Characterization of the<scp>d</scp>-Xylulose 5-Phosphate/<scp>d</scp>-Fructose 6-Phosphate Phosphoketolase Gene (<i>xfp</i>) from<i>Bifidobacterium lactis</i>

Meile, Léo; Rohr, Lukas M.; Geissmann, Thomas; Herensperger, Monique; Teuber, Michael

doi:10.1128/jb.183.9.2929-2936.2001

Cited by 110 publications

(110 citation statements)

References 30 publications

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“…Here the TPP-dependent enzymes are classified into six groups (Figure 1) in which the domains are alternatively arranged in the primary structure, or appear on different subunits. Enzymes of the TK-like group (TK; DXPS; dihydroxyacetone synthase (DHAS); and phosphoketolase (PKL)) contain the PP-, Pyr-and TKC-domains on the same subunit, and are homodimeric, except PKL which is a homohexamer (Meile et al 2001). The 2-oxoisovalerate dehydrogenase (2OXO) -like enzymes form the E1 subunits of large multienzyme complexes, and differ from the TK-like enzymes in that the PP-domain is found on a different subunit to the Pyr-and TKC-domains.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary Analysis of the TPP-Dependent Enzyme Family

2007

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The evolutionary relationships of the thiamine pyrophosphate (TPP) dependent family of enzymes was investigated by generation of a neighbor joining (NJ) phylogenetic tree using sequences from the conserved pyrophosphate (PP) and pyrimidine (Pyr) binding domains of 17 TPP-dependent enzymes.This represents the most comprehensive analysis of TPP-dependent enzyme evolution to date. The phylogeny was shown to be robust by comparison with maximum likelihood (ML) trees generated for each individual enzyme. The study discerned the order in which enzymes diverged in the progenote population and several instances where enzyme types diverged later, and broadly confirms the evolutionary history proposed recently from structural comparisons alone (Duggleby 2006). The relationship between the PP-and Pyr-domains and the recruitment of additional protein domains was examined using the transketolase C-terminal (TKC) domain as an example. This domain has been recruited by several members of the family and yet forms no part of the active site and has unknown function. Removal of the TKC-domain was found to increase activity towards β-hydroxypyruvate (HPA) and glycolaldehyde (GA). Further truncations of the Pyr-domain yielded several variants with retained activity. This suggests the influence of TKC-domain recruitment on the evolution of the mechanism and specificity of transketolase (TK) has been minor, and that the smallest functioning unit of TK comprises the PP-and Pyr-domains whose evolutionary histories extend to all TPP-dependent enzymes.

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Section: Introductionmentioning

confidence: 99%

Evolutionary Analysis of the TPP-Dependent Enzyme Family

2007

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“…: one specific for F6P and one that recognizes both X5P and F6P (XFP) on May 12, 2018 by guest http://mmbr.asm.org/ (301). The xfp gene, which encodes the dual-substrate enzyme, resides just upstream of pta (301).…”

Section: Other Acetylϳp-forming Enzymesmentioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,066

1,274

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To succeed, many cells must alternate between life-styles that permit rapid growth in the presence of abundant nutrients and ones that enhance survival in the absence of those nutrients. One such change in life-style, the “acetate switch,” occurs as cells deplete their environment of acetate-producing carbon sources and begin to rely on their ability to scavenge for acetate. This review explains why, when, and how cells excrete or dissimilate acetate. The central components of the “switch” (phosphotransacetylase [PTA], acetate kinase [ACK], and AMP-forming acetyl coenzyme A synthetase [AMP-ACS]) and the behavior of cells that lack these components are introduced. Acetyl phosphate (acetyl∼P), the high-energy intermediate of acetate dissimilation, is discussed, and conditions that influence its intracellular concentration are described. Evidence is provided that acetyl∼P influences cellular processes from organelle biogenesis to cell cycle regulation and from biofilm development to pathogenesis. The merits of each mechanism proposed to explain the interaction of acetyl∼P with two-component signal transduction pathways are addressed. A short list of enzymes that generate acetyl∼P by PTA-ACKA-independent mechanisms is introduced and discussed briefly. Attention is then directed to the mechanisms used by cells to “flip the switch,” the induction and activation of the acetate-scavenging AMP-ACS. First, evidence is presented that nucleoid proteins orchestrate a progression of distinct nucleoprotein complexes to ensure proper transcription of its gene. Next, the way in which cells regulate AMP-ACS activity through reversible acetylation is described. Finally, the “acetate switch” as it exists in selected eubacteria, archaea, and eukaryotes, including humans, is described

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“…1) [5,25]. Two types of enzymes have been described in Bifidobacterium to date: a specific enzyme acting on fructose-6-phosphate, which catalyses the conversion of this substrate to erythrose-4-phosphate and acetyl-phosphate, and a dual enzyme Figure 1.…”

Section: Some Interesting Features Of the Bifidus Pathwaymentioning

confidence: 99%

“…Short schematic representation of the main steps of the fructose-6-phosphate shunt in Bifidobacterium [4,25]. which can also act on xylulose-5-phosphate, rendering acetyl-phosphate and glyceraldehyde-3-phosphate [13,25]. The acetyl-phosphate is converted to acetate with the production of 1 mol of ATP, whereas the glyceraldehyde-3-phosphate is transformed into the intermediate pyruvate, rendering 2 mol of ATP.…”

Section: Some Interesting Features Of the Bifidus Pathwaymentioning

confidence: 99%

“…Two types of enzymes have been described in Bifidobacterium to date: a specific enzyme acting on fructose-6-phosphate, which catalyses the conversion of this substrate to erythrose-4-phosphate and acetyl-phosphate, and a dual enzyme Figure 1. Short schematic representation of the main steps of the fructose-6-phosphate shunt in Bifidobacterium [4,25]. which can also act on xylulose-5-phosphate, rendering acetyl-phosphate and glyceraldehyde-3-phosphate [13,25].…”

Section: Some Interesting Features Of the Bifidus Pathwaymentioning

confidence: 99%

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Effect of acquired resistance to bile salts on enzymatic activities involved in the utilisation of carbohydrates by bifidobacteria. An overview

Reyes‐Gavilán

Ruas‐Madiedo

Noriega

et al. 2005

Lait

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-Bifidobacteria are probiotics widely used in dairy-based products. In order to exert the health-promoting benefits attributed to these microorganisms, they must survive the restrictive conditions of the gastrointestinal tract, being resistant, among other factors, to the toxic action of bile salts. The inhibition exerted by these compounds on bifidobacteria can be overcome by progressive adaptation to gradually increasing concentrations of bile. The acquisition of stable resistance, or even transient exposure to bile salts in Bifidobacterium, promoted in these microorganisms irreversible physiological changes that are reviewed in this article. The presence of, or short-term exposure to bile salts caused a diminution in adhesion to mucus and intestinal epithelial cells, as well as a decrease in cellular surface hydrophobicity. However, adaptation to high bile salt concentrations promoted an enhancement of adhesion to intestinal mucus, which correlates in some cases with increases in cellular surface hydrophobicity. In addition, differences in membrane protein profiles, better tolerance to low pH, and variations in glycosidic activities and fructose-6-phosphate-phosphoketolase (F6PPK) activity were detected in some bile-adapted strains with respect to their originals. In particular, some bile-resistant derivatives showed higher levels of F6PPK activity than the corresponding more sensitive strains of origin, and increases in α-glucosidase and β-glucosidase activities. These glycosidases are responsible for the hydrolysis of maltose and cellobiose, respectively. Both disaccharides can result from the partial hydrolysis of glucose polysaccharides. The more detailed study of one original/resistant derivative pair indicated that the acquisition of bile salt resistance maintained the viability of old cultures and promoted shifts in the carbohydrate fermentation patterns, which modified growth in media containing maltose or glucose as a carbon source, as well as the profile of organic acids formed. Bile tolerance adaptative mechanisms may lead to better adaptation to the colon environment and available carbon sources as well as to an increase in the viability and permanence of Bifidobacterium in the intestinal environment.Bifidobacterium / carbohydrate / bile salt resistance / organic acid / glycosidase Résumé -Effet de la résistance acquise vis-à-vis des sels biliaires sur des activités enzymatiques impliquées dans l'utilisation des sucres par les bifidobactéries. Les bifidobactéries sont des probiotiques largement utilisés dans les produits laitiers. Afin d'exercer les effets bénéfiques qui leur sont attribués, elles doivent survivre aux conditions restrictives du tractus gastro-intestinal en résistant, entre autres facteurs, à l'action toxique des sels biliaires.

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Characterization of thed-Xylulose 5-Phosphate/d-Fructose 6-Phosphate Phosphoketolase Gene (xfp) fromBifidobacterium lactis

Cited by 110 publications

References 30 publications

Evolutionary Analysis of the TPP-Dependent Enzyme Family

Evolutionary Analysis of the TPP-Dependent Enzyme Family

The Acetate Switch

Effect of acquired resistance to bile salts on enzymatic activities involved in the utilisation of carbohydrates by bifidobacteria. An overview

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