Krebs cycle metabolon formation: metabolite concentration gradient enhanced compartmentation of sequential enzymes

2015 ◽  
Vol 51 (7) ◽  
pp. 1244-1247 ◽  
Author(s):  
Fei Wu ◽  
Lindsey N. Pelster ◽  
Shelley D. Minteer
Keyword(s):  
Malate Dehydrogenase ◽  
Concentration Gradient ◽  
Citrate Synthase ◽  
Krebs Cycle ◽  
Microfluidic Channel ◽  
Metabolite Concentration ◽  
Concentration Region ◽  
Directional Diffusion ◽  
Mitochondrial Malate Dehydrogenase

The substrate (l-malate) gradient created in a microfluidic channel induced the directional diffusion of mitochondrial malate dehydrogenase (mMDH) toward a higher concentration region and in situ generation of an intermediate (OAA) gradient enhanced the co-diffusion of citrate synthase (CS) together with mMDH.

Nardilysin facilitates complex formation between mitochondrial malate dehydrogenase and citrate synthase

2005 ◽  
Vol 1723 (1-3) ◽  
pp. 292-301 ◽  
Author(s):  
K. Martin Chow ◽  
Zhangliang Ma ◽  
Jian Cai ◽  
William M. Pierce ◽  
Louis B. Hersh
Keyword(s):  
Complex Formation ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Mitochondrial Malate Dehydrogenase

Electrostatic Channeling of Oxaloacetate in a Fusion Protein of Porcine Citrate Synthase and Porcine Mitochondrial Malate Dehydrogenase†

Biochemistry ◽  
1999 ◽  
Vol 38 (3) ◽  
pp. 881-889 ◽  
Author(s):  
Konstantin Shatalin ◽  
Sandrine Lebreton ◽  
Magali Rault-Leonardon ◽  
Christian Vélot ◽  
Paul A. Srere
Keyword(s):  
Fusion Protein ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Mitochondrial Malate Dehydrogenase

scholarly journals Hydrophobic interaction between the monomer of mitochondrial malate dehydrogenase and phospholipid membranes

1980 ◽  
Vol 186 (1) ◽  
pp. 227-233 ◽  
Author(s):  
K A Webster ◽  
K B Freeman ◽  
S Ohki
Keyword(s):  
Malate Dehydrogenase ◽  
Conformational Changes ◽  
Ribonuclease A ◽  
Phospholipid Vesicles ◽  
Mitochondrial Matrix ◽  
Dimer Formation ◽  
Dimeric Form ◽  
Oil Water ◽  
Mitochondrial Malate Dehydrogenase

Porcine mitochondrial malate dehydrogenase (EC 1.1.1.37) dissociates into subunits on dilution. The enzyme monomer caused large increases in the surface pressure of monolayers of 1:1 phosphatidylserine/phosphatidylcholine at air/water and oil/water interfaces. The monomer increased the permeability of phospholipid vesicles to 22Na+. Both effects were significantly greater than the corresponding effects of ribonuclease A, cytochrome c and the dimeric form of malate dehydrogenase. Changes in the circular-dichroism spectra of the enzyme indicated that conformational changes may be associated with dimer formation or when monomer interacts with lysophosphatidyl-choline. Similar interactions to those described may occur in situ when mitochondrial malate dehydrogenase is transported to the mitochondrial matrix from its site of synthesis on cytosolic ribosomes.

Identification, cloning and expression analysis of strawberry (Fragaria x ananassa) mitochondrial citrate synthase and mitochondrial malate dehydrogenase

2004 ◽  
Vol 121 (1) ◽  
pp. 15-26 ◽  
Author(s):  
Pietro P. M. Iannetta ◽  
Nieves Medina Escobar ◽  
Heather A. Ross ◽  
Edwige J. F. Souleyre ◽  
Robert D. Hancock ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Expression Analysis ◽  
Citrate Synthase ◽  
Fragaria X Ananassa ◽  
Cloning And Expression ◽  
Mitochondrial Malate Dehydrogenase

scholarly journals Effect of Nitric Oxide on the Interaction Between Mitochondrial Malate Dehydrogenase and Citrate Synthase

2014 ◽  
Vol 13 (12) ◽  
pp. 2616-2624
Author(s):  
Yu-chen LIU ◽  
Juan WANG ◽  
Pei-ying SU ◽  
Chun-mei MA ◽  
Shu-hua ZHU
Keyword(s):  
Nitric Oxide ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Mitochondrial Malate Dehydrogenase
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