Thermoacidophilic Archaebacteria Contain Bacterial-Type Ferredoxins Acting as Electron Acceptors of 2-Oxoacid: Ferredoxin Oxidoreductases

Kerscher, Lorenz; Nowitzki, Susanne; Oesterhelt, Dieter

doi:10.1111/j.1432-1033.1982.tb06955.x

Cited by 71 publications

(16 citation statements)

References 33 publications

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“…7), suggesting that this E1p ␣-subunit gene has been recruited via gene transfer from the gram-positive bacteria. The obvious absence of PDHCs in other archaea (70) is in agreement with the finding that the oxidative decarboxylation of pyruvate is generally catalyzed by pyruvate:ferredoxin oxidoreductases in archaea (31,32,47).…”

Section: Discussionsupporting

confidence: 75%

E1 Enzyme of the Pyruvate Dehydrogenase Complex in Corynebacterium glutamicum : Molecular Analysis of the Gene and Phylogenetic Aspects

et al. 2005

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The E1p enzyme is an essential part of the pyruvate dehydrogenase complex (PDHC) and catalyzes the oxidative decarboxylation of pyruvate with concomitant acetylation of the E2p enzyme within the complex. We analyzed the Corynebacterium glutamicum aceE gene, encoding the E1p enzyme, and constructed and characterized an E1p-deficient mutant. Sequence analysis of the C. glutamicum aceE gene and adjacent regions revealed that aceE is not flanked by genes encoding other enzymes of the PDHC. Transcriptional analysis revealed that aceE from C. glutamicum is monocistronic and that its transcription is initiated 121 nucleotides upstream of the translational start site. Inactivation of the chromosomal aceE gene led to the inability to grow on glucose and to the absence of PDHC and E1p activities, indicating that only a single E1p enzyme is present in C. glutamicum and that the PDHC is essential for the growth of this organism on carbohydrate substrates. Surprisingly, the E1p enzyme of C. glutamicum showed up to 51% identity to homodimeric E1p proteins from gram-negative bacteria but no similarity to E1 ␣-or ␤-subunits of heterotetrameric E1p enzymes which are generally assumed to be typical for gram-positives. To investigate the distribution of E1p enzymes in bacteria, we compiled and analyzed the phylogeny of 46 homodimeric E1p proteins and of 58 ␣-subunits of heterotetrameric E1p proteins deposited in public databases. The results revealed that the distribution of homodimeric and heterotetrameric E1p subunits in bacteria is not in accordance with the rRNA-based phylogeny of bacteria and is more heterogeneous than previously assumed.The pyruvate dehydrogenase complex (PDHC) represents a member of a multienzyme complex family that also comprises the 2-oxoglutarate dehydrogenase complex (OGDHC) and the branched-chain 2-oxoacid dehydrogenase complex (BCOADHC). These enzymes catalyze the oxidative decarboxylation of pyruvate, 2-oxoglutarate, and the 2-oxo acids of the branched-chain amino acids L-leucine, L-valine, and L-isoleucine, respectively. In general, the multienzyme complexes are composed of multiple copies of three different enzymes, a thiamine pyrophosphate (TPP) containing 2-oxoacid decarboxylase (E1), a lipoic acid-containing dihydrolipoamide acyltransferase (E2), and the flavin-containing lipoamide dehydrogenase (LPD). The E1 enzyme catalyzes the irreversible, TPP-dependent oxidative decarboxylation of the 2-oxoacid, followed by the acylation of the lipoyl prosthetic group covalently attached to the E2 chain. The E2 component catalyzes the transfer of the acyl group from the lipoyl group to coenzyme A (CoA). The resulting dihydrolipoyl group is reoxidized by LPD, generating NADH and H ϩ from NAD ϩ (for a recent review, see reference 11). The E1 and E2 enzymes are specific for each of the three multienzyme complexes and therefore specified as E1p and E2p in the PDHC, E1o and E2o in the OGDHC, and E1b, and E2b in the BCOADHC. In contrast, the LPD component is common in the three multienzyme complexes in most organ...

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Section: Discussionsupporting

confidence: 75%

E1 Enzyme of the Pyruvate Dehydrogenase Complex in Corynebacterium glutamicum : Molecular Analysis of the Gene and Phylogenetic Aspects

et al. 2005

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“…The physiological significance of bacterial-type ferredoxins in the aerobic and thermoacidophilic archaea, such as Sulfolobus and Thermoplasma , was first recognized by Kerscher et al [15], who demonstrated that ferredoxins are abundant in the cytoplasm and serve as an effective electron acceptor of a coenzyme A-acylating 2-oxoacid:ferredoxin oxidoreductase. It is a key Fe-S enzyme of the oxidative tricarboxylic acid cycle and of coenzyme A-dependent pyruvate oxidation in aerobic archaea [15, 16, 27–30].…”

Section: Zinc-containing Ferredoxins Are Abundant In the Aerobic Amentioning

confidence: 99%

Iron-Sulfur World in Aerobic and Hyperthermoacidophilic ArchaeaSulfolobus

Iwasaki

2010

Archaea

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The general importance of the Fe-S cluster prosthetic groups in biology is primarily attributable to specific features of iron and sulfur chemistry, and the assembly and interplay of the Fe-S cluster core with the surrounding protein is the key to in-depth understanding of the underlying mechanisms. In the aerobic and thermoacidophilic archaea, zinc-containing ferredoxin is abundant in the cytoplasm, functioning as a key electron carrier, and many Fe-S enzymes are produced to participate in the central metabolic and energetic pathways. De novo formation of intracellular Fe-S clusters does not occur spontaneously but most likely requires the operation of a SufBCD complex of the SUF machinery, which is the only Fe-S cluster biosynthesis system conserved in these archaea. In this paper, a brief introduction to the buildup and maintenance of the intracellular Fe-S world in aerobic and hyperthermoacidophilic crenarchaeotes, mainly Sulfolobus, is given in the biochemical, genetic, and evolutionary context.

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“…(Electron micrograph courtesy of Sonja-Verena Albers, Max Planck Institute, Marburg, Germany, reproduced with permission.) ferredoxin oxidoreductase to acetyl-CoA (473,495), which enters the oxidative CAC, forming precursor molecules for anabolism as well as CO 2 . Reducing equivalents are transferred to a branched electron transfer chain (3 terminal oxidases), with O 2 as the terminal electron acceptor (aerobic respiration) (496,497).…”

Section: Sulfolobus Solfataricusmentioning

confidence: 99%

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Bräsen

Esser

Rauch

et al. 2014

Microbiol Mol Biol Rev

271

294

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SUMMARY The metabolism of Archaea , the third domain of life, resembles in its complexity those of Bacteria and lower Eukarya . However, this metabolic complexity in Archaea is accompanied by the absence of many “classical” pathways, particularly in central carbohydrate metabolism. Instead, Archaea are characterized by the presence of unique, modified variants of classical pathways such as the Embden-Meyerhof-Parnas (EMP) pathway and the Entner-Doudoroff (ED) pathway. The pentose phosphate pathway is only partly present (if at all), and pentose degradation also significantly differs from that known for bacterial model organisms. These modifications are accompanied by the invention of “new,” unusual enzymes which cause fundamental consequences for the underlying regulatory principles, and classical allosteric regulation sites well established in Bacteria and Eukarya are lost. The aim of this review is to present the current understanding of central carbohydrate metabolic pathways and their regulation in Archaea . In order to give an overview of their complexity, pathway modifications are discussed with respect to unusual archaeal biocatalysts, their structural and mechanistic characteristics, and their regulatory properties in comparison to their classic counterparts from Bacteria and Eukarya . Furthermore, an overview focusing on hexose metabolic, i.e., glycolytic as well as gluconeogenic, pathways identified in archaeal model organisms is given. Their energy gain is discussed, and new insights into different levels of regulation that have been observed so far, including the transcript and protein levels (e.g., gene regulation, known transcription regulators, and posttranslational modification via reversible protein phosphorylation), are presented.

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Thermoacidophilic Archaebacteria Contain Bacterial-Type Ferredoxins Acting as Electron Acceptors of 2-Oxoacid: Ferredoxin Oxidoreductases

Cited by 71 publications

References 33 publications

E1 Enzyme of the Pyruvate Dehydrogenase Complex in Corynebacterium glutamicum : Molecular Analysis of the Gene and Phylogenetic Aspects

E1 Enzyme of the Pyruvate Dehydrogenase Complex in Corynebacterium glutamicum : Molecular Analysis of the Gene and Phylogenetic Aspects

Iron-Sulfur World in Aerobic and Hyperthermoacidophilic ArchaeaSulfolobus

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

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