Kinetic mechanism of NADP-malic enzyme from maize leaves

1995 ◽  
Vol 43 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Claudia P. Spampinato ◽  
Carlos S. Andreo
Keyword(s):  
Malic Enzyme ◽  
Kinetic Mechanism ◽  
Maize Leaves

Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo
Keyword(s):  
Metal Ions ◽  
Malic Enzyme ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Maize Leaves

scholarly journals Evidence for the Existence of Two Essential and Proximal Cysteinyl Residues in NADP-Malic Enzyme from Maize Leaves

1992 ◽  
Vol 100 (4) ◽  
pp. 2035-2040 ◽  
Author(s):  
María F. Drincovich ◽  
Claudia P. Spampinato ◽  
Carlos S. Andreo
Keyword(s):  
Malic Enzyme ◽  
Maize Leaves

Two forms of NAD-malic enzyme in maize leaves are regulated by light in opposite ways via promoter methylation

2020 ◽  
Vol 251 ◽  
pp. 153193
Author(s):  
Alexander T. Eprintsev ◽  
Dmitry N. Fedorin ◽  
Marina O. Gataullina ◽  
Abir U. Igamberdiev
Keyword(s):  
Promoter Methylation ◽  
Malic Enzyme ◽  
Maize Leaves

Adenylate Kinase from Maize Leaves: True Substrates, Inhibition by P1 , P5-di(adenosine-5′) pentaphosphate and Kinetic Mechanism

1990 ◽  
Vol 45 (6) ◽  
pp. 607-613 ◽  
Author(s):  
Leszek A. Kleczkowski ◽  
Douglas D. Randall ◽  
Warren L. Zahler
Keyword(s):  
Adenylate Kinase ◽  
Kinetic Studies ◽  
Kinetic Mechanism ◽  
Reverse Reaction ◽  
Plant Tissues ◽  
Forward Reaction ◽  
Higher Plant ◽  
Maize Leaves ◽  
Variable Substrate ◽  
Free Magnesium

Abstract Purified maize leaf adenylate kinase (AK) was shown to use one molecule each of free ADP and Mg-ADP as well as free AM P and Mg-ATP as substrates in the forward and reverse reaction, respectively. This was deduced from substrate kinetic studies which were carried out under conditions of strictly defined concentrations of free and Mg-complexed adenylate species and under controlled free magnesium levels. Apparent Km values of the substrates of AK were 3 and 6 μM for ADP and Mg-ADP, respectively (forward reaction), and 69 and 25 μM for free AMP and Mg-ATP, respectively (reverse reaction). The enzyme was competitively inhibited by P1,P5-di(adenosine-5′)pentaphosphate (Ap5A), a bisubstrate analog of AK reaction, with apparent Ki values in the range of 11 -80 nM , depending on variable substrate. Substrate kinetic studies and inhibition patterns with Ap5A suggested a sequential random kinetic mechanism in both directions of the reaction. These properties of a higher plant AK are similar or analogous to those previously established for the enzyme from yeast and non-plant tissues.

A study on the inactivation of maize leaves nadp-malic enzyme by 3-bromopyruvate

1992 ◽  
Vol 31 (6) ◽  
pp. 1883-1888 ◽  
Author(s):  
Maria F. Drincovich ◽  
Carlos S. Andreo
Keyword(s):  
Malic Enzyme ◽  
Maize Leaves

Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum

Biochemistry ◽  
1984 ◽  
Vol 23 (23) ◽  
pp. 5446-5453 ◽  
Author(s):  
Sang Hoon Park ◽  
Dennis M. Kiick ◽  
Ben G. Harris ◽  
Paul F. Cook
Keyword(s):  
Malic Enzyme ◽  
Ascaris Suum ◽  
Kinetic Mechanism ◽  
Oxidative Decarboxylation

Two forms of NADP-dependent malic enzyme in expanding maize leaves

Planta ◽  
1979 ◽  
Vol 144 (3) ◽  
pp. 283-289 ◽  
Author(s):  
Paolo Pupillo ◽  
Patrizia Bossi
Keyword(s):  
Malic Enzyme ◽  
Maize Leaves

scholarly journals NADP-linked malic enzyme. Purification from maize leaves, Mr and subunit composition

1988 ◽  
Vol 254 (1) ◽  
pp. 229-233 ◽  
Author(s):  
M S Thorniley ◽  
K Dalziel
Keyword(s):  
Malic Enzyme ◽  
Enzyme Purification ◽  
Gel Filtration ◽  
Sedimentation Velocity ◽  
Exchange Chromatography ◽  
Subunit Composition ◽  
Sedimentation Equilibrium ◽  
Apparent Homogeneity ◽  
Maize Leaves ◽  
A Subunit

1. The isolation of NADP-linked malic enzyme (EC 1.1.1.40) from maize leaves is described, together with studies of its Mr and subunit composition. 2. The enzyme was purified to apparent homogeneity by affinity chromatography on N6-aminohexyl-2′,5′-bisphosphoadenosine-agarose, gel filtration with Sephadex G-100 and ion-exchange chromatography on DEAE-Sephadex A-50. A purification of 140-fold with a 30% yield was obtained. 3. A detailed study of the Mr by several methods revealed the existence of different Mr forms in solution. 4. In the presence of dithiothreitol the enzyme appears to be present in triethanolamine buffer, pH 7.5, as a tetramer with a subunit Mr of 60,000 and an S20,w of 10.75 S. 5. In phosphate buffer, pH 7.0, it seems to be a dimer of Mr 120,000 with an S20,w of 7.95 S. 6. In the absence of dithiothreitol, lower-Mr forms were detected by sedimentation-equilibrium and sedimentation-velocity studies in triethanolamine buffer. 7. Results from gel filtration gave Mr values of about 340,000 in both buffers.

Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo
Keyword(s):  
Metal Ions ◽  
Malic Enzyme ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Maize Leaves
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