Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction

Biochemistry ◽  
1991 ◽  
Vol 30 (23) ◽  
pp. 5755-5763 ◽  
Author(s):  
Paul M. Weiss ◽  
Sandhya R. Gavva ◽  
Ben G. Harris ◽  
Jeffrey L. Urbauer ◽  
W. W. Cleland ◽  
...  
Keyword(s):  
Malic Enzyme ◽  
Isotope Effects ◽  
Enzyme Reaction

Kinetic Mechanism and Intrinsic Isotope Effects for the Peptidylglycine α-Amidating Enzyme Reaction†

Biochemistry ◽  
1998 ◽  
Vol 37 (22) ◽  
pp. 8244-8252 ◽  
Author(s):  
Wilson A. Francisco ◽  
David J. Merkler ◽  
Ninian J. Blackburn ◽  
Judith P. Klinman
Keyword(s):  
Isotope Effects ◽  
Enzyme Reaction ◽  
Kinetic Mechanism

Determination of the Chemical Mechanism of Malic Enzyme by Isotope Effects†

Biochemistry ◽  
1997 ◽  
Vol 36 (5) ◽  
pp. 1141-1147 ◽  
Author(s):  
William A. Edens ◽  
Jeffrey L. Urbauer ◽  
W. W. Cleland
Keyword(s):  
Malic Enzyme ◽  
Isotope Effects ◽  
Chemical Mechanism

Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies

Biochemistry ◽  
1977 ◽  
Vol 16 (4) ◽  
pp. 571-576 ◽  
Author(s):  
Michael I. Schimerlik ◽  
C. E. Grimshaw ◽  
W. W. Cleland
Keyword(s):  
Malic Enzyme ◽  
Isotope Effects ◽  
Kinetic Studies ◽  
Rate Limiting

scholarly journals Properties and regulation of leaf nicotinamide–adenine dinucleotide phosphate–malate dehydrogenase and ‘malic’ enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis

1970 ◽  
Vol 119 (2) ◽  
pp. 273-280 ◽  
Author(s):  
Hilary S. Johnson ◽  
M. D. Hatch
Keyword(s):  
Dicarboxylic Acid ◽  
Malate Dehydrogenase ◽  
Malic Enzyme ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Maximum Velocity ◽  
Enzyme Reaction ◽  
Reverse Direction ◽  
Leaf Extracts ◽  
Ph Optimum ◽  
Acid Pathway

1. NADP–malate dehydrogenase and `malic' enzyme in maize leaf extracts were separated from NAD–malate dehydrogenase and their properties were examined. 2. The NADP–malate dehydrogenase was nicotinamide nucleotide-specific but otherwise catalysed a reaction comparable with that with the NAD-specific enzyme. By contrast with the latter enzyme, a thiol was absolutely essential for maintaining the activity of the NADP–malate dehydrogenase, and the initial velocity in the direction of malate formation, relative to the reverse direction, was faster. 3. For the `malic' enzyme reaction the Km for malate was dependent on pH and the pH optimum varied with the malate concentration. At their respective optimum concentrations the maximum velocity for this enzyme was higher with Mg2+ than with Mn2+. 4. The NADP–malate dehydrogenase in green leaves was rapidly inactivated in the dark and was reactivated when plants were illuminated. Reactivation of the enzyme extracted from darkened leaves was achieved simply by adding a thiol compound. 5. The activity of both enzymes was low in etiolated leaves of maize plants grown in the dark but increased 10–20-fold, together with chlorophyll, when leaves were illuminated. 6. The activity of these enzymes in different species with the C4-dicarboxylic acid pathway was compared and their possible role in photosynthesis was considered.

Metal Ion Activator on Intrinsic Isotope Effects of Hydride Transfer and Decarboxylation in the Reaction Catalyzed by the NAD-Malic Enzyme from Ascaris suum

Biochemistry ◽  
1995 ◽  
Vol 34 (10) ◽  
pp. 3253-3260 ◽  
Author(s):  
William E. Karsten ◽  
Sandya R. Gavva ◽  
Sang-Hoon Park ◽  
Paul F. Cook
Keyword(s):  
Malic Enzyme ◽  
Metal Ion ◽  
Ascaris Suum ◽  
Isotope Effects ◽  
Hydride Transfer
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