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1.1.1.38: malate dehydrogenase (oxaloacetate-decarboxylating)

This is an abbreviated version!
For detailed information about malate dehydrogenase (oxaloacetate-decarboxylating), go to the full flat file.

Word Map on EC 1.1.1.38

Reaction

(S)-malate
+
NAD+
=
pyruvate
+
CO2
+
NADH
+
H+

Synonyms

m-NAD(P)-ME, maeA, malic enzyme, malic enzyme 2, ME2, MHD, mitochondrial malic enzyme ME2, mitochondrial NAD(P) malic enzyme, mitochondrial NAD(P) malic enzyme ME2, mitochondrial NAD(P)+-dependent malic enzyme, mitochondrial NAD-malic enzyme, NAD+-dependent malic enzyme, NAD-dependent ME, NAD-malic enzyme, NAD-ME, NAD-specific malic enzyme, NADH-dependent malic enzyme, pyruvic-malic carboxylase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.38 malate dehydrogenase (oxaloacetate-decarboxylating)

Engineering

Engineering on EC 1.1.1.38 - malate dehydrogenase (oxaloacetate-decarboxylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N434A
with N434A, the interaction of the residue with malate is lost, causing the malate to reorient itself, leading to a slower decarboxylation step
N479Q
the Kmalate value for the N479Q mutant enzyme increases by 2.2fold compared to the wild type enzyme, the KNAD value for the N479Q mutant enzyme increases by 1.1fold compared to the wild type enzyme
N479S
the Kmalate value for the N479Q mutant enzyme increases by 2.1fold compared to the wild type enzyme, the KNAD value for the N479Q mutant enzyme increases by 1.8fold compared to the wild type enzyme
S433A
the KNAD value for the S433A mutant enzyme increases by 80fold compared to the wild type enzyme, indicating that this residue provides significant binding affinity for the dinucleotide
L310R
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/Q401C
L310R/R346A/Q401C
the mutant prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346D/Q401C
the mutant prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346F/Q401C
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346K/Q401C
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346Y/Q401C
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
K57S/E59N/K73E/D102S
site-directed mutagenesis
G444A
-
inactive enzyme
additional information
generation of Me2 single and double knockdown cell lines, thereby generating cel lines Me2–2124(H)/Me2–2124(P) and Me2–2124(H)/Me2-654(P), overview. Me2 mRNA and ME2 enzyme activity are drastically reduced in the double-knockdown cell lines Me2-2124(H)/Me2-2124(P) and Me2-2124(H)/Me2-456(P). Me3 mRNA is slightly reduced in these two cell lines, whereas Me1 mRNA and ME1 enzyme activity are not affected. Resident siRNA might interfere with the expression of the siRNA expressed from the second vector. Knockdown of isozyme ME3, EC 1.1.1.40, 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