Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.39 0.00015
-
NADH isoform ME1, at pH 6.5 and 37°C Zea mays
1.1.1.39 0.00018
-
NADH isoform ME2, at pH 6.5 and 37°C Zea mays
1.1.1.39 0.00035
-
NAD+ isoform ME1, at pH 6.5 and 37°C Zea mays
1.1.1.39 0.00037
-
NAD+ isoform ME2, at pH 6.5 and 37°C Zea mays
1.1.1.39 0.00125
-
pyruvate isoform ME2, at pH 6.5 and 37°C Zea mays
1.1.1.39 0.00158
-
pyruvate isoform ME1, at pH 6.5 and 37°C Zea mays
1.1.1.39 0.003
-
(S)-malate isoform ME2, at pH 6.5 and 37°C Zea mays
1.1.1.39 0.0035
-
(S)-malate isoform ME1, at pH 6.5 and 37°C Zea mays

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.39 (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
1.1.1.39 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

EC Number Organism UniProt Comment Textmining
1.1.1.39 Zea mays
-
cultivar Voronezhskaya 76
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.39 leaf
-
Zea mays
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.39 0.04
-
enzyme from homogenate, at pH 6.5 and 37°C Zea mays
1.1.1.39 4.7
-
enzyme after 117fold purification, at pH 6.5 and 37°C Zea mays

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.39 (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
1.1.1.39 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

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.39 6.4
-
pH optimum of isoform ME1 in the forward reaction Zea mays
1.1.1.39 6.7
-
pH optimum of isoform ME1 in the reverse reaction Zea mays
1.1.1.39 6.9
-
pH optimum of isoform ME2 in the forward reaction Zea mays
1.1.1.39 7.3
-
pH optimum of isoform ME2 in the reverse reaction Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.39 NAD+
-
Zea mays
1.1.1.39 NADH
-
Zea mays

Expression

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