PYRUVATE DEHYDROGENASE COMPLEX FROM <i>Azotohacter vinelandii:</i> STRUCTURE, FUNCTION, AND INTER‐ENZYME CATALYSIS*

Bosma, H.J.; Graaf-Hess, A.C. de; Kok, A. de; Veeger, C.; Visser, A.J.W.G.; Voordouw, Gerrit

doi:10.1111/j.1749-6632.1982.tb31202.x

Cited by 24 publications

(7 citation statements)

References 27 publications

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“…The recovered correlation time of 24 ns, however, is too short to account for a spherical rotor of 102 kDa (39 ns at 20°C, see also table 1). Exactly the same result was obtained earlier for the .4zotobacter vinelandii lipoamide dehydrogenase [14,15]. The shorter correlation time than expected was ascribed to a hinged subunit movement.…”

Section: Fluorescence Anisotropy Decaysupporting

confidence: 75%

Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time‐resolved flavin fluorescence

Kok

Visser

1987

FEBS Letters

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Subnanosecond-resolved fluorescence measurements of the FAD bound in glutathione reductase and lipoamide dehydrogenase revealed characteristic differences in dynamic properties of both enzymes, which are considered to have common structural features. The flavin fluorescence in glutathione reductase is quenched mainly via a dynamic mechanism, in agreement with enhanced flexibility of the flavin as inferred from rapid depolarization of the fluorescence.

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Section: Fluorescence Anisotropy Decaysupporting

confidence: 75%

Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time‐resolved flavin fluorescence

Kok

Visser

1987

FEBS Letters

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“…Pdhc from Azotobacter (Bosma et al, ), Escherichia (Hansen and Henning, ), and Enterococcus (Snoep et al, ) is active in both aerobic and anaerobic systems. By contrast, Pfl from Escherichia (Nnyepi et al, ), Staphylococcus (Leibig et al, ), and Streptococcus (Abbe et al, ; Lindmark et al, ), and Pfo from Clostridium (Uyeda and Rabinowitz, ) are inhibited by oxygen and therefore primarily active in anaerobic systems.…”

Section: Review Of Metabolic Pathwaysmentioning

confidence: 99%

Regulation mechanisms in mixed and pure culture microbial fermentation

Hoelzle

Virdis

Batstone

2014

Biotech & Bioengineering

101

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Mixed-culture fermentation is a key central process to enable next generation biofuels and biocommodity production due to economic and process advantages over application of pure cultures. However, a key limitation to the application of mixed-culture fermentation is predicting culture product response, related to metabolic regulation mechanisms. This is also a limitation in pure culture bacterial fermentation. This review evaluates recent literature in both pure and mixed culture studies with a focus on understanding how regulation and signaling mechanisms interact with metabolic routes and activity. In particular, we focus on how microorganisms balance electron sinking while maximizing catabolic energy generation. Analysis of these mechanisms and their effect on metabolism dynamics is absent in current models of mixed-culture fermentation. This limits process prediction and control, which in turn limits industrial application of mixed-culture fermentation. A key mechanism appears to be the role of internal electron mediating cofactors, and related regulatory signaling. This may determine direction of electrons towards either hydrogen or reduced organics as end-products and may form the basis for future mechanistic models.

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“…According to activity determinations in cell-free extracts, the C. glutamicum pyruvate dehydrogenase complex is not subject to any significant regulation that could modulate its activity [237,238]. This is surprising since in other bacteria and in eukaryotic organisms the activity of the complex is controlled by various metabolites [217,[241][242][243][244]. However, there is a need for purification and biochemical Fig.…”

Section: The Pep-pyruvate-oxaloacetate Node In C Glutamicummentioning

confidence: 99%

The PEP—pyruvate—oxaloacetate node as the switch point for carbon flux distribution in bacteria: We dedicate this paper to Rudolf K. Thauer, Director of the Max-Planck-Institute for Terrestrial Microbiology in Marburg, Germany, on the occasion of his 65th birthday

2005

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In many organisms, metabolite interconversion at the phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node involves a structurally entangled set of reactions that interconnects the major pathways of carbon metabolism and thus, is responsible for the distribution of the carbon flux among catabolism, anabolism and energy supply of the cell. While sugar catabolism proceeds mainly via oxidative or non-oxidative decarboxylation of pyruvate to acetyl-CoA, anaplerosis and the initial steps of gluconeogenesis are accomplished by C3- (PEP- and/or pyruvate-) carboxylation and C4- (oxaloacetate- and/or malate-) decarboxylation, respectively. In contrast to the relatively uniform central metabolic pathways in bacteria, the set of enzymes at the PEP-pyruvate-oxaloacetate node represents a surprising diversity of reactions. Variable combinations are used in different bacteria and the question of the significance of all these reactions for growth and for biotechnological fermentation processes arises. This review summarizes what is known about the enzymes and the metabolic fluxes at the PEP-pyruvate-oxaloacetate node in bacteria, with a particular focus on the C3-carboxylation and C4-decarboxylation reactions in Escherichia coli, Bacillus subtilis and Corynebacterium glutamicum. We discuss the activities of the enzymes, their regulation and their specific contribution to growth under a given condition or to biotechnological metabolite production. The present knowledge unequivocally reveals the PEP-pyruvate-oxaloacetate nodes of bacteria to be a fascinating target of metabolic engineering in order to achieve optimized metabolite production.

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PYRUVATE DEHYDROGENASE COMPLEX FROM Azotohacter vinelandii: STRUCTURE, FUNCTION, AND INTER‐ENZYME CATALYSIS*

Cited by 24 publications

References 27 publications

Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time‐resolved flavin fluorescence

Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time‐resolved flavin fluorescence

Regulation mechanisms in mixed and pure culture microbial fermentation

The PEP—pyruvate—oxaloacetate node as the switch point for carbon flux distribution in bacteria: We dedicate this paper to Rudolf K. Thauer, Director of the Max-Planck-Institute for Terrestrial Microbiology in Marburg, Germany, on the occasion of his 65th birthday

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