EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.39 | K143A |
site-directed mutagenesis, malate binding residue, mutant shows highly increased kcat for malate and fumarate compared to the wild-type enzyme |
654720 |
| 1.1.1.39 | K362H |
the mutant enzyme displays a considerable elevation in Km for NADP+, and the kcat for NAD+ value is elevated compared to the wild-type enzyme |
723540 |
| 1.1.1.39 | more |
azc3656 mutants show about 4fold reduced NAD+-malic enzyme activity |
-, 721353 |
| 1.1.1.39 | more |
construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism |
711147 |
| 1.1.1.39 | more |
construction of two chimeras NADME1q and NAD-ME2q by interchanging the first 176 amino residues between NAD-ME1 and -2, altered regulation in comparison to the wild-type enzymes, overview |
712417 |
| 1.1.1.39 | more |
expression of the tme gene, EC 1.1.1.40, under the control of the dme promoter, cannot restore the N2 fixation activity which is lost in dme mutant cells in alfalfa root nodules, despite elevated levels of TME within bacteroids, no symbiotic nitrogen fixation occurs in dme mutant strains, overview |
669132 |
| 1.1.1.39 | more |
generation of Me1 single and double knockdown cell lines, thereby generating cell line 753(H)/Me1-753(P), overview. The level of Me1 mRNA in the double-knockdown cell line Me1-753(H)/Me1-753(P) is decreased to 2% as compared with 14% in the single knockdown Me1-753(H) cell line. The level of Me2mRNAis lowered by only 10% in the Me1-753(H) cell line and Me3 mRNA is lowered by only 27% in the Me1-753(H) cell line and lowered by only 35% in the Me1-753(H)/Me1-753(P) cell line. 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. 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 |
741010 |
| 1.1.1.39 | more |
method optimization of the reverse reaction of the malic enzyme for HCO3- fixation into pyruvic acid to produce L-malic acid with NADH generation including the activity of glucose-6-phosphate dehydrogenase, EC1.1.1.49, from Leuconostoc mesenteroides |
-, 685678 |
| 1.1.1.39 | more |
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of chimeric protein NAD-ME1q, which is composed of the first 176 amino acid residues of isozyme NAD-ME2 and the central and C-terminal sequence of isozyme NAD-ME1, exhibits a significantly lower Km L-malate value than the parental isoforms and a hyperbolic behavior that is not modified by fumarate |
741121 |
| 1.1.1.39 | more |
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of the chimeric protein NAD-ME2q, that possesses the first 176 amino acid residues of NAD-ME1 and the central and C-terminal sequence of NAD-ME2, presents a sigmoidal L-malate response similar to the one for NAD-ME1, but also a higher Km L-malate value and a lower kcat value. NAD-ME2q is activated by fumarate and an increase in its concentration produces a decrease in Km and nH values. At 4 mM fumarate, the Lmalate saturation curve is hyperbolic (nH = 1.1) with an 8fold decrease in Km value. There are no significant changes in kcat value by addition of fumarate, which implies a 9fold increase in NAD-ME2q catalytic efficiency when compared to the enzyme in the absence of fumarate |
741121 |
