Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from <i>Bacillus subtilis</i>

Godinho, Lia M.; Sá‐Nogueira, Isabel

doi:10.1111/j.1742-4658.2011.08177.x

Cited by 13 publications

(15 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although NagD is expressed from the N-acetylglucosamine (GlcNAc) metabolic operon, it has no effect on metabolism (27). Because nonspecific HAD enzymes have broad and low substrate specificities and do not participate in specific metabolic pathways, it was previously proposed that nonspecific HAD enzymes detoxify sugar phosphates that accidentally accumulate at metabolic bottlenecks (9).…”

Section: Discussionmentioning

confidence: 99%

“…Although two bacterial enzymes, AraL from Bacillus subtilis (a Gram-positive bacterium) and NagD from Escherichia coli (a Gram-negative bacterium), are classified into this subfamily as well, their biochemical properties differ from those of eukaryotic enzymes (9,10). Moreover, the physiological importance of this group of enzymes is not yet understood.…”

mentioning

confidence: 99%

“…Saccharomyces cerevisiae Pho13 is structurally classified as a member of HAD subfamily IIA (9), which contains ϳ3,000 sequences, including eukaryotic 2-phosphoglycolate phosphatase (PGP or PGLP) and pyridoxal phosphatase. Although two bacterial enzymes, AraL from Bacillus subtilis (a Gram-positive bacterium) and NagD from Escherichia coli (a Gram-negative bacterium), are classified into this subfamily as well, their biochemical properties differ from those of eukaryotic enzymes (9,10).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Deletion of PHO13 , Encoding Haloacid Dehalogenase Type IIA Phosphatase, Results in Upregulation of the Pentose Phosphate Pathway in Saccharomyces cerevisiae

Kim

Lesmana

et al. 2015

Appl Environ Microbiol

View full text Add to dashboard Cite

eThe haloacid dehalogenase (HAD) superfamily is one of the largest enzyme families, consisting mainly of phosphatases. Although intracellular phosphate plays important roles in many cellular activities, the biological functions of HAD enzymes are largely unknown. Pho13 is 1 of 16 putative HAD enzymes in Saccharomyces cerevisiae. Pho13 has not been studied extensively, but previous studies have identified PHO13 to be a deletion target for the generation of industrially attractive phenotypes, namely, efficient xylose fermentation and high tolerance to fermentation inhibitors. In order to understand the molecular mechanisms underlying the improved xylose-fermenting phenotype produced by deletion of PHO13 (pho13⌬), we investigated the response of S. cerevisiae to pho13⌬ at the transcriptomic level when cells were grown on glucose or xylose. Transcriptome sequencing analysis revealed that pho13⌬ resulted in upregulation of the pentose phosphate (PP) pathway and NADPH-producing enzymes when cells were grown on glucose or xylose. We also found that the transcriptional changes induced by pho13⌬ required the transcription factor Stb5, which is activated specifically under NADPH-limiting conditions. Thus, pho13⌬ resulted in the upregulation of the PP pathway and NADPH-producing enzymes as a part of an oxidative stress response mediated by activation of Stb5. Because the PP pathway is the primary pathway for xylose, its upregulation by pho13⌬ might explain the improved xylose metabolism. These findings will be useful for understanding the biological function of S. cerevisiae Pho13 and the HAD superfamily enzymes and for developing S. cerevisiae strains with industrially attractive phenotypes.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Deletion of PHO13 , Encoding Haloacid Dehalogenase Type IIA Phosphatase, Results in Upregulation of the Pentose Phosphate Pathway in Saccharomyces cerevisiae

Kim

Lesmana

et al. 2015

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…Recently, Papenfort et al provided strong evidence that the phosphatase YigL in Salmonella enterica serovar Typhimurium is needed for dephosphorylation of accumulated hexose phosphate prior to efflux by an unidentified efflux pump (11). Sugar phosphate stress is still not well understood, but current evidence indicates that accumulation of sugar phosphates leads to depletion of other carbon metabolites or phosphorus (13)(14)(15)(16). Sugar phosphatases might then be used to alleviate this problem.…”

Section: Figmentioning

confidence: 99%

Identification of a New Phosphatase Enzyme Potentially Involved in the Sugar Phosphate Stress Response in Pseudomonas fluorescens

Maleki

Hrudíková

Zotchev

et al. 2017

Appl Environ Microbiol

View full text Add to dashboard Cite

The alginate-producing bacterium Pseudomonas fluorescens utilizes the Entner-Doudoroff (ED) and pentose phosphate (PP) pathways to metabolize fructose, since the upper part of its Embden-Meyerhof-Parnas pathway is defective. Our previous study indicated that perturbation of the central carbon metabolism by diminishing glucose-6-phosphate dehydrogenase activity could lead to sugar phosphate stress when P. fluorescens was cultivated on fructose. In the present study, we demonstrate that PFLU2693, annotated as a haloacid dehalogenase-like enzyme, is a new sugar phosphate phosphatase, now designated Spp, which is able to dephosphorylate a range of phosphate substrates, including glucose 6-phosphate and fructose 6-phosphate, in vitro. The effect of spp overexpression on growth and alginate production was investigated using both the wild type and several mutant strains. The results obtained suggested that sugar phosphate accumulation caused diminished growth in some of the mutant strains, since this was partially relieved by spp overexpression. On the other hand, overexpression of spp in fructose-grown alginate-producing strains negatively affected both growth and alginate production. The latter implies that Spp dephosphorylates the sugar phosphates, thus depleting the pool of these important metabolites. Deletion of the spp gene did not affect growth of the wildtype strain on fructose, but the gene could not be deleted in the alginate-producing strain. This indicates that Spp is essential for relieving the cells of sugar phosphate stress in P. fluorescens actively producing alginate.IMPORTANCE In enteric bacteria, the sugar phosphate phosphatase YigL is known to play an important role in combating stress caused by sugar phosphate accumulation. In this study, we identified a sugar phosphate phosphatase, designated Spp, in Pseudomonas fluorescens. Spp utilizes glucose 6-phosphate, fructose 6-phosphate, and ribose 5-phosphate as substrates, and overexpression of the gene had a positive effect on growth in P. fluorescens mutants experiencing sugar phosphate stress. The gene was localized downstream of gnd and zwf-2, which encode enzymes involved in the pentose phosphate and Entner-Doudoroff pathways. Genes encoding Spp homologues were identified in similar genetic contexts in some bacteria belonging to several phylogenetically diverse families, suggesting similar functions.

show abstract

“…AbfA and AbfB remove a-1,2-and a-1,3-linked arabinofuranoside substitutions [13][14][15][16][17]. The role of the araJKLMN genes in the arabinan system is not fully understood and they are likely to constitute a novel utilization pathway for pentoses in G. stearothermophilus [5,18].…”

Section: Introductionmentioning

confidence: 99%

The abp gene in Geobacillus stearothermophilus T‐6 encodes a GH27 β‐l‐arabinopyranosidase

et al. 2012

View full text Add to dashboard Cite

Edited by Miguel De la RosaKeywords: b-L-Arabinopyranosidase Glycoside hydrolase family 27 Arabinopyranose Sugar beet arabinan Larch arabinogalactan 13 C NMR a b s t r a c tIn this study we demonstrate that the abp gene in Geobacillus stearothermophilus T-6 encodes a family 27 glycoside hydrolase b-L-arabinopyranosidase. The catalytic constants towards the chromogenic substrate pNP-b-L-arabinopyranoside were 0.8 ± 0.1 mM, 6.6 ± 0.3 s À1 , and 8.2 ± 0.3 s À1 mM À1for K m , k cat and k cat /K m , respectively. 13C NMR spectroscopy unequivocally showed that Abp is capable of removing b-L-arabinopyranose residues from the natural arabino-polysaccharide, larch arabinogalactan. Most family 27 enzymes are active on galactose and contain a conserved Asp residue, whereas in Abp this residue is Ile67, which shifts the specificity of the enzyme towards arabinopyranoside.

show abstract

Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis

Cited by 13 publications

References 40 publications

Deletion of PHO13 , Encoding Haloacid Dehalogenase Type IIA Phosphatase, Results in Upregulation of the Pentose Phosphate Pathway in Saccharomyces cerevisiae

Deletion of PHO13 , Encoding Haloacid Dehalogenase Type IIA Phosphatase, Results in Upregulation of the Pentose Phosphate Pathway in Saccharomyces cerevisiae

Identification of a New Phosphatase Enzyme Potentially Involved in the Sugar Phosphate Stress Response in Pseudomonas fluorescens

The abp gene in Geobacillus stearothermophilus T‐6 encodes a GH27 β‐l‐arabinopyranosidase

Contact Info

Product

Resources

About