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Literature summary for 1.1.1.39 extracted from

  • Tronconi, M.A.; Gerrard Wheeler, M.C.; Maurino, V.G.; Drincovich, M.F.; Andreo, C.S.
    NAD-malic enzymes of Arabidopsis thaliana display distinct kinetic mechanisms that support differences in physiological control (2010), Biochem. J., 430, 295-303.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of NAD-ME1, NAD-ME2, and NAD-MEH Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information 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 Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
(S)-malate isozyme NAD-ME2, competitive Arabidopsis thaliana
5'-AMP isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate Arabidopsis thaliana
CO2 chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate; isozyme NAD-ME2 and chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate Arabidopsis thaliana
additional information product inhibition patterns of isozyme NAD-ME2, overview; product inhibition patterns of isozyme NAD-ME2, overview Arabidopsis thaliana
NADH isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate. NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q; NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q Arabidopsis thaliana
pyruvate isozyme NAD-ME2, uncompetitive versus NAD+, mixed inhibition versus (S)-malate. Pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q; pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q Arabidopsis thaliana
Tartrate substrate analogue, isozyme NAD-ME2, uncompetitive versus NAD+, competitive versus (S)-malate Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Isozyme NAD-ME2 follows a sequential ordered Bi-Ter mechanism. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview Arabidopsis thaliana
additional information
-
additional information kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview Arabidopsis thaliana
1.1
-
NAD+ isozyme NAD-ME2, pH 6.5, temperature not specified in the publication Arabidopsis thaliana
2.6
-
(S)-malate isozyme NAD-ME2, pH 6.5, temperature not specified in the publication Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion isozyme NAD-ME1 Arabidopsis thaliana 5739
-
mitochondrion isozymes NAD-ME1 and NAD-ME2 Arabidopsis thaliana 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates Arabidopsis thaliana
Mn2+ activates probably Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Arabidopsis thaliana NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria pyruvate + NADH + H+ + CO2
-
ir
(S)-malate + NAD+ Arabidopsis thaliana NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria pyruvate + NADH + H+ + CO2
-
r

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8L7K9 isozyme NAD-ME2
-
Arabidopsis thaliana Q9SIU0 isozyme NAD-ME1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant NAD-ME1, NAD-ME2, and NAD-MEH Arabidopsis thaliana

Reaction

Reaction Comment Organism Reaction ID
(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Hetereodimer NAD-MEH can bind both substrates randomly. Interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour Arabidopsis thaliana
(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Isozyme NAD-ME1 and hetereodimer NAD-MEH can bind both substrates randomly. However, NAD-ME1 shows a preferred route that involves the addition of NAD+ first. interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+ NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria Arabidopsis thaliana pyruvate + NADH + H+ + CO2
-
ir
(S)-malate + NAD+ NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria Arabidopsis thaliana pyruvate + NADH + H+ + CO2
-
r

Subunits

Subunits Comment Organism
dimer isozymes NAD-ME1 and NAD-ME2 assemble as homo- and heterodimers, the latter is termed NAD-MEH, in vitro and in vivo. Interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
NAD-malic enzyme
-
Arabidopsis thaliana
NAD-ME1
-
Arabidopsis thaliana
NAD-ME2
-
Arabidopsis thaliana
NAD-MEH
-
Arabidopsis thaliana

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
46
-
NAD+ isozyme NAD-ME2, pH 6.5, temperature not specified in the publication Arabidopsis thaliana
46
-
(S)-malate isozyme NAD-ME2, pH 6.5, temperature not specified in the publication Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
forward reaction, assay at Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Arabidopsis thaliana

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.041
-
NADH versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
0.15
-
NADH versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
0.45
-
5'-AMP versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
0.8
-
Tartrate versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
1.5
-
5'-AMP versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
3
-
CO2 versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
4
-
Tartrate versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
7
-
CO2 versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
11
-
pyruvate versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana
14
-
pyruvate versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2 Arabidopsis thaliana

General Information

General Information Comment Organism
additional information interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The 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, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism Arabidopsis thaliana
physiological function for a metabolic condition in which the mitochondrial NAD level is low and the (S)-malate level is high, the activity of homodimeric isozyme NAD-ME2 and/or heterodimer NAD-MEH would be preferred over that of homodimeric isozyme NAD-ME1 Arabidopsis thaliana