Where is malate dehydrogenase located

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View Metrics. Email alerts Article activity alert. Advance article alerts. New issue alert. Malate dehydrogenase has been extensively studied due to its many isozymes [2]. The enzyme exists in two subcellular locations: mitochondria and cytoplasm.

In the mitochondria, the enzyme catalyzes the reaction of malate to oxaloacetate; however, in the cytoplasm, the enzyme catalyzes oxaloacetate to malate to allow transport [3]. This conversion is an essential catalytic step in each different metabolic mechanism. The enzyme malate dehydrogenase is composed of either a dimer or tetramer depending on the location of the enzyme and the organism it is located in [4]. During catalysis, the enzyme subunits are non-cooperative between active sites.

The mitochondrial MDH suffers a complex allosteric control by citrate, but no other known metabolic regulation mechanisms have been discovered. Further, the exact mechanism of regulation has yet to be discovered [5].

The optimal pH is 7. For halophilic MDH details, see Halophilic malate dehydrogenase. Similar results were observed under photoheterotrophic, nitrogen-limited, and dark conditions Nakajima et al.

In vivo studies have shown that many genes of the cyanobacterial TCA cycle are unnecessary for normal growth Broddrick et al. Therefore, the oxidative reaction of Sy MDH is also thought to be unnecessary in cyanobacteria, because fumarase-deficient cyanobacteria grow normally.

These studies support our biochemical studies suggesting that the oxidative reaction of Sy MDH is very weak and almost non-functional. Our study revealed that Sy MDH shows a higher affinity for substances produced through the reductive reaction than those produced through the oxidative reaction, similar to MDHs derived from anaerobic microorganisms in which the oxidative TCA cycle seems to be barely functioning.

Cyanobacteria have been found to close the TCA cycle using various bypasses Zhang and Bryant, ; Steinhauser et al. However, the results in this study indicate that the oxidative TCA cycle of Synechocystis may be functionally linear, and not cyclic in nature, because Sy MDH preferentially undergoes a reductive reaction rather than an oxidative reaction and turns off the cyclic process of the oxidative TCA cycle.

MT designed the research, performed the experiments, analysed the data, and wrote the manuscript. SI analysed the data. HS performed the experiments. TO analysed the data and wrote the manuscript. The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. Bennett, B. Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli.

Beyer, S. Transcription of genes coding for metabolic key functions in Nitrosomonas europaea during aerobic and anaerobic growth. Broddrick, J.

Unique attributes of cyanobacterial metabolism revealed by improved genome-scale metabolic modeling and essential gene analysis. Cendrin, F. Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui.

Biochemistry 32, — Coleman, J. Inorganic carbon accumulation and photosynthesis in a blue-green alga as a function of external pH. Plant Physiol. Deutch, C. L-Malate dehydrogenase activity in the reductive arm of the incomplete citric acid cycle of Nitrosomonas europaea.

Antonie Van Leeuwenhoek , — Eszes, C. Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue change. FEBS Lett. Ge, Y. Identification and biochemical characterization of a thermostable malate dehydrogenase from the mesophile Streptomyces coelicolor A3 2. Harmsen, H.

Detection and localization of syntrophic propionate-oxidizing bacteria in granular sludge by in situ hybridization using 16S rRNA-based oligonucleotide probes. PubMed Abstract Google Scholar.

Hasunuma, T. Improved sugar-free succinate production by Synechocystis sp. PCC following identification of the limiting steps in glycogen catabolism. Honka, E. Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus. Huynen, M. Variation and evolution of the citric-acid cycle: a genomic perspective.

Trends Microbiol. Ito, S. Substrate specificity and allosteric regulation of a d-lactate dehydrogenase from a unicellular cyanobacterium are altered by an amino acid substitution. Knoop, H.

Flux balance analysis of cyanobacterial metabolism: the metabolic network of Synechocystis sp. PCC PLoS Comput. Labrou, N. L-Malate dehydrogenase from Pseudomonas stutzeri : purification and characterization.

Mangan, N. Matsunaga, T. Glutamate production from CO 2 by marine cyanobacterium Synechococcus sp. Purification and characterization of the malate dehydrogenase from Streptomyces aureofaciens. FEMS Microbiol. Malate dehydrogenases structure and function. Google Scholar. Molenaar, D. Biochemical and genetic characterization of the membrane associated malate dehydrogenase acceptor from Corynebacterium glutamicum. Muro-Pastor, M. Purification and properties of NADP-isocitrate dehydrogenase from the unicellular cyanobacterium Synechocystis sp.

Nakajima, T. Integrated metabolic flux and omics analysis of Synechocystis sp. PCC under mixotrophic and photoheterotrophic conditions. Plant Cell Physiol. Metabolic flux analysis of the Synechocystis sp.