The Role of Malate Dehydrogenase Isoforms in the Regulation of Anabolic and Catabolic Processes in the Colorless Sulfur Bacterium Beggiatoa leptomitiformis D-402

Епринцев, А. Т.; Фалалеева, М. И.; Grabovich, M. Yu.; Parfenova, N. V.; Kashirskaya, N. N.; Дубинина, Г. А.

doi:10.1023/b:mici.0000036977.79822.7a

Cited by 9 publications

(8 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A decrease in the tempera ture of cultivation results in the decomposition of the tetrameric MDH into the inactive dimers and trimers. The thermostability of the dimeric and tetrameric MDH from thermophilic and mesophilic bacteria correlates with the temperature of growth [10].Previously, our investigations [11,12] and the works of other authors [8] demonstrated that the rearrangement of the oligomeric structure of MDH from Beggiatoa lep tomitiformis and Bacillus sp. resulted in important changes in metabolism providing the adaptation to the environ mental conditions.…”

mentioning

confidence: 71%

Malate Dehydrogenase from the Thermophilic Bacterium Vulcanithermus medioatlanticus

Епринцев

Фалалеева

Parfyonova

2005

Biochemistry (Moscow)

Self Cite

View full text Add to dashboard Cite

Thermostable dimeric malate dehydrogenase (MDH) was isolated from the microorganism of hydrothermal vents Vulcanithermus medioatlanticus. The enzyme was electrophoretically homogeneous and possessed the specific activity of 6.9 U/mg. The large molecular weight of the subunits (55 kD) is likely to provide the rigidity of the enzyme structure (the activation energy of the enzymatic reaction is 32.6 kJ/mol). The thermophilic MDH differs little from the mesophilic enzyme in terms of kinetic and regulatory characteristics.

show abstract

mentioning

confidence: 71%

Malate Dehydrogenase from the Thermophilic Bacterium Vulcanithermus medioatlanticus

Епринцев

Фалалеева

Parfyonova

2005

Biochemistry (Moscow)

Self Cite

View full text Add to dashboard Cite

show abstract

“…The hypothetical syntrophic Spirochaeta sp. are physiologically identical to Dubinina's aerotolerant ones: substratelevel phosphorylation generated by glycolysis pathways was enhanced by ambient oxygen in the spirochetes with their minimal oxygen metabolism-acetogenesis by pyruvate oxidation and exopolysaccharide production (41). The microxic, more efficient glucose oxidation preadapted spirochetes for association with Thermoplasma.…”

Section: Karyomastigont Evolved From Attached Symbiotic Aerotolerant mentioning

confidence: 88%

“…The sulfate-reducing physiology suggested the spirochete's partner was a Desulfovibrio. Further work identified at least two new genera (i.e., Desulfobacter and Dethiosulfovibrio) as the sulfidogens (41). In all ''Thiodendrons'' studied, the spirochete partners, based on swimming behavior, electron microscopic morphology, metabolism, and 16S rRNA, classify as Spirochaeta sp.…”

Section: Karyomastigont Evolved From Attached Symbiotic Aerotolerant mentioning

confidence: 99%

See 1 more Smart Citation

The last eukaryotic common ancestor (LECA): Acquisition of cytoskeletal motility from aerotolerant spirochetes in the Proterozoic Eon

Margulis

Chapman

Guerrero

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

124

View full text Add to dashboard Cite

We develop a symbiogenetic concept of the origin of eukaryotic intracellular motility systems from anaerobic but aerotolerant spirochetes in sulfide-rich environments. The last eukaryotic common ancestors (LECAs) have extant archaeprotist descendants: motile nucleated cells with Embden-Meyerhof glycolysis and substrate-level phosphorylation that lack the ␣-proteobacterial symbiont that became the mitochondrion. Swimming and regulated O 2-tolerance via sulfide oxidation already had been acquired by sulfidogenic wall-less archaebacteria (thermoplasmas) after aerotolerant cytoplasmictubule-containing spirochetes (eubacteria) attached to them. Increasing stability of sulfide-oxidizing͞sulfur-reducing consortia analogous to extant sulfur syntrophies (Thiodendron) led to fusion. The eubacteria-archaebacteria symbiosis became permanent as the nucleus evolved by prokaryotic recombination with membrane hypertrophy, analogous to Gemmata obscuriglobus and other ␦-proteobacteria with membrane-bounded nucleoids. Histone-coated DNA, proteinsynthetic RNAs, amino-acylating, and other enzymes were contributed by the sulfidogen whereas most intracellular motility derives from the spirochete. From this redox syntrophy in anoxic and microoxic Proterozoic habitats LECA evolved. The nucleus originated by recombination of eu-and archaebacterial DNA that remained attached to eubacterial motility structures and became the microtubular cytoskeleton, including the mitotic apparatus. Direct LECA descendants include free-living archaeprotists in anoxic environments: archamoebae, metamonads, parabasalids, and some mammalian symbionts with mitosomes. LECA later acquired the fully aerobic Krebs cycle-oxidative phosphorylation-mitochondrial metabolism by integration of the protomitochondrion, a third ␣-proteobacterial symbiont from which the ancestors to most protoctists, all fungi, plants, and animals evolved. Secondarily anaerobic eukaryotes descended from LECA after integration of this oxygen-respiring eubacterium. Explanatory power and experimental predictions for molecular biology of the LECA concept are stated.karyomastigont ͉ kinetosome-centriole ͉ mitotic apparatus ͉ nucleus origin ͉ Thiodendron

show abstract

“…Two MDH isoforms have been characterized in R. sphaeroides 2R, R. palustris f-8pt, and B. leptomitiformis D-402. The dimeric isoforms participate in the TCA cycle, and the tetrameric isoforms participate in the glyoxylate cycle (Eprintsev et al, 2004;2008a;2008b;2009b).…”

Section: Function Of Malate Dehydrogenasementioning

confidence: 99%

Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase

Takahashi-Íñiguez

Aburto-Rodríguez

Vilchis-González

et al. 2016

J. Zhejiang Univ. Sci. B

View full text Add to dashboard Cite

Abstract:Malate dehydrogenase (MDH) is an enzyme widely distributed among living organisms and is a key protein in the central oxidative pathway. It catalyzes the interconversion between malate and oxaloacetate using NAD + or NADP + as a cofactor. Surprisingly, this enzyme has been extensively studied in eukaryotes but there are few reports about this enzyme in prokaryotes. It is necessary to review the relevant information to gain a better understanding of the function of this enzyme. Our review of the data generated from studies in bacteria shows much diversity in their molecular properties, including weight, oligomeric states, cofactor and substrate binding affinities, as well as differences in the direction of the enzymatic reaction. Furthermore, due to the importance of its function, the transcription and activity of this enzyme are rigorously regulated. Crystal structures of MDH from different bacterial sources led to the identification of the regions involved in substrate and cofactor binding and the residues important for the dimer-dimer interface. This structural information allows one to make direct modifications to improve the enzyme catalysis by increasing its activity, cofactor binding capacity, substrate specificity, and thermostability. A comparative analysis of the phylogenetic reconstruction of MDH reveals interesting facts about its evolutionary history, dividing this superfamily of proteins into two principle clades and establishing relationships between MDHs from different cellular compartments from archaea, bacteria, and eukaryotes.

show abstract

The Role of Malate Dehydrogenase Isoforms in the Regulation of Anabolic and Catabolic Processes in the Colorless Sulfur Bacterium Beggiatoa leptomitiformis D-402

Cited by 9 publications

References 9 publications

Malate Dehydrogenase from the Thermophilic Bacterium Vulcanithermus medioatlanticus

Malate Dehydrogenase from the Thermophilic Bacterium Vulcanithermus medioatlanticus

The last eukaryotic common ancestor (LECA): Acquisition of cytoskeletal motility from aerotolerant spirochetes in the Proterozoic Eon

Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase

Contact Info

Product

Resources

About