G
0.8
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H
0.8
(S)-malate
pH 7.4, 30°C, recombinant mutant [51-105]_c-NADP-ME
0.81
(S)-malate
-
at pH 8.0, temperature not specified in the publication
0.83
(S)-malate
-
pH 7.5, NADP-ME3
0.83
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME3
0.84
(S)-malate
-
mutant enzyme H51A/D90A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.85
(S)-malate
-
mutant I140F of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.89
(S)-malate
-
mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.9
(S)-malate
-
mutant S346K, with NADP+, pH 7.4, 30°C
0.9
(S)-malate
mutant enzyme N59E, at pH 7.4 and 30°C
0.9
(S)-malate
pH 7.4, 30°C, recombinant mutant N59E
0.92
(S)-malate
-
mutant enzyme H142A/D568A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.95
(S)-malate
-
mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.95
(S)-malate
-
mutant DelN of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.97
(S)-malate
-
mutant enzyme D568A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.98
(S)-malate
-
mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30°C
1
(S)-malate
-
mutant E314A/S346K/K347Y/K362H, with NAD+, pH 7.4, 30°C
1
(S)-malate
-
mutant S346K/K347Y, with NADP+, pH 7.4, 30°C
1
(S)-malate
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30°C
1
(S)-malate
-
with NADP+, wild-type enzyme, pH 7.4, 30°C
1
(S)-malate
mutant enzyme S57K/N59E/E73K, at pH 7.4 and 30°C
1
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H, at pH 7.4 and 30°C
1
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K
1
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H
1.03
(S)-malate
-
mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C
1.05
(S)-malate
-
mutant DelN/I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
1.06
(S)-malate
-
activation by Mn2+
1.06
(S)-malate
-
in the presence of 10 mM Mn2+, at pH 7.4 and 25°C
1.1
(S)-malate
-
mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30°C
1.1
(S)-malate
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30°C
1.12
(S)-malate
-
mutant I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
1.2
(S)-malate
-
mutant E314A/S346K, with NADP+, pH 7.4, 30°C
1.2
(S)-malate
wild type enzyme, at pH 7.4 and 30°C
1.2
(S)-malate
mutant enzyme N59E/E73K, at pH 7.4 and 30°C
1.2
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D, at pH 7.4 and 30°C
1.2
(S)-malate
pH 7.4, 30°C, recombinant mutant N59E/E73K
1.2
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme
1.3
(S)-malate
mutant enzyme E73K, at pH 7.4 and 30°C
1.3
(S)-malate
pH 7.4, 30°C, recombinant mutant E73K
1.3
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D
1.4
(S)-malate
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30°C
1.4
(S)-malate
mutant enzyme N59E/E73K/S102D, at pH 7.4 and 30°C
1.4
(S)-malate
pH 7.4, 30°C, recombinant mutant N59E/E73K/S102D
1.46
(S)-malate
pH 7.0, isozyme NADP-ME2
1.5
(S)-malate
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30°C
1.6
(S)-malate
mutant enzyme S102D, at pH 7.4 and 30°C
1.6
(S)-malate
pH 7.4, 30°C, recombinant mutant S102D
1.7
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C231A
1.7
(S)-malate
mutant enzyme S57K, at pH 7.4 and 30°C
1.7
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K
1.8
(S)-malate
-
mutants K347Y and K362Q, with NADP+, pH 7.4, 30°C
2
(S)-malate
-
mutant E314A/S346K/K347Y/K362Q, with NAD+, pH 7.4, 30°C
2.19
(S)-malate
-
at pH 7.5 and 33°C
2.3
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication
2.3
(S)-malate
-
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
2.68
(S)-malate
mutant enzyme S419A, at pH 8.0 and 25°C
2.7
(S)-malate
-
at pH 7.0 and 30°C
2.9
(S)-malate
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30°C
2.9
(S)-malate
-
in the presence of 1 mM NADP+, at pH 8.0 and 30°C
2.96
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME1
3
(S)-malate
-
mutant E314A/S346I/K347D/K362H, with NAD+, pH 7.4, 30°C
3
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C192A
3.1
(S)-malate
recombinant NADP-ME2
3.33
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME2
3.41
(S)-malate
-
pH 7.5, recombinant MaeB
3.63
(S)-malate
-
activation by Mg2+
3.63
(S)-malate
-
in the presence of 10 mM Mg2+, at pH 7.4 and 25°C
3.7
(S)-malate
-
mutant S346K/K362Q, with NADP+, pH 7.4, 30°C
4
(S)-malate
-
mutants E314A, S346K, E314A/S346K, S346K/K362Q, and S346K/K347Y/K362Q, with NAD+, pH 7.4, 30°C
4.3
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C270A
4.9
(S)-malate
-
mutant K362H, with NADP+, pH 7.4, 30°C
5
(S)-malate
-
mutants K347Y, K362Q, and S346K/K347Y, with NAD+, pH 7.4, 30°C
5
(S)-malate
-
with NAD+, wild-type enzyme, pH 7.4, 30°C
5.5
(S)-malate
at pH 8.0, temperature not specified in the publication
5.5
(S)-malate
-
mutant S347Y/K362Q, with NADP+, pH 7.4, 30°C
5.6
(S)-malate
-
mutant E314A/S346K/K347Y/K362Q, with NADP+, pH 7.4, 30°C
6
(S)-malate
-
mutants S346K/K347Y/K362H, with NAD+, pH 7.4, 30°C
6.4
(S)-malate
pH 8.0, 30°C, recombinant enzyme
7
(S)-malate
-
mutant S346I/K347D/K362H, with NAD+, pH 7.4, 30°C
7.3
(S)-malate
-
mutant E314A/S346K/K347Y/K362H, with NADP+, pH 7.4, 30°C
8
(S)-malate
-
mutants K362H and S347Y/K362Q, with NAD+, pH 7.4, 30°C
10
(S)-malate
-
mutant S346K/K347Y/K362Q, with NADP+, pH 7.4, 30°C
11
(S)-malate
-
mutant S346K/K347Y/K362H, with NADP+, pH 7.4, 30°C
13.33
(S)-malate
-
pH 7.4, 25°C, mutant enzyme E234A
24
(S)-malate
-
mutant E314A/S346I/K347D/K362H, with NADP+, pH 7.4, 30°C
36
(S)-malate
-
mutant S346I/K347D/K362H, with NADP+, pH 7.4, 30°C
13.3
CO2
-
-
0.04
L-malate
-
-
0.041
L-malate
Pigeon
-
pH 6.5
0.12
L-malate
-
with NADP+ as cosubstrate
0.14
L-malate
-
cytosolic enzyme
0.19
L-malate
recombinant enzyme, pH 7.0
0.22
L-malate
-
pH 7.6-7.7, 25°C
0.23
L-malate
wild-type enzyme, pH 7.0
0.23
L-malate
-
wild-type enzyme, pH 8.0, 30°C
0.26
L-malate
-
pH 8.0, 30°C, light
0.28
L-malate
-
pH 8.0, 30°C, dark
0.31
L-malate
-
mutant K435L/K436L, pH 8.0, 30°C
0.39
L-malate
Pigeon
-
pH 7.5
0.5
L-malate
mutant A392G, pH 7.0
0.6
L-malate
-
cytosolic enzyme
0.666
L-malate
-
at 1.0 mM Mn2+
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, 30°C, isozyme 2
1.25
L-malate
-
mitochondrial enzyme
2.6
L-malate
-
mutant K225I, pH 8.0, 30°C
2.9
L-malate
mutant R237L, pH 7.0
2.9
L-malate
-
mutant R237L, pH 8.0, 30°C
3.3
L-malate
Pigeon
-
pH 8.5
0.25
NAD+
-
60°C, pH 8.0
0.9
NAD+
-
mutants E314A/S346K/K347Y/K362H and E314A/S346I/K347D/K362H, pH 7.4, 30°C
0.96
NAD+
pH 8.0, 70°C, recombinant mutant R221G/K228R
1.28
NAD+
pH 8.0, 70°C, recombinant mutant K228R
1.5
NAD+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30°C
1.54
NAD+
pH 8.0, 70°C, recombinant mutant R221G/K228R/I310V
1.6
NAD+
-
mutant E314A, pH 7.4, 30°C
1.9
NAD+
-
mutant K435L/K436L, pH 8.0, 30°C
2.06
NAD+
pH 8.0, 70°C, recombinant wild-type enzyme
2.29
NAD+
pH 8.0, 70°C, recombinant mutant R221G
5
NAD+
-
mutant E314A/S346K, pH 7.4, 30°C
6
NAD+
mutant A392G, pH 7.0
6.5
NAD+
-
mutant S346I/K347D/K362H, pH 7.4, 30°C
6.55
NAD+
pH 8.0, 70°C, recombinant mutant I310V
7.1
NAD+
-
mutant S346K/K347Y/K362H, pH 7.4, 30°C
8.1
NAD+
wild-type enzyme, pH 7.0
8.1
NAD+
-
wild-type enzyme, pH 8.0, 30°C
10
NAD+
-
mutant S346K/K347Y/K362Q, pH 7.4, 30°C
11
NAD+
-
mutant K347Y, pH 7.4, 30°C
11.5
NAD+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30°C
13
NAD+
-
mutant K362Q, pH 7.4, 30°C
14
NAD+
-
mutant K362H, pH 7.4, 30°C
14
NAD+
-
mutant S346K/K362Q, pH 7.4, 30°C
17
NAD+
-
mutant S346K, pH 7.4, 30°C
18
NAD+
-
mutant S346K/K347Y, pH 7.4, 30°C
18.35
NAD+
-
wild-type enzyme, pH 7.4, 30°C
18.6
NAD+
-
in 50 mM Tris-HCl (pH 7.4)
20
NAD+
-
mutant S347Y/K362Q, pH 7.4, 30°C
0.00118
NADP+
-
cytosolic enzyme
0.00171
NADP+
pH 7.3, isozyme NADP-ME1
0.00179
NADP+
-
pH 7.4, 25°C, mutant enzyme D235A
0.0018
NADP+
-
pH 7.4, 25°C, mutant enzyme E234A
0.0018
NADP+
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H, at pH 7.4 and 30°C
0.00188
NADP+
-
mitochondrial enzyme
0.0019
NADP+
wild type enzyme, at pH 7.4 and 30°C
0.0019
NADP+
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G, at pH 7.4 and 30°C
0.002
NADP+
-
mutant E314A, pH 7.4, 30°C
0.00207
NADP+
-
pH 7.4, 25°C, Mn2+-activated, wild-type enzyme
0.0023
NADP+
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H, at pH 7.4 and 30°C
0.0026
NADP+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30°C
0.0028
NADP+
pH 7.6, 25°C
0.00283
NADP+
-
pH 7.4, 25°C, mutant enzyme D257A
0.00296
NADP+
-
pH 7.4, 25°C, mutant enzyme D258A
0.003
NADP+
-
60°C, pH 8.0
0.003
NADP+
-
mutant E314A/S346K, pH 7.4, 30°C
0.0031
NADP+
mutant enzyme S57K/N59E/E73K/S102D, at pH 7.4 and 30°C
0.0034
NADP+
-
pH 4.5, 25°C, wild-type enzyme
0.0036
NADP+
pH 7.0, 30°C, oxidized isozyme ZmC4-NADP-ME
0.0036
NADP+
pH 7.0, 30°C, wild-type, treated with diamide
0.0037
NADP+
-
mutant enzyme H51A/D90A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.0039
NADP+
-
mutant enzyme D90A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.004
NADP+
-
mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.004
NADP+
-
mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.0042
NADP+
-
mutant enzyme H142A/D568A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.00429
NADP+
pH 7.0, isozyme NADP-ME2
0.0045
NADP+
mutant enzyme N59E/E73K/S102D, at pH 7.4 and 30°C
0.0045
NADP+
mutant enzyme S57K, at pH 7.4 and 30°C
0.0046
NADP+
mutant enzyme N59E/E73K, at pH 7.4 and 30°C
0.0048
NADP+
-
mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.0049
NADP+
mutant enzyme S102D, at pH 7.4 and 30°C
0.005
NADP+
-
mutant enzyme D568A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.005
NADP+
-
mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.005
NADP+
-
wild-type enzyme, pH 7.4, 30°C
0.0053
NADP+
-
in 50 mM Tris-HCl (pH 7.4)
0.0053
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C246A
0.0053
NADP+
pH 8.0, 30°C, mutant C246A
0.0065
NADP+
-
pH 7.5, NADP-ME3
0.0065
NADP+
-
pH 7.5, 30°C, isozyme NADP-ME3
0.0069
NADP+
mutant enzyme S57K/N59E/E73K, at pH 7.4 and 30°C
0.0072
NADP+
-
mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.008
NADP+
wild-type enzyme, pH 7.0
0.008
NADP+
-
wild-type enzyme, pH 8.0, 30°C
0.008
NADP+
-
at pH 8.0, temperature not specified in the publication
0.008
NADP+
pH 8.0, 70°C, recombinant wild-type enzyme
0.0082
NADP+
-
mutant F140I of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.0086
NADP+
recombinant enzyme, pH 7.0
0.0088
NADP+
pH 8.0, 30°C, oxidized isozyme ZmC4-NADP-ME
0.0088
NADP+
pH 8.0, 30°C, wild-type, treated with diamide
0.0089
NADP+
mutant enzyme N59E, at pH 7.4 and 30°C
0.009
NADP+
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30°C
0.0102
NADP+
-
pH 7.5, NADP-ME4
0.0102
NADP+
-
pH 7.5, 30°C, isozyme NADP-ME4
0.0103
NADP+
-
pH 7.6-7.7, 25°C
0.011
NADP+
-
at pH 8.0, temperature not specified in the publication
0.0123
NADP+
wild type enzyme, at pH 8.0 and 25°C
0.0125
NADP+
-
pH 7.0, 60°C
0.0125
NADP+
mutant enzyme E73K, at pH 7.4 and 30°C
0.0128
NADP+
-
mutant Q503E of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.013
NADP+
-
pH 7.3, 30°C, isozyme 2
0.013
NADP+
-
mutant S346K, pH 7.4, 30°C
0.0131
NADP+
-
mutant DelN/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.0135
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C270A
0.0135
NADP+
pH 8.0, 30°C, mutant C270A
0.014
NADP+
-
activation by Mn2+
0.0147
NADP+
pH 7.0, 30°C, reduced isozyme ZmC4-NADP-ME
0.0147
NADP+
pH 7.0, 30°C, wild-type, treated with dithiothreitol
0.0149
NADP+
-
wild type isoform C4-NADP-ME, at pH 7.0 and 25°C
0.015
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C231A
0.015
NADP+
pH 8.0, 30°C, mutant C231A
0.015
NADP+
-
mutant A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.0154
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C192A
0.0154
NADP+
pH 8.0, 30°C, mutant C192A
0.0159
NADP+
-
mutant E339A of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.0159
NADP+
-
mutant L544F of isoform C4-NADP-ME, at pH 7.0 and 25°C
0.016
NADP+
Pigeon
-
pH 7.5
0.016
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication
0.016
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
0.019
NADP+
pH 8.0, 70°C, recombinant mutant K228R
0.021
NADP+
pH 8.0, 70°C, recombinant mutant I310V
0.023
NADP+
-
at pH 7.4 and 37°C
0.023
NADP+
-
mutant DelN of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.023
NADP+
-
wild type isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.025
NADP+
-
activation by Mg2+
0.025
NADP+
pH 8.0, 70°C, recombinant mutant R221G
0.027
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication
0.027
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
0.0276
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME
0.0276
NADP+
pH 8.0, 30°C, wild-type, treated with dithiothreitol
0.03
NADP+
mutant A392G, pH 7.0
0.03
NADP+
-
mutant K347Y, pH 7.4, 30°C
0.03
NADP+
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30°C
0.032
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication
0.032
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
0.035
NADP+
-
at pH 8.0, temperature not specified in the publication
0.036
NADP+
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30°C
0.037
NADP+
mutant A387G, pH 7.0
0.038
NADP+
-
mutant I140F of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.04
NADP+
-
pH 7.0, wild-type C4-NADP-ME isozyme
0.04
NADP+
-
at pH 7.4 and 37°C
0.0412
NADP+
-
mutant I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.0415
NADP+
-
pH 7.5, recombinant MaeB
0.048
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication
0.048
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
0.0503
NADP+
-
mutant DelN/I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
0.064
NADP+
-
at pH 7.0 and 30°C
0.0721
NADP+
-
pH 7.5, NADP-ME2
0.0721
NADP+
-
pH 7.5, 30°C, isozyme NADP-ME2
0.073
NADP+
-
mutant K435L/K436L, pH 8.0, 30°C
0.075
NADP+
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30°C
0.079
NADP+
recombinant NADP-ME2
0.093
NADP+
recombinant NADP-ME2
0.1
NADP+
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30°C
0.107
NADP+
pH 8.0, 30°C, recombinant enzyme
0.12
NADP+
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30°C
0.123
NADP+
-
mutant K225I, pH 8.0, 30°C
0.14
NADP+
-
mutant S346K/K347Y, pH 7.4, 30°C
0.157
NADP+
-
at pH 8.0 and 30°C
0.1595
NADP+
mutant enzyme S419A, at pH 8.0 and 25°C
0.205
NADP+
-
pH 7.5, NADP-ME1
0.205
NADP+
-
pH 7.5, 30°C, isozyme NADP-ME1
0.244
NADP+
pH 8.0, 70°C, recombinant mutant R221G/K228R
0.29
NADP+
mutant R237L, pH 7.0
0.29
NADP+
-
mutant R237L, pH 8.0, 30°C
0.36
NADP+
-
mutant K362H, pH 7.4, 30°C
0.38
NADP+
-
at pH 7.5 and 33°C
0.384
NADP+
pH 8.0, 70°C, recombinant mutant R221G/K22P8R/I310V
0.51
NADP+
-
pH 7.0, wild-type non-C4-NADP-ME isozyme
0.76
NADP+
-
mutant K362Q, pH 7.4, 30°C
3
NADP+
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30°C
5
NADP+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30°C
6
NADP+
-
mutant S346K/K362Q, pH 7.4, 30°C
12
NADP+
-
mutant S347Y/K362Q, pH 7.4, 30°C
17
NADP+
-
mutant S346K/K347Y/K362Q, pH 7.4, 30°C
29
NADP+
-
mutants S346K/K347Y/K362H and E314A/S346I/K347D/K362H, pH 7.4, 30°C
116
NADP+
-
mutant S346I/K347D/K362H, pH 7.4, 30°C
0.0018
NADPH
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H
0.0019
NADPH
pH 7.4, 30°C, recombinant mutant 57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G
0.0019
NADPH
pH 7.4, 30°C, recombinant wild-type enzyme
0.0023
NADPH
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H
0.0027
NADPH
pH 7.4, 30°C, recombinant mutant [51-105]_c-NADP-ME
0.0031
NADPH
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D
0.0045
NADPH
pH 7.4, 30°C, recombinant mutant N59E/E73K/S102D
0.0045
NADPH
pH 7.4, 30°C, recombinant mutant S57K
0.0046
NADPH
pH 7.4, 30°C, recombinant mutant N59E/E73K
0.0049
NADPH
pH 7.4, 30°C, recombinant mutant S102D
0.0069
NADPH
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K
0.0089
NADPH
pH 7.4, 30°C, recombinant mutant N59E
0.0125
NADPH
pH 7.4, 30°C, recombinant mutant E73K
0.047
NADPH
-
at pH 7.0 and 30°C
0.5
pyruvate
pH 7.0
0.69
pyruvate
pH 7.0, isozyme NADP-ME1
1.3
pyruvate
at pH 8.0, temperature not specified in the publication
2.6
pyruvate
pH 7.0, isozyme NADP-ME2
4.3
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication
4.3
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
5.1
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication
5.1
pyruvate
-
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
5.3
pyruvate
-
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
6
pyruvate
-
at pH 7.0 and 30°C
7.6
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication
7.6
pyruvate
-
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, 30°C, isozyme NADP-ME1
18.1
pyruvate
pH 8.0, 30°C, recombinant enzyme
25
pyruvate
-
mitochondrial enzyme
26.3
pyruvate
-
pH 7.0, 30°C, isozyme NADP-ME4
48.2
pyruvate
-
pH 7.0, 30°C, isozyme NADP-ME3
138.9
pyruvate
-
pH 7.0, 30°C, isozyme NADP-ME2
additional information
additional information
-
kinetics of mutant enzymes, overview
-
additional information
additional information
-
kinetics of isozymes at different pH, overview
-
additional information
additional information
-
kinetics of recombinant chimeric mutant enzymes, overview
-
additional information
additional information
recombinant isozyme Hvme1, kinetics
-
additional information
additional information
recombinant isozyme Hvme1, kinetics
-
additional information
additional information
recombinant isozyme Hvme1, kinetics
-
additional information
additional information
-
recombinant isozyme Hvme1, kinetics
-
additional information
additional information
recombinant isozyme Hvme3, kinetics
-
additional information
additional information
recombinant isozyme Hvme3, kinetics
-
additional information
additional information
recombinant isozyme Hvme3, kinetics
-
additional information
additional information
-
recombinant isozyme Hvme3, kinetics
-
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
-
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
-
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
-
additional information
additional information
-
kinetics of NADP+ and (S)-malate at different NADP+ and fumarate concentrations, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
additional information
-
-
-
0.004
(S)-malate
-
pH 7.4, 25°C, mutant enzyme D235A
0.005
(S)-malate
-
pH 7.4, 25°C, mutant enzyme E234A
0.006
(S)-malate
-
pH 7.4, 25°C, mutant enzyme D258A
0.3
(S)-malate
-
pH 7.4, 25°C, Mg2+-activated, wild-type enzyme
0.3
(S)-malate
-
at pH 7.0 and 30°C
0.9
(S)-malate
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30°C
1.1
(S)-malate
-
pH 7.4, 25°C, mutant enzyme D257A
1.1
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C246A
1.6
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C270A
2 - 8
(S)-malate
mutant enzyme N59E/E73K, at pH 7.4 and 30°C
2 - 8
(S)-malate
mutant enzyme N59E/E73K/S102D, at pH 7.4 and 30°C
2 - 8
(S)-malate
pH 7.4, 30°C, recombinant mutant N59E/E73K
2 - 8
(S)-malate
pH 7.4, 30°C, recombinant mutant N59E/E73K/S102D
3 - 6
(S)-malate
pH 7.4, 30°C, recombinant mutant [51-105]_c-NADP-ME
3.55
(S)-malate
pH 7.0, 30°C, oxidized isozyme ZmC4-NADP-ME
3.6
(S)-malate
-
mutant F140I of isoform C4-NADP-ME, at pH 7.0 and 25°C
4
(S)-malate
-
mutant DelN/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
5.6
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C192A
8.35
(S)-malate
pH 7.0, 30°C, reduced isozyme ZmC4-NADP-ME
12.6
(S)-malate
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30°C
13.6
(S)-malate
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30°C
15
(S)-malate
-
pH 7.4, 25°C, Mn2+-activated, wild-type enzyme
15.7
(S)-malate
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30°C
19.1
(S)-malate
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30°C
21
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H, at pH 7.4 and 30°C
21
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H
22
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G, at pH 7.4 and 30°C
22
(S)-malate
pH 7.4, 30°C, recombinant mutant 57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G
22
(S)-malate
-
mutant DelN of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
23
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H, at pH 7.4 and 30°C
23
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H
23.2
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C231A
26.3
(S)-malate
-
wild type isoform nonC4-NADP-ME, at pH 7.0 and 25°C
27
(S)-malate
mutant enzyme N59E, at pH 7.4 and 30°C
27
(S)-malate
pH 7.4, 30°C, recombinant mutant N59E
27.4
(S)-malate
-
mutant L544F of isoform C4-NADP-ME, at pH 7.0 and 25°C
28.1
(S)-malate
-
wild type isoform C4-NADP-ME, at pH 7.0 and 25°C
28.7
(S)-malate
-
mutant E339A of isoform C4-NADP-ME, at pH 7.0 and 25°C
29
(S)-malate
mutant enzyme S102D, at pH 7.4 and 30°C
29
(S)-malate
pH 7.4, 30°C, recombinant mutant S102D
29.8
(S)-malate
-
mutant Q503E of isoform C4-NADP-ME, at pH 7.0 and 25°C
30
(S)-malate
wild type enzyme, at pH 7.4 and 30°C
30
(S)-malate
mutant enzyme E73K, at pH 7.4 and 30°C
30
(S)-malate
mutant enzyme S57K/N59E/E73K, at pH 7.4 and 30°C
30
(S)-malate
pH 7.4, 30°C, recombinant mutant E73K
30
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K
30
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme
31
(S)-malate
mutant enzyme S57K/N59E/E73K/S102D, at pH 7.4 and 30°C
31
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D
31.34
(S)-malate
-
pH 7.4, 25°C, Mn2+-activated, wild-type enzyme
32
(S)-malate
mutant enzyme S57K, at pH 7.4 and 30°C
32
(S)-malate
pH 7.4, 30°C, recombinant mutant S57K
32.1
(S)-malate
-
mutant A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
34.83
(S)-malate
-
pH 7.4, 25°C, Mg2+-activated, wild-type enzyme
36.7
(S)-malate
-
mutant I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
38.7
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME1
39.6
(S)-malate
-
mutant I140F of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
46.44
(S)-malate
-
pH 7.4, 25°C, mutant enzyme E234A
84.83
(S)-malate
-
mutant enzyme H51A/D90A, in 50 mM Tris-HCl, pH 7.4, at 30°C
85.8
(S)-malate
-
mutant DelN/I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
91
(S)-malate
pH 8.0, 30°C, oxidized isozyme ZmC4-NADP-ME
91.7
(S)-malate
recombinant NADP-ME2
94.57
(S)-malate
-
mutant enzyme D90A, in 50 mM Tris-HCl, pH 7.4, at 30°C
95.53
(S)-malate
-
mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C
96.7
(S)-malate
recombinant NADP-ME3
98.03
(S)-malate
-
mutant enzyme H142A/D568A, in 50 mM Tris-HCl, pH 7.4, at 30°C
104.4
(S)-malate
-
pH 7.0, wild-type C4-NADP-ME isozyme
105.3
(S)-malate
-
mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C
106
(S)-malate
-
mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30°C
109.5
(S)-malate
-
mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30°C
110.9
(S)-malate
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30°C
113.63
(S)-malate
-
at pH 7.4 and 37°C
122.23
(S)-malate
-
at pH 7.4 and 37°C
122.7
(S)-malate
-
mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30°C
136.9
(S)-malate
-
mutant enzyme D568A, in 50 mM Tris-HCl, pH 7.4, at 30°C
140.1
(S)-malate
-
pH 4.5, 25°C, wild-type enzyme
151.3
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME4
151.7
(S)-malate
-
pH 7.0, wild-type non-C4-NADP-ME isozyme
154.3
(S)-malate
pH 7.3, isozyme NADP-ME1
177
(S)-malate
pH 7.0, isozyme NADP-ME2
181.6
(S)-malate
-
at pH 8.0, temperature not specified in the publication
198.9
(S)-malate
-
at pH 8.0, temperature not specified in the publication
242
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication
242
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
268.1
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME3
269
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME
275.7
(S)-malate
-
at pH 8.0, temperature not specified in the publication
324.1
(S)-malate
-
pH 7.5, 30°C, isozyme NADP-ME2
327
(S)-malate
-
at pH 8.0 and 30°C
376
(S)-malate
-
pH 8.0, 60°C
518
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication
518
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
683
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication
683
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
1132
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication
1132
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
160
L-malate
-
-
582
L-malate
-
assuming an octameric oligomerization state
3.37
NAD+
pH 8.0, 70°C, recombinant mutant K228R
4.69
NAD+
pH 8.0, 70°C, recombinant wild-type enzyme
7.44
NAD+
pH 8.0, 70°C, recombinant mutant R221G/K228R
12.7
NAD+
pH 8.0, 70°C, recombinant mutant R221G
13.5
NAD+
wild-type enzyme, pH 7.0
13.5
NAD+
-
wild-type enzyme, pH 8.0, 30°C
18.4
NAD+
-
mutant K435L/K436L, pH 8.0, 30°C
21.3
NAD+
pH 8.0, 70°C, recombinant mutant R221G/K228R/I310V
22
NAD+
-
mutant S346K, pH 7.4, 30°C
28.9
NAD+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30°C
34.18
NAD+
-
in 50 mM Tris-HCl (pH 7.4)
37.7
NAD+
pH 8.0, 70°C, recombinant mutant I310V
40
NAD+
-
mutant K347Y, pH 7.4, 30°C
40.6
NAD+
mutant A392G, pH 7.0
51
NAD+
-
wild-type enzyme, pH 7.4, 30°C
53
NAD+
-
mutant S347Y/K362Q, pH 7.4, 30°C
60
NAD+
-
mutant K362Q, pH 7.4, 30°C
65
NAD+
-
mutant S346K/K347Y, pH 7.4, 30°C
108
NAD+
-
mutant K362H, pH 7.4, 30°C
110
NAD+
-
mutant S346K/K362Q, pH 7.4, 30°C
113
NAD+
-
mutant E314A, pH 7.4, 30°C
124
NAD+
-
mutant S346K/K347Y/K362Q, pH 7.4, 30°C
131
NAD+
-
mutant S346I/K347D/K362H, pH 7.4, 30°C
145
NAD+
-
mutant E314A/S346K, pH 7.4, 30°C
166
NAD+
-
mutant E314A/S346I/K347D/K362H, pH 7.4, 30°C
208
NAD+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30°C
219
NAD+
-
mutant S346K/K347Y/K362H, pH 7.4, 30°C
258
NAD+
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30°C
0.38
NADP+
mutant R237L, pH 7.0
0.38
NADP+
-
mutant R237L, pH 8.0, 30°C
0.8
NADP+
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30°C
1.1
NADP+
-
mutant K225I, pH 8.0, 30°C
1.1
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C246A
1.1
NADP+
pH 8.0, 30°C, mutant C246A
1.3
NADP+
-
mutant S346I/K347D/K362H, pH 7.4, 30°C
1.6
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C270A
1.6
NADP+
pH 8.0, 30°C, mutant C270A
2.1
NADP+
mutant enzyme S419A, at pH 8.0 and 25°C
2.97
NADP+
pH 8.0, 70°C, recombinant mutant K228R
3.55
NADP+
pH 7.0, 30°C, oxidized isozyme ZmC4-NADP-ME
3.55
NADP+
pH 7.0, 30°C, wild-type, treated with diamide
4.2
NADP+
mutant A387G, pH 7.0
5.6
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C192A
5.6
NADP+
pH 8.0, 30°C, mutant C192A
6.48
NADP+
pH 8.0, 70°C, recombinant mutant R221G/K228R
8
NADP+
-
mutant S346K/K347Y/K362H, pH 7.4, 30°C
8.3
NADP+
mutant enzyme S419A, at pH 8.0 and 25°C
8.35
NADP+
pH 7.0, 30°C, reduced isozyme ZmC4-NADP-ME
8.35
NADP+
pH 7.0, 30°C, wild-type, treated with dithiothreitol
12.2
NADP+
wild type enzyme, at pH 8.0 and 25°C
13.2
NADP+
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30°C
14.2
NADP+
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30°C
15
NADP+
-
mutant E314A/S346I/K347D/K362H, pH 7.4, 30°C
15
NADP+
-
mutant S346K/K347Y/K362Q, pH 7.4, 30°C
15.9
NADP+
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30°C
19.5
NADP+
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30°C
23.2
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C231A
23.2
NADP+
pH 8.0, 30°C, mutant C231A
26
NADP+
-
mutant E314A/S346K/K347Y/K362H, pH 7.4, 30°C
30.8
NADP+
recombinant enzyme, pH 7.0
31.1
NADP+
pH 8.0, 70°C, recombinant wild-type enzyme
38.7
NADP+
-
pH 7.5, NADP-ME1
40.1
NADP+
pH 8.0, 70°C, recombinant mutant R221G/K22P8R/I310V
42.6
NADP+
pH 8.0, 70°C, recombinant mutant R221G
43.4
NADP+
pH 8.0, 70°C, recombinant mutant I310V
51
NADP+
-
mutant E314A/S346K/K347Y/K362Q, pH 7.4, 30°C
66.6
NADP+
-
pH 7.5, recombinant MaeB
78
NADP+
-
mutant S347Y/K362Q, pH 7.4, 30°C
88.3
NADP+
recombinant NADP-ME2
91
NADP+
pH 8.0, 30°C, oxidized isozyme ZmC4-NADP-ME
91
NADP+
pH 8.0, 30°C, wild-type, treated with diamide
98.3
NADP+
recombinant NADP-ME3
102
NADP+
-
mutant S346K/K347Y, pH 7.4, 30°C
106.93
NADP+
-
at pH 7.4 and 37°C
110
NADP+
-
mutant E314A, pH 7.4, 30°C
112
NADP+
-
mutant S346K/K362Q, pH 7.4, 30°C
113.2
NADP+
-
in 50 mM Tris-HCl (pH 7.4)
119.89
NADP+
-
at pH 7.4 and 37°C
121
NADP+
-
mutant K347Y, pH 7.4, 30°C
126
NADP+
-
wild-type enzyme, pH 7.4, 30°C
129
NADP+
-
mutant S346K, pH 7.4, 30°C
132
NADP+
-
mutant K362Q, pH 7.4, 30°C
135.8
NADP+
-
wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30°C
137
NADP+
-
mutant E314A/S346K, pH 7.4, 30°C
149
NADP+
-
mutant K362H, pH 7.4, 30°C
151.3
NADP+
-
pH 7.5, NADP-ME4
181.1
NADP+
-
mutant K435L/K436L, pH 8.0, 30°C
200.3
NADP+
mutant A392G, pH 7.0
201.3
NADP+
wild-type enzyme, pH 7.0
201.3
NADP+
-
wild-type enzyme, pH 8.0, 30°C
268.1
NADP+
-
pH 7.5, NADP-ME3
269
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME
269
NADP+
pH 8.0, 30°C, wild-type, treated with dithiothreitol
284
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication
284
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
324.1
NADP+
-
pH 7.5, NADP-ME2
504
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication
504
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
691
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication
691
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
1206
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication
1206
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
4670
NADP+
-
pH 7.5, NADP-ME2
0.067
pyruvate
-
at pH 7.0 and 30°C
3
pyruvate
-
at pH 8.0 and 30°C
8.3
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication
8.3
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
16.5
pyruvate
-
pH 7.0, 30°C, isozyme NADP-ME1
21.6
pyruvate
pH 7.0, isozyme NADP-ME2
34
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication
34
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
39
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication
39
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
75
pyruvate
-
pH 7.0, 30°C, isozyme NADP-ME2
113
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication
113
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
158.4
pyruvate
pH 7.0, isozyme NADP-ME1
237
pyruvate
-
pH 7.0, 30°C, isozyme NADP-ME3
284.1
pyruvate
-
pH 7.0, 30°C, isozyme NADP-ME4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.117
(S)-malate
-
at pH 7.0 and 30°C
0.14
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C246A
0.37
(S)-malate
pH 8.0, 30°C, mutant C270A
0.9
(S)-malate
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30°C
1.7
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C231A
1.9
(S)-malate
pH 8.0, 30°C, mutant C192A
3
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C192A
4.3
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C270A
4.3
(S)-malate
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30°C
7.7
(S)-malate
-
mutant F140I of isoform C4-NADP-ME, at pH 7.0 and 25°C
7.8
(S)-malate
pH 8.0, 30°C, mutant C246A
9.1
(S)-malate
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30°C
10
(S)-malate
-
mutant DelN/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
11
(S)-malate
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30°C
13.6
(S)-malate
pH 8.0, 30°C, mutant C231A
23.2
(S)-malate
-
mutant DelN of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
32.8
(S)-malate
-
mutant I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
46.6
(S)-malate
-
mutant I140F of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
47.2
(S)-malate
-
mutant L544F of isoform C4-NADP-ME, at pH 7.0 and 25°C
61.1
(S)-malate
-
mutant E339A of isoform C4-NADP-ME, at pH 7.0 and 25°C
62.6
(S)-malate
-
wild type isoform nonC4-NADP-ME, at pH 7.0 and 25°C
64.8
(S)-malate
-
mutant Q503E of isoform C4-NADP-ME, at pH 7.0 and 25°C
81.7
(S)-malate
-
mutant DelN/I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
118.9
(S)-malate
-
mutant A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C
122.2
(S)-malate
-
wild type isoform C4-NADP-ME, at pH 7.0 and 25°C
170
(S)-malate
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30°C
188
(S)-malate
-
at pH 7.4 and 37°C
224.1
(S)-malate
-
at pH 8.0, temperature not specified in the publication
258
(S)-malate
-
at pH 7.4 and 37°C
297
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication
297
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
494
(S)-malate
-
isozyme ME2, pH 7.4, temperature not specified in the publication
494
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
689.7
(S)-malate
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME
690
(S)-malate
pH 8.0, 30°C, wild-type, treated with dithiothreitol
765.7
(S)-malate
-
at pH 8.0, temperature not specified in the publication
1047
(S)-malate
-
at pH 8.0, temperature not specified in the publication
3536
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication
3536
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
3981
(S)-malate
-
isozyme ME1, pH 7.4, temperature not specified in the publication
3981
(S)-malate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
2.27
NAD+
pH 8.0, 70°C, recombinant wild-type enzyme
2.64
NAD+
pH 8.0, 70°C, recombinant mutant K228R
2.8
NAD+
-
wild-type enzyme, pH 7.4, 30°C
5.57
NAD+
pH 8.0, 70°C, recombinant mutant R221G
5.76
NAD+
pH 8.0, 70°C, recombinant mutant I310V
7.72
NAD+
pH 8.0, 70°C, recombinant mutant R221G/K228R
13.8
NAD+
pH 8.0, 70°C, recombinant mutant R221G/K228R/I310V
0.12
NADP+
pH 8.0, 30°C, mutant C270A
0.21
NADP+
pH 8.0, 30°C, mutant C246A
0.36
NADP+
pH 8.0, 30°C, mutant C192A
0.37
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C270A
1.5
NADP+
pH 8.0, 30°C, mutant C231A
1.86
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C192A
7.86
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C246A
9.7
NADP+
pH 8.0, 30°C, wild-type, treated with dithiothreitol
13.64
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C231A
22
NADP+
-
recombinant isozyme PtNADP-ME1, pH 7.5, 30°C
27.5
NADP+
pH 8.0, 70°C, recombinant mutant R221G/K228R
104
NADP+
pH 8.0, 70°C, recombinant mutant R221G/K22P8R/I310V
110
NADP+
-
recombinant isozyme PtNADP-ME2, pH 7.5, 30°C
140
NADP+
-
recombinant isozyme PtNADP-ME3, pH 7.5, 30°C
156
NADP+
pH 8.0, 70°C, recombinant mutant K228R
210
NADP+
-
recombinant isozyme PtNADP-ME4, pH 7.5, 30°C
650
NADP+
-
recombinant isozyme PtNADP-ME5, pH 7.5, 30°C
1700
NADP+
pH 8.0, 70°C, recombinant mutant R221G
2070
NADP+
pH 8.0, 70°C, recombinant mutant I310V
3000
NADP+
-
at pH 7.4 and 37°C
3760
NADP+
pH 8.0, 70°C, recombinant wild-type enzyme
4650
NADP+
-
at pH 7.4 and 37°C
5800
NADP+
-
at pH 8.0, temperature not specified in the publication
9746
NADP+
pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME
17780
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication
17780
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
18680
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication
18680
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
21600
NADP+
-
isozyme ME2, pH 7.4, temperature not specified in the publication
21600
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
25170
NADP+
-
isozyme ME1, pH 7.4, temperature not specified in the publication
25170
NADP+
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
27900
NADP+
-
at pH 8.0, temperature not specified in the publication
36000
NADP+
-
wild-type enzyme, pH 7.4, 30°C
61200
NADP+
-
at pH 8.0, temperature not specified in the publication
0.01
pyruvate
-
at pH 7.0 and 30°C
1.1
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication
1.1
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
6
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication
6
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
8
pyruvate
-
isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication
8
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+
26
pyruvate
-
isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication
26
pyruvate
-
pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+
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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)
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
evolution
-
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
-
evolution
-
the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily
-
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
-
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
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
-
deletion of the enzyme gene in a Magnaporthe oryzae-resistant rice cultivar disrupts innate immunity against the rice blast fungus
malfunction
-
down-regulation of isoform ME2 reciprocally activates p53 through distinct Mdm2 and AMP-activated kinase -mediated mechanisms in a feed-forward manner, bolstering this pathway and enhancing p53 activation. Down-regulation of isoform ME2 also modulates the outcome of p53 activation leading to strong induction of senescence, but not apoptosis
malfunction
-
knockdown of malic enzyme 2 suppresses lung tumor growth, induces differentiation and impacts PI3K/AKT signaling. In the A-549 non-small cell lung cancer cell line, ME2 depletion inhibits cell proliferation and induces cell death and differentiation, accompanied by increased reactive oxygen species (ROS) and NADP1/NADPH ratio, a drop in ATP, and increased sensitivity to cisplatin. ME2 knockdown impacts phosphoinositide-dependent protein kinase 1 (PDK1) and phosphatase and tensin homolog (PTEN) expression, leading to AKT inhibition. Depletion of ME2 leads to malate accumulation and pyruvate decrease, and exogenous cell permeable dimethyl-malate mimics the ME2 knockdown phenotype. Both ME2 knockdown and dimethyl-malate treatment reduce A-549 cell growth in vivo. Survival of ME2 knockdown cells is exquisitely dependent on glucose. Phenotype, overview
malfunction
knockdown of ME3, but not ME1 or ME2 (both EC 1.1.1.39) alone or together, inhibits insulin release stimulated by glucose, pyruvate or 2-aminobicyclo [2,2,1]heptane-2-carboxylic acid-plus-glutamine
malfunction
-
the decrease of malic enzyme activity is consistent with the cease of lipid accumulation. Reduction of malic enzyme activity is not due to the downregulation of malic enzyme but the feedback repression after nitrogen starvation. Malic enzyme activity recovered by adding ammonium tartrate even at a high cyclohexamide concentration
malfunction
the deprivation of malic enzyme activity limited the lipid accumulation
malfunction
enzyme inactivation improves the anaerobic production of four-carbon dicarboxylic acids by recombinant Escherichia coli strains expressing oxaloacetate-forming pyruvate carboxylase
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
malfunction
-
suppressing increased enzyme expression in hypertrophied rat hearts reduces pyruvate carboxylation thereby normalizing anaplerosis, restoring GSH content, and reducing lactate accumulation. Reducing the enzyme induces favorable metabolic shifts for carbohydrate oxidation, improving intracellular redox state and enhanced cardiac performance in pathological hypertrophy
malfunction
-
the decrease of malic enzyme activity is consistent with the cease of lipid accumulation. Reduction of malic enzyme activity is not due to the downregulation of malic enzyme but the feedback repression after nitrogen starvation. Malic enzyme activity recovered by adding ammonium tartrate even at a high cyclohexamide concentration
-
malfunction
-
the deprivation of malic enzyme activity limited the lipid accumulation
-
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
-
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
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
metabolism
the enzyme plays a role during fatty acid synthesis
metabolism
during adipocyte differentiation, there is coordinate upregulation of ATP citrate lyase and cytosolic malic enzyme (ME1), which together with cytosolic malate dehydrogenase and at the expense of 1 ATP molecule, can convert citrate and NADH into acetyl-CoA, NADPH and pyruvate
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
-
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
metabolism
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation. The enzyme serves as the sole source of NADPH for fatty acid biosynthesis
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
metabolism
-
the enzyme plays a role during fatty acid synthesis
-
metabolism
-
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
-
metabolism
-
the enzyme is involved in the fatty acid biosynthesis
-
metabolism
-
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation
-
metabolism
-
the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation. The enzyme serves as the sole source of NADPH for fatty acid biosynthesis
-
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
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
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
-
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
Mnium undulatum
-
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
-
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
-
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
-
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
-
NADP-malic enzyme is the primary enzyme decarboxylating malate in bundle sheath cells to supply CO2 to Rubisco
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
-
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
-
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
the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
physiological function
-
enzyme activation in fruit exposed to 20% (v/v) CO2 provides NADPH for glutathione regeneration by glutathione reductase, thereby conferring protection against the cellular damage caused by low temperatures or excessive high CO2 levels
physiological function
-
malic enzyme overexpression during the larval period lengthenes the lifespan of Drosophila melanogaster. Metabolic changes mediated by the enzyme during development are related to the control of reactive oxygen species tolerance and the longevity of Drosophila
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
physiological function
-
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. Activity of isoform E is intensely associated with the profiles and the level of lipid biosynthesis in N-limitation condition, while isoform D is reduced as lipid is produced. With ammonium tartrate as nitrogen source, activity of isoform D is pronounced, while isoform E is very low. Isoform E is the crucial regulator of lipid accumulation in strain 2A1
physiological function
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. The final governance over the malic enzyme activity is supposed to be the supply of its substrate
physiological function
mitochondrial NADP malic enzyme is necessary for insulin release
physiological function
NADP+-malic enzyme may not be the sole rate-limiting enzyme, but does play a role, during fatty acid synthesis in oleaginous fungi
physiological function
-
pivotal role of malic enzyme in enhancing oil accumulation in green microalga Chlorella pyrenoidosa. The enzyme promte fatty acid biosynthesis
physiological function
significance of malic enzyme in fat synthesis. Malic enzyme is the main NADPH source in normoxic 3T3-L1 adipocytes, with total NADPH production more than double that from the oxidative pentose phosphate pathway
physiological function
-
enzyme overexpression can simultaneously improve the carbon concentration and reducing power in cells, thereby increasing the lipid and fatty acid methyl ester yields of Nannochloropsis salina
physiological function
-
enzyme overexpression in cancer cells leads to decreased cellular differentiation, enhanced invasiveness associated with cellular differentiation proteins, modulation of AKT and AMPK signalling, modulation of p53 levels and its downstream target p21, increased cellular growth rate and proliferation with decreasing apoptotic rate, as well as modulation of glutamine oxidation via the Krebs cycle
physiological function
-
enzyme overexpression of Sorghum bicolor NADP-ME in Arabidopsis thaliana increases salt tolerance and alleviates photosystem II and photosystem I photoinhibition under salt stress by improving photosynthetic capacity
physiological function
-
isoform ME1 contributes to increased internal malate and citrate concentrations and their external efflux to confer higher aluminium resistance
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 is associated with resistance against the root-knot nematode Meloidogyne javanica in field pea
physiological function
-
the enzyme is important for survival of Leishmania amastigotes within host macrophages
physiological function
-
the enzyme plays an important role in maintaining the supply of NADPH during pepper fruit ripening
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)
physiological function
-
NADP+-malic enzyme may not be the sole rate-limiting enzyme, but does play a role, during fatty acid synthesis in oleaginous fungi
-
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
-
physiological function
-
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
-
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. Activity of isoform E is intensely associated with the profiles and the level of lipid biosynthesis in N-limitation condition, while isoform D is reduced as lipid is produced. With ammonium tartrate as nitrogen source, activity of isoform D is pronounced, while isoform E is very low. Isoform E is the crucial regulator of lipid accumulation in strain 2A1
-
physiological function
-
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation
-
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
-
physiological function
-
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
-
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
-
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
-
malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. The final governance over the malic enzyme activity is supposed to be the supply of its substrate
-
physiological function
-
the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
-
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
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
additional information
-
fatty acid composition analysis of wild-type and mutant overexpressing strains, overview
additional information
the molecular basis for the different allosteric properties and quaternary structural stability of m-NAD(P)-ME, EC 1.1.1.39 and c-NADP-ME, EC 1.1.1.40. The structural features near the fumarate binding site and the dimer interface are highly related to the quaternary structural stability of c-NADP-ME and m-NAD(P)-ME
additional information
-
the molecular basis for the different allosteric properties and quaternary structural stability of m-NAD(P)-ME, EC 1.1.1.39 and c-NADP-ME, EC 1.1.1.40. The structural features near the fumarate binding site and the dimer interface are highly related to the quaternary structural stability of c-NADP-ME and m-NAD(P)-ME
additional information
-
tracing carbon flux through malic enzyme, overview
additional information
tracing carbon flux through malic enzyme, overview
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C99S
-
turnover number decreases 3fold and Km for malate increases 4fold
R70Q
-
kinetic parameters are similar except for a slightly lower turnover number and higher Km for L-malate
D235A
-
turnover number is 783.5fold lower than wild-type value
D257A
-
turnover number is 28.5fold lower than wild-type value
D258A
-
turnover number is 522fold lower than wild-type value
E234A
-
turnover number is 1.3fold higher than wild-type value
K162A
-
site-directed mutagenesis, the mutation does not affect Mn2+ binding of the mutant enzyme, but kcat is 27000fold reduced compared to the wild-type enzyme, NH4Cl shows no rescue of the pyruvate reduction in the K162A mutant, while for oxaloacetate decarboxylation, ammonium chloride demonstrated a maximum restoration of 3.5fold at 1 mM, and its rescue efficiency decreases with increasing concentration
K162Q
-
site-directed mutagenesis, the mutation does not affect Mn2+ binding of the mutant enzyme, but kcat is 3500fold reduced compared to the wild-type enzyme
K162R
-
site-directed mutagenesis,the mutation does not affect Mn2+ binding of the mutant enzyme, but kcat is 125fold reduced compared to the wild-type enzyme
K362A
-
site-directed mutagenesis, 70fold increased Km for NADP+ compared to the wild-type enzyme
W252A
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252F
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252H
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252I
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
W252S
-
site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin
Y91F
-
site-directed mutagenesis, the mutation does not affect Mn2+ binding of the mutant enzyme, the mutant shows a 25fold increase and a 3fold decrease in the Km values for (S)-malate and NADP+ respectively, and its kcat value is decreased by 200fold compared to wild-type enzyme
D139A
-
dimeric mutant enzyme with reduced activity compared to the wild type enzyme
D568A
-
dimeric or tetrameric mutant enzyme with increased activity compared to the wild type enzyme
D90A
-
dimeric or tetrameric mutant enzyme with reduced activity compared to the wild type enzyme
E314A
-
site-directed mutagenesis
E314A/S346I/K347D/K362H
-
site-directed mutagenesis, the quadruple mutant enzyme is a mainly NAD+-utilizing enzyme by a considerable increase in catalysis using NAD+ as the cofactor, shows increased inhibition by ATP compared to the wild-type enzyme
E314A/S346K
-
site-directed mutagenesis
E314A/S346K/K347Y/K362H
-
site-directed mutagenesis, the quadruple mutant enzyme is a mainly NAD+-utilizing enzyme by a considerable increase in catalysis using NAD+ as the cofactor, shows increased inhibition by ATP compared to the wild-type enzyme
E314A/S346K/K347Y/K362Q
-
site-directed mutagenesis, the quadruple mutant enzyme is a mainly NAD+-utilizing enzyme by a considerable increase in catalysis using NAD+ as the cofactor, shows increased inhibition by ATP compared to the wild-type enzyme
H51A
-
dimeric or tetrameric mutant enzyme with wild type activity
K347Y
-
site-directed mutagenesis, the mutant enzyme shows a 5fold increased Km for NADP+ compared to the wild-type enzyme
K347Y/K362Q
-
site-directed mutagenesis
K362H
-
site-directed mutagenesis
K362Q
-
site-directed mutagenesis, the mutant enzyme displays a significant, over 140fold elevation in Km,NADP value compared with that of wild-type c-NADP-ME but no significant changes in the kcat,NADP value
K57S/E59N/K73E/D102S
site-directed mutagenesis, the mutant is primarily monomeric with some dimer formation
S346I/K347D/K362H
-
site-directed mutagenesis, the triple c-NADP-ME mutant does not show significant reduction in its Km,NAD values. This mutant exclusively utilizes NAD+ as its cofactor
S346K
-
site-directed mutagenesis, site-directed mutagenesis, the mutant enzyme shows a 3fold increased Km for NADP+ compared to the wild-type enzyme
S346K/K347Y
-
site-directed mutagenesis, the double mutant enzyme shows a 30fold increased Km for NADP+ compared to the wild-type enzyme
S346K/K347Y/K362H
-
site-directed mutagenesis, the triple c-NADP-ME mutant does not show significant reduction in its Km,NAD values, but displays an enhanced value for kcat,NAD
S346K/K347Y/K362Q
-
site-directed mutagenesis, the triple c-NADP-ME mutant does not show significant reduction in its Km,NAD values
S346K/K362Q
-
site-directed mutagenesis
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H
moe
-
enzyme inactivation by shRNA, ME1 activity is reduced by 62% and glucose-induced insulin secretion is decreased
I310V
site-directed mutagenesis
K228R
site-directed mutagenesis
R221G
site-directed mutagenesis
R221G/K228R
site-directed mutagenesis, substitution of Arg221 with Gly is responsible for the shift in reaction specificity
R221G/K228R/I310V
site-directed mutagenesis, the reaction specificity of the triple mutant is significantly shifted to malate production and the mutant gives a reduced amount of the byproduct than the wild-type. When the triple mutant enzyme is used as a catalyst for pyruvate carboxylation with NADH, the enzyme gives 1.2times higher concentration of malate than the wild-type with NADPH. Single-point mutation analysis reveals that the substitution of Arg221 with Gly is responsible for the shift in reaction specificity
V393V
1179 GTC /GTT results in a synonymous mutation of V393V
A339E
-
the mutant of isoform nonC4-NADP-ME shows increased catalytic efficiency compared to the wild type enzyme
A387G
site directed mutagenesis, mutation at the NADP+ binding site, mutant shows 48fold decreased kcat and 4.3 and 5.8fold increased Km for NADP+ and L-malate, respectively, compared to the wild-type enzyme, no activity with NAD+
A392G
site directed mutagenesis, mutation at the NADP+ binding site, mutant shows unaltered kcat, but 3.5 and 2.6fold increased Km for NADP+ and L-malate, respectively, and increased activity with NAD+ compared to the wild-type enzyme
DelN
-
the mutant of isoform nonC4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme and is not inhibited by (S)-malate
DelN/A339E
-
the mutant of isoform nonC4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme
DelN/I140F/A339E
-
the mutant of isoform nonC4-NADP-ME shows increased catalytic efficiency compared to the wild type enzyme and is not inhibited by (S)-malate
E339A
-
the mutant of isoform C4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme and is not inhibited by (S)-malate
F140I
-
the mutant of isoform C4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme
I140F
-
the mutant of isoform nonC4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme and is not inhibited by (S)-malate
I140F/A339E
-
the mutant of isoform nonC4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme and is not inhibited by (S)-malate
K225I
-
site-directed mutagenesis, mutation of a conserved residue involved in catalysis and substrate binding, mutant shows highly reduced activity and a 10fold higher partitioning ratio of oxaloacetate and malate compared to the wild-type enzyme, preference for reduction of oxaloacetate instead of decarboxylation
K435L/K436L
-
site-directed mutagenesis, mutation of residues which are important in cofactor binding, over 6fold increased Ki for 2'-AMP, and 1.7fold decreased Ki for 5'-AMP, and increased activity with NAD+ compared to the wild-type enzyme
L544F
-
the mutant of isoform C4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme
Q503E
-
the mutant of isoform C4-NADP-ME shows reduced catalytic efficiency compared to the wild type enzyme
S419A
the variant presents 72.3% of the wild type activity
S419E
the variant presents 8.7% of the wild type activity. The mutation dramatically decreases the affinity for the cofactor, as saturation is not observed even at NADP+ concentrations as high as 5 mM
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
E73K
site-directed mutagenesis
E73K
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
H142A
-
dimeric mutant enzyme with increased activity compared to the wild type enzyme
H142A
-
site-directed mutagenesis, a dimeric tetramer interface mutant
H142A/D568A
-
dimeric mutant enzyme with reduced activity compared to the wild type enzyme
H142A/D568A
-
site-directed mutagenesis, a dimeric tetramer interface mutant. The mutant dimer completely dissociates into monomers after a 2.5 M urea treatment
H51A/D139A
-
dimeric or tetrameric mutant enzyme with reduced activity compared to the wild type enzyme
H51A/D139A
-
site-directed mutagenesis, a dimeric dimer interface mutant
H51A/D90A
-
dimeric or tetrameric mutant enzyme with reduced activity compared to the wild type enzyme
H51A/D90A
-
site-directed mutagenesis, a dimeric dimer interface mutant. The mutant dimer completely dissociates into monomers after a 1.5 M urea treatment
N59E
site-directed mutagenesis
N59E
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
N59E/E73K
site-directed mutagenesis
N59E/E73K
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
N59E/E73K/S102D
site-directed mutagenesis
N59E/E73K/S102D
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
S102D
site-directed mutagenesis
S102D
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
S57K
site-directed mutagenesis
S57K
the mutant shows increased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
S57K/N59E/E73K
site-directed mutagenesis
S57K/N59E/E73K
the mutant shows wild type turnover numbers for (S)-malate and NADP+
S57K/N59E/E73K/S102D
the mutant shows increased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
S57K/N59E/E73K/S102D
site-directed mutagenesis, the mutant is tetrameric
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G
site-directed mutagenesis, the mutant is tetrameric
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H
site-directed mutagenesis
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H
site-directed mutagenesis
S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H
the mutant shows decreased turnover numbers for (S)-malate and NADP+ compared to the wild type enzyme
W572A
-
dimeric mutant enzyme with slightly reduced activity compared to the wild type enzyme
W572A
-
site-directed mutagenesis, a dimeric tetramer interface mutant
C192A
site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, the mutant displays lower malate affinity than the wild-type enzyme
C192A
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Unlike wild-type, activity is not significantly changed in presence of oxidant iodosobenzoate
C231A
site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, the mutant displays lower malate affinity than the wild-type enzyme
C231A
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Similar to wild-type, activity decreases in presence of oxidant iodosobenzoate
C246A
site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, C246A exhibits a nearly 5fold increase in its affinity towards NADP+ and a 3fold decrease for malate compared to the wild-tpe enzyme
C246A
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Unlike wild-type, activity is not significantly changed in presence of oxidant iodosobenzoate
C270A
site-directed mutagenesis of isozyme ZmC4-NADP-ME, the mutation does not affect the tetrameric state, the mutant displays lower malate affinity than the wild-type enzyme
C270A
marked decrease in kcat value, less than 10% of wild-type, with concomitant increase in Km value for NADP+. Unlike wild-type, activity is not significantly changed in presence of oxidant iodosobenzoate
R237L
site directed mutagenesis, mutation at the NADP+ binding site, mutant shows 530fold decreased kcat and 36.3 and 15.3fold increased Km for NADP+ and L-malate, respectively, compared to the wild-type enzyme, no activity with NAD+
R237L
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site-directed mutagenesis, mutation of a conserved residue involved in catalysis and substrate binding, mutant shows and an over 100fold higher partitioning ratio of oxaloacetate and malate compared to the wild-type enzyme, preference for reduction of oxaloacetate instead of decarboxylation
additional information
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construction of deletion mutants of isozyme NADP-ME2
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
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generation of knock-out mutants nadp-me2.1 and -2.2 by Agrobacterium tumefaciens strain GV3101-mediated transformation using the vacuum infiltration method
additional information
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recombinant enzyme overexpression in Chlorella pyrenoidosa for enhanced lipid production, method, overview
additional information
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effects of enzyme overexpression on the concentration of CO2 and the C4 metabolsim in wild-type strain and strains overexpressing other anaeplerotic enzymes, phenotypes, overview
additional information
deletion of gene maeB by chromosomal homologous recombination
additional information
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deletion of gene maeB by chromosomal homologous recombination
additional information
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deletion of gene maeB by chromosomal homologous recombination
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additional information
AF288898
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression pattern and regulation, overview
additional information
AF288899
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression pattern and regulation, overview
additional information
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construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression pattern and regulation, overview
additional information
AF288898
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression patterns and regulation, overview
additional information
AF288899
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression patterns and regulation, overview
additional information
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construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei, expression patterns and regulation, overview
additional information
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generation of an antisense construct targeting the C4 isoform of NADP-malic enzyme, transformation of Flaveria bidentis via Agrobacterium tumefaciens, transgenic Flaveria bidentis plants exhibit a 34% to 75% reduction in NADP-ME activity relative to the wild-type with no visible growth phenotype. In transgenic plants, CO2 assimilation rates at high intercellular CO2 are significantly reduced, whereas the in vitro activities of both phosphoenolpyruvate carboxylase and Rubisco are increased
additional information
AF288911
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs bearing parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs bearing parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
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construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs bearing parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
AF288911
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
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construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
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construction of transgenic seedlings of Flaveria bidentis, expressing heterologous constructs beasring parts of isozymes ChlME1 and ChlME2 from Flaveria trinervia and Flaveria pringlei
additional information
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ME1 overexpression results in an increased glucose-dependent rise in malate and citrate levels in INS-1 832/13 cells. Introduction of ME1 activity alters glucose-stimulated insulin secretion to a lesser degree in mouse islets than in INS-1 832/13 cells, overview. In contrast to rat, mouse beta-cells lack ME1 activity, which is suggested to explain their lack of methyl succinate-stimulated insulin secretion. Metabolic phenotypes of transfected cells, overview
additional information
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a series of E314A-containing c-NADP-ME quadruple mutants are changed to NAD+-utilizing enzymes by abrogating NADP+ binding and increasing NAD+ binding. Abolishing the repulsive effect of Glu314 in the quadruple mutants increases the binding affinity of NAD+
additional information
multiple residues corresponding to the fumarate-binding site are mutated in human c-NADP-ME to correspond to those found in human m-NAD(P)-ME, EC 1.1.1.39. No significant difference between the wild-type and mutant enzymes in Km values for NADP+ and malate, and in kcat values. A chimeric enzyme, [51-105]_c-NADP-ME, is designed to include the putative fumarate-binding site ofm-NAD(P)-ME at the dimer interface of c-NADP-ME, but the chimera remains nonallosteric
additional information
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multiple residues corresponding to the fumarate-binding site are mutated in human c-NADP-ME to correspond to those found in human m-NAD(P)-ME, EC 1.1.1.39. No significant difference between the wild-type and mutant enzymes in Km values for NADP+ and malate, and in kcat values. A chimeric enzyme, [51-105]_c-NADP-ME, is designed to include the putative fumarate-binding site ofm-NAD(P)-ME at the dimer interface of c-NADP-ME, but the chimera remains nonallosteric
additional information
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expression of the enzyme from Mucor circinelloides as a strategy to improve lipid content inside the Rhodotorula glutinis yeast cells, overview. Heterologous expression of NADP+-dependent ME involved in fatty acid biosynthesis increases the lipid accumulation in the oleaginous yeast Rhodotorula glutinis
additional information
expression of the enzyme from Mucor circinelloides as a strategy to improve lipid content inside the Rhodotorula glutinis yeast cells, overview. Heterologous expression of NADP+-dependent ME involved in fatty acid biosynthesis increases the lipid accumulation in the oleaginous yeast Rhodotorula glutinis
additional information
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expression of malic enzyme from Mucor circinelloides as a strategy to improve lipid content inside the cells. The 26S rDNA and 5.8S rDNA gene fragments, with PGK1 gene from Saccharomyces cerevisiae strain 2.1445, isolated from Rhodotorula glutinis strain GM4 are used for homologous integration of the malc enzyme gene into Rhodotorula glutinis chromosome under the control of the constitutively highly expressed gene phosphoglycerate kinase 1 resulting in stable expression. Improvment of the lipid content by more than twofold. There are no significant differences in fatty acid profiles between the wild-type strain and the recombinant strain of Rhodotorula glutinis
additional information
expression of malic enzyme from Mucor circinelloides as a strategy to improve lipid content inside the cells. The 26S rDNA and 5.8S rDNA gene fragments, with PGK1 gene from Saccharomyces cerevisiae strain 2.1445, isolated from Rhodotorula glutinis strain GM4 are used for homologous integration of the malc enzyme gene into Rhodotorula glutinis chromosome under the control of the constitutively highly expressed gene phosphoglycerate kinase 1 resulting in stable expression. Improvment of the lipid content by more than twofold. There are no significant differences in fatty acid profiles between the wild-type strain and the recombinant strain of Rhodotorula glutinis
additional information
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expression of the enzyme from Mucor circinelloides as a strategy to improve lipid content inside the Rhodotorula glutinis yeast cells, overview. Heterologous expression of NADP+-dependent ME involved in fatty acid biosynthesis increases the lipid accumulation in the oleaginous yeast Rhodotorula glutinis
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additional information
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expression of malic enzyme from Mucor circinelloides as a strategy to improve lipid content inside the cells. The 26S rDNA and 5.8S rDNA gene fragments, with PGK1 gene from Saccharomyces cerevisiae strain 2.1445, isolated from Rhodotorula glutinis strain GM4 are used for homologous integration of the malc enzyme gene into Rhodotorula glutinis chromosome under the control of the constitutively highly expressed gene phosphoglycerate kinase 1 resulting in stable expression. Improvment of the lipid content by more than twofold. There are no significant differences in fatty acid profiles between the wild-type strain and the recombinant strain of Rhodotorula glutinis
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additional information
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construction of transgenic tobacco plants by expression of the maize enzyme, recombinant expression leads to plants with altered malate metabolism in guard cells and stomatal function which are more drought tolerant than the wild-type tobacco, overview
additional information
overexpression of rice isozyme NADP-ME2 in Arabidopsis thaliana enhances tolerance to salt and osmotic stresses in transgenic seedlings, overview
additional information
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overexpression of rice isozyme NADP-ME2 in Arabidopsis thaliana enhances tolerance to salt and osmotic stresses in transgenic seedlings, overview
additional information
transgenic Arabidopsis thaliana plants overexpressing rice cytosolic NADP-ME have a greater salt tolerance at the seedling stage than wild-type plants in MS medium-supplemented with different levels of NaCl, no obvious morphological or developmental differences between the transgenic and wild-type plants
additional information
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transgenic Arabidopsis thaliana plants overexpressing rice cytosolic NADP-ME have a greater salt tolerance at the seedling stage than wild-type plants in MS medium-supplemented with different levels of NaCl, no obvious morphological or developmental differences between the transgenic and wild-type plants
additional information
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siRNA knockdown of cytosolic ME1 by 89% of mRNA expression and enzyme activity significantly reduces glucose and decreases the flux of both pools of pyruvate through pyruvate carboxylase affecting the anaplerotic pathways, insulin secretion in response to membrane depolarization using potassium chloride is unaffected by siRNA knockdown of malic enzyme, overview
additional information
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siRNA knockout of ME1 in INS-1 832/13 beta-cells, siRNA knockdown and isotopic labeling strategies, method optimization, overview
additional information
generation of several ME3 knockdown cell lines, knockdown of inhibits insulin release. In the Me3 double-knockdown cells, the level of Me1 mRNA is not significantly decreased in the Me3-628(P)/Me2-725(H) and Me3-1672(P)/Me2-725(H) cell lines. However, a 32%, 49%, and 47% decrease in ME1 activity is observed in the cell lines Me3-628(P), Me3-628(P)/Me2-725(H), and Me3-628(P)/Me2-2124(H), respectively. Me3 mRNA is decreased in the Me3 single-knockdown cell line Me3-628(P), and it is lowered further in the Me3 and Me1 double-knockdown Me3628(P)/Me1-753(H) but not Me3-1672(P)/Me1-753(H). The level of Me3 mRNA in Me3-628(P)/Me1-753(H) and Me3-1672(P)/Me1-753(H) is 10% and 59% of the CHS control, respectively
additional information
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the tme gene is placed under the control of the dme promoter, and despite elevated levels of TME within bacteroids, no symbiotic nitrogen fixation occurred in dme mutant strains, the dme mutant cells fail to fix N2 in alfalfa root nodules, overview, no TME in the tme mutant RmG994
additional information
directed evolution of the thermotolerant NADP(H)-dependent malic enzyme from Thermococcus kodakarensis is conducted to alter the cofactor preference of the enzyme from NADP(H) to NAD(H). Integration of the thermotolerant NADPH-dependent malic enzyme (EC 1.1.1.40) from Thermococcus kodakarensis (TkME) to the chimeric EM pathway enables the construction of a cofactor-balanced and HCO3- fixing synthetic pathway, through which the direct conversion of glucose to malate can be achieved. The thermal degradation of the redox cofactors NADP+ and NADPH tends to be a major obstacle to the long-term operation of the in vitro metabolic system because, unlike living biological systems, it is not equipped with the complete enzyme apparatus for the de novo synthesis of these cofactors. No significant change is observed in the thermal stability of the wild type and mutant enzymes
additional information
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directed evolution of the thermotolerant NADP(H)-dependent malic enzyme from Thermococcus kodakarensis is conducted to alter the cofactor preference of the enzyme from NADP(H) to NAD(H). Integration of the thermotolerant NADPH-dependent malic enzyme (EC 1.1.1.40) from Thermococcus kodakarensis (TkME) to the chimeric EM pathway enables the construction of a cofactor-balanced and HCO3- fixing synthetic pathway, through which the direct conversion of glucose to malate can be achieved. The thermal degradation of the redox cofactors NADP+ and NADPH tends to be a major obstacle to the long-term operation of the in vitro metabolic system because, unlike living biological systems, it is not equipped with the complete enzyme apparatus for the de novo synthesis of these cofactors. No significant change is observed in the thermal stability of the wild type and mutant enzymes
additional information
construction of the Gsite5V and Gsite2V mutants, mutation at the NADP+ binding site
additional information
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construction of the Gsite5V and Gsite2V mutants, mutation at the NADP+ binding site
additional information
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construction of transgenic tobacco plants by expression of the maize enzyme, recombinant expression leads to plants with altered malate metabolism in guard cells and stomatal function which are more drought tolerant than the wild-type tobacco
additional information
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construction of chimerical NADP-ME sequences obtained from C4 and non-C4 isozymes
additional information
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transgenic Arabidopsis thaliana plants overexpressing the maize C4 NADP-malic enzyme show 6-33fold increase enzyme activity and a more rapid progression of dark-induced senescence compared to the wild type plants, overview
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3'-UTR region, cloning, sequencing, and analysis
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
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cytosolic and mitochondrial isozymes, expression in of His-tagged isozymes ME1 and ME2 Escherichia coli Rosetta (DE3)pLysS
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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)
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DNA and amino acid sequence determination and analysis
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain JM109
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expressed in Arabidopsis thaliana
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expressed in Chlorella pyrenoidosa
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expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(lambdaDE3) cells
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expressed in Escherichia coli BL21-CodonPlus (DE3) RIL cells
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expressed in Escherichia coli Rosetta (DE3) pLysS cells
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expressed in Escherichia coli Rosetta cells
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expressed in Escherichia coli Rosetta(DE3) cells
expressed in Mucor circinelloides strain MU290
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expressed in Rhodotorula glutinis strain GM4
expression in Arabidopsis thaliana under control of the 35S promoter
expression in Escherichia coli
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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
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expression in Escherichia coli, NADP-ME1
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expression in Escherichia coli, NADP-ME2
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expression in Escherichia coli, NADP-ME3
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expression in Escherichia coli, NADP-ME4
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expression in tobacco plants via infection with Agrobacterium tumefaciens
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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
expression of His-tagged chimeric NADP-ME mutants in Escherichia coli strain BL21(DE3)
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expression of His-tagged isozymes ME1 and ME2 in Escherichia coli strain BL21(DE3)
expression of isozyme NADP-ME2 in Escherichia coli strain BL21(DE3)
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expression of the maize enzyme in Arabidopsis thaliana under control of the cauliflower mosaic virus 35S promoter
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant isozymes NADP-ME2 in Escherichia coli
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expression of wild-type and mutants in Escherichia coli BL21(DE3)
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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
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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
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functional recombinant enzyme expression in Rhodotorula glutinis strain GM4, subcloning in Escherichia coli strain DH5alpha
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 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
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gene maeB, sequence comparisons, recombinant expression in Escherichia coli strain BL21 resulting in increased malic enzyme activity and a 4fold enhancement in lipid content. Overexpressing the NADP-ME of Escherichia coli strain BL21 results in a 15% decrease in fatty acid production instead
gene malE, DNA and amino acid sequence determination and analysis, genomic library construction, screening, and functional enzyme expression in Escherichia coli
gene malE1, recombinant overexpression of the gene encoding ME isoform E from Mortierella alpina via Agrobacterium tumefaciens-mediated transformation in Mortierella alpina uracil auxotrophic strain increasing the fatty acid content by 30% compared to that for wild-type control, quantitative reverse transcription PCR enzyme expression analysis. The expression of the malE1 gene in three randomly selected malE1-overexpressing strains
gene Sco5261, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expressionin Escherichia coli strain BL21(DE3)
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
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genes NADP-ME1, NADP-ME2, and NADP-ME3, quantitative RT-PCR expression analysis
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isozyme DNA and amino acid sequence determination and analysis, phylogenetic analysis, overview
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
isozyme NADP-ME2, expression in Escherichia coli
isozymes expression analysis, overview
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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
ME1 and ME3, quantitative real time PCR expression analysis
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mutant enzymes expressed in Escherichia coli
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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
nadp-me1, expression in Escherichia coli
overexpression in Escherichia coli
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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
preparation of a genomic library, DNA and amino acid sequence determination and analysis, detailed phylogenetic reconstruction of malic enzymes, overview
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
sequence comparisons, recombinant enzyme overexpression in Chlorella pyrenoidosa
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sequence comparisons, recombinant expression in Mortierella alpine
sequence comparisons,, recombinant expressionin Mucor circinelloides
subcloning in strain K-12, expression of the His-tagged enzyme in strain BL21(DE3)
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3'-UTR region, cloning, sequencing, and analysis
3'-UTR region, cloning, sequencing, and analysis
3'-UTR region, cloning, sequencing, and analysis
expressed in Escherichia coli BL21 (DE3) cells
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expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expression of His-tagged isozymes ME1 and ME2 in Escherichia coli strain BL21(DE3)
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expression of His-tagged isozymes ME1 and ME2 in Escherichia coli strain BL21(DE3)
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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
sequence comparisons
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