Evidence for Electrostatic Channeling in a Fusion Protein of Malate Dehydrogenase and Citrate Synthase†

Biochemistry ◽  
1996 ◽  
Vol 35 (39) ◽  
pp. 12652-12658 ◽  
Author(s):  
Adrian H. Elcock ◽  
J. Andrew McCammon
Keyword(s):  
Fusion Protein ◽  
Malate Dehydrogenase ◽  
Citrate Synthase

Preparation and kinetic characterization of a fusion protein of yeast mitochondrial citrate synthase and malate dehydrogenase

Biochemistry ◽  
1994 ◽  
Vol 33 (39) ◽  
pp. 11692-11698 ◽  
Author(s):  
C. Lindbladh ◽  
M. Rault ◽  
C. Hagglund ◽  
W. C. Small ◽  
K. Mosbach ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Kinetic Characterization

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

Kinetics of the coupled reaction catalysed by a fusion protein of yeast mitochondrial malate dehydrogenase and citrate synthase

2000 ◽  
Vol 267 (16) ◽  
pp. 5041-5046 ◽  
Author(s):  
Henrik Pettersson ◽  
Peter Olsson ◽  
Leif Bülow ◽  
Gösta Pettersson
Keyword(s):  
Fusion Protein ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Kinetics Of ◽  
Mitochondrial Malate Dehydrogenase ◽  
Coupled Reaction

scholarly journals Quantitation of the interaction between citrate synthase and malate dehydrogenase.

1987 ◽  
Vol 262 (13) ◽  
pp. 6089-6092
Author(s):  
P. Tompa ◽  
J. Batke ◽  
J. Ovadi ◽  
G.R. Welch ◽  
P.A. Srere
Keyword(s):  
Malate Dehydrogenase ◽  
Citrate Synthase

Polyethylene glycol-induced heteroassociation of malate dehydrogenase and citrate synthase

1987 ◽  
Vol 258 (1) ◽  
pp. 132-142 ◽  
Author(s):  
J.M. Merz ◽  
T.A. Webster ◽  
J.R. Appleman ◽  
E.R. Manley ◽  
H.-A. Yu ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Malate Dehydrogenase ◽  
Citrate Synthase

scholarly journals Association of the malate dehydrogenase-citrate synthase metabolon is modulated by intermediates of the Krebs tricarboxylic acid cycle

2021 ◽  
Author(s):  
Joy Omini ◽  
Izabela Wojciechowska ◽  
Aleksandra Skirycz ◽  
Hideaki Moriyama ◽  
Toshihiro Obata
Keyword(s):  
Malate Dehydrogenase ◽  
Metabolic Flux ◽  
Citrate Synthase ◽  
Tricarboxylic Acid Cycle ◽  
Feedback Regulation ◽  
Dynamic Structure ◽  
Tca Cycle ◽  
Tricarboxylic Acid ◽  
Enzyme Complex ◽  
Acetyl Coa

Mitochondrial malate dehydrogenase (MDH)-citrate synthase (CS) multi-enzyme complex is a part of the Krebs tricarboxylic acid (TCA) cycle 'metabolon' which is enzyme machinery catalyzing sequential reactions without diffusion of reaction intermediates into a bulk matrix. This complex is assumed to be a dynamic structure involved in the regulation of the cycle by enhancing metabolic flux. Microscale Thermophoresis analysis of the porcine heart MDH-CS complex revealed that substrates of the MDH and CS reactions, NAD+ and acetyl-CoA, enhance complex association while products of the reactions, NADH and citrate, weaken the affinity of the complex. Oxaloacetate enhanced the interaction only when it was presented together with acetyl-CoA. Structural modeling using published CS structures suggested that the binding of these substrates can stabilize the closed format of CS which favors the MDH-CS association. Two other TCA cycle intermediates, ATP, and low pH also enhanced the association of the complex. These results suggest that dynamic formation of the MDH-CS multi-enzyme complex is modulated by metabolic factors responding to respiratory metabolism, and it may function in the feedback regulation of the cycle and adjacent metabolic pathways.

Muscle enzyme adaptations to added load during training and nontraining hours in rats

1991 ◽  
Vol 70 (2) ◽  
pp. 764-769 ◽  
Author(s):  
H. Rusko ◽  
C. Bosco ◽  
J. Komulainen ◽  
A. Leinonen ◽  
V. Vihko
Keyword(s):  
Creatine Kinase ◽  
Endurance Training ◽  
Dehydrogenase Activity ◽  
Malate Dehydrogenase ◽  
Enzyme Activities ◽  
Citrate Synthase ◽  
Effective Means ◽  
Sedentary Control ◽  
Muscle Enzyme ◽  
Gastrocnemius Muscles

The effects of added load (20% of body mass) on the selected enzyme activities of red and white quadriceps femoris (QF), soleus, and gastrocnemius muscles of rats were studied. The rats were divided into sedentary control (SC), sedentary control with added load (SC+AL), endurance training (ET), and endurance training with added load (ET+AL) groups (n = 10 rats/group). After 6 wk, the SC+AL group had 57% higher (P less than 0.001) beta-glucuronidase (beta-GU) activity and 24% lower (P less than 0.05) citrate synthase activity in white QF than SC. Citrate synthase activity was also decreased in red QF (P less than 0.05) after the added load was used during nontraining hours. The training with added load induced similar but more pronounced changes than normal endurance training, especially in white QF. The ET+AL group demonstrated higher citrate synthase activity in white QF (P less than 0.001) and gastrocnemius (P less than 0.01) and higher malate dehydrogenase activity (P less than 0.05) and beta-GU activity (P less than 0.001) in white QF than the ET group. ET+AL rats also had higher phosphofructokinase (P less than 0.01) and lower creatine kinase (P less than 0.001) activity in white QF than ET rats. In conclusion, the added load without training had minor adaptive influences on muscles. The added load during training hours seemed to be an effective means of influencing the activation and adaptation in muscles that contain fast glycolytic fibers.

pH-mediated control of anti-aggregation activities of cyanobacterial and E. coli chaperonin GroELs

2020 ◽  
Author(s):  
Tahmina Akter ◽  
Hitoshi Nakamoto
Keyword(s):  
Escherichia Coli ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Ph Dependence ◽  
Chaperone Activity ◽  
Ph Change ◽  
Aggregation Assay ◽  
E Coli ◽  
Aggregation Activity

Abstract In contrast to Escherichia coli, cyanobacteria have multiple GroELs, the bacterial homologues of chaperonin/Hsp60. We have shown that cyanobacterial GroELs are mutually distinct and different from E. coli GroEL with which the paradigm for chaperonin structure/function has been established. However, little is known about regulation of cyanobacterial GroELs. This study investigated effect of pH (varied from 7.0 to 8.5) on chaperone activity of GroEL1 and GroEL2 from the cyanobacterium Synechococcus elongatus PCC7942 and E. coli GroEL. GroEL1 and GroEL2 showed pH dependency in suppression of aggregation of heat-denatured malate dehydrogenase, lactate dehydrogenase and citrate synthase. They exhibited higher anti-aggregation activity at more alkaline pHs. Escherichia coli GroEL showed a similar pH-dependence in suppressing aggregation of heat-denatured lactate dehydrogenase. No pH dependence was observed in all the GroELs when urea-denatured lactate dehydrogenase was used for anti-aggregation assay, suggesting that the pH-dependence is related to some denatured structures. There was no significant influence of pH on the chaperone activity of all the GroELs to promote refolding of heat-denatured malate dehydrogenase. It is known that pH in cyanobacterial cytoplasm increases by one pH unit following a shift from darkness to light, suggesting that the pH-change modulates chaperone activity of cyanobacterial GroEL1 and GroEL2.

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.

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