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Literature summary for 1.1.1.39 extracted from

  • Eprintsev, A.T.; Fedorin, D.N.; Gataullina, M.O.; Igamberdiev, A.U.
    Two forms of NAD-malic enzyme in maize leaves are regulated by light in opposite ways via promoter methylation (2020), J. Plant Physiol., 251, 153193 .
    View publication on PubMed
Search for more literature for 1.1.1.39

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00015
-
 NADH isoform ME1, at pH 6.5 and 37°C Zea mays
0.00018
-
 NADH isoform ME2, at pH 6.5 and 37°C Zea mays
0.00035
-
 NAD+ isoform ME1, at pH 6.5 and 37°C Zea mays
0.00037
-
 NAD+ isoform ME2, at pH 6.5 and 37°C Zea mays
0.00125
-
 pyruvate isoform ME2, at pH 6.5 and 37°C Zea mays
0.00158
-
 pyruvate isoform ME1, at pH 6.5 and 37°C Zea mays
0.003
-
 (S)-malate isoform ME2, at pH 6.5 and 37°C Zea mays
0.0035
-
 (S)-malate isoform ME1, at pH 6.5 and 37°C Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Zea mays
Mn2+ activates, 5 mM used in assay conditions Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Zea mays the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate pyruvate + CO2 + NADH + H+
-
 r
pyruvate + CO2 + NADH + H+ Zea mays the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate (S)-malate + NAD+
-
 r

Organism

Organism UniProt Comment Textmining
Zea mays
-
 cultivar Voronezhskaya 76
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, DEAE Sephacel column chromatography, and Sephadex G-25 gel filtration Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.04
-
 enzyme from homogenate, at pH 6.5 and 37°C Zea mays
4.7
-
 enzyme after 117fold purification, at pH 6.5 and 37°C Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+ the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate Zea mays pyruvate + CO2 + NADH + H+
-
 r
pyruvate + CO2 + NADH + H+ the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate Zea mays (S)-malate + NAD+
-
 r

Synonyms

Synonyms Comment Organism
ME1 isoform Zea mays
ME2 isoform Zea mays
NAD-dependent malate dehydrogenase (decarboxylating)
-
 Zea mays
NAD-malic enzyme
-
 Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4
-
 pH optimum of isoform ME1 in the forward reaction Zea mays
6.7
-
 pH optimum of isoform ME1 in the reverse reaction Zea mays
6.9
-
 pH optimum of isoform ME2 in the forward reaction Zea mays
7.3
-
 pH optimum of isoform ME2 in the reverse reaction Zea mays

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Zea mays
NADH
-
 Zea mays

Expression

Organism Comment Expression
Zea mays the enzymes total activity is suppressed by white light and by red light (660 nm) down
Zea mays the enzymes total activity is high in darkness and upon irradiation by far-red light (730 nm) up