Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655

Passariello, Claudio; Forleo, C.; Micheli, Vanna; Schippa, Serena; Leone, R.; Mangani, Stefano; Thaller, María Cristina; Rossolini, Gian María

doi:10.1016/j.bbapap.2005.08.028

Cited by 22 publications

(40 citation statements)

References 16 publications

(23 reference statements)

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“…Although this result implicates D-glucose-6P as the direct precursor to extracellular D-glucose, we do not establish how D-glucose-6P itself is hydrolyzed. Unfortunately, E. coli has numerous candidate enzymes that could hydrolyze D-glucose-6P: a periplasmic acid phosphatase (25), an alkaline phosphatase (26), and eight different haloacid dehalogenase-like hydrolases (27) have all been observed to hydrolyze D-glucose-6P under various environmental conditions. Each of these enzymes might mediate the final step to D-glucose during growth on D-xylose or L-arabinose.…”

Section: Discussionmentioning

confidence: 99%

Accumulation of d -Glucose from Pentoses by Metabolically Engineered Escherichia coli

Xia

Han

Costanzo

et al. 2015

Appl Environ Microbiol

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T he pentose phosphate (PP) pathway interconverts phosphosugars having 3 to 7 carbon atoms principally by the action of the reversible enzymes transketolase and transaldolase. During the consumption of hexoses such as D-glucose or D-fructose, entry of carbon into this pathway provides many microorganisms, including Escherichia coli, the means to generate the reduced cofactor NADPH and to synthesize specific building-block compounds derived from intermediates of this pathway (e.g., phenylalanine, histidine, and ribose). For microorganisms having the requisite kinases and sugar transport mechanisms, the PP pathway also provides convenient entry points for the catabolism of many other sugars, including D-xylose and L-arabinose (49).We have previously studied D-xylose and L-arabinose metabolism in E. coli that lacks the ability to metabolize D-glucose due to knockouts in the ptsG, manZ, and glk genes (1-3). Recently, small but consistent amounts (about 50 mg/liter) of D-glucose were observed as the accumulated end product when E. coli ptsG manZ glk was grown on 5 g/liter of either pentose in a defined medium (unpublished data). How might D-glucose be derived from these pentoses?Both D-xylose and L-arabinose are converted to the common intermediate D-xylulose-5-phosphate (D-xylulose-5P) (Fig. 1), which via the PP pathway partitions to 67% D-fructose-6P and 33% D-glyceraldehyde-3P without the involvement of ATP:(1) During growth of cells having a complete glycolytic pathway, the 2 mol of D-fructose-6P formed via equation 1 readily generates 4 mol of D-glyceraldehyde-3P. For D-glucose to accumulate from pentoses in cells prevented from metabolizing D-glucose, we reasoned that some D-fructose-6P generated from these pentoses (i.e., by equation 1) is converted "back" to D-glucose and that once formed, the D-glucose is unable to reenter metabolism in the triple knockout strain. We furthermore hypothesized that even more D-glucose would accumulate from pentoses in cells that were further constrained from metabolizing D-fructose-6P or D-glucose-6P.Because D-fructose-6P conversion to D-glyceraldehyde-3P is ubiquitous in wild-type organisms, D-glucose is not typically considered a product of D-xylose or L-arabinose metabolism, and the conversion of these pentoses to readily available D-glucose would in itself not seem to be an economically viable process. However, if the yields and rates were sufficiently large, the accumulation of hexoses directly from pentoses might advance the use of lignocellulosic hydrolysates with organisms, such as Saccharomyces cerevisiae, which metabolize D-glucose readily but are natively unable to consume pentoses. Moreover, conversion of 5-carbon saccharides into 6-carbon saccharides derived from D-fructose-6P offers a unique platform both to build carbon length and potentially to generate compounds in industrially relevant organisms such as E. coli that might not be possible under typical conditions in which products of D-fructose-6P do not accumulate.The objectives of this study were to examine ...

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Section: Discussionmentioning

confidence: 99%

Accumulation of d -Glucose from Pentoses by Metabolically Engineered Escherichia coli

Xia

Han

Costanzo

et al. 2015

Appl Environ Microbiol

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“…PhoA and AphA are an alkaline phosphatase and an acid phosphatase, respectively, and catalyze the hydrolysis of a wide variety of phosphoesters (Holtz and Kantrowitz, 1999;Passariello et al, 2006). BacA and PgpB exhibit undecaprenyl pyrophosphate (UPP) phosphatase activity and are known as a UPP phosphatase (El Ghachi et al, 2004;Touze et al, 2008).…”

Section: Investigation Of Putative Phosphatases Catalyzing Foh Formationmentioning

confidence: 99%

Farnesol production from Escherichia coli by harnessing the exogenous mevalonate pathway

Wang

Yoon

Shah

et al. 2010

Biotech & Bioengineering

102

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Farnesol (FOH) production has been carried out in metabolically engineered Escherichia coli. FOH is formed through the depyrophosphorylation of farnesyl pyrophosphate (FPP), which is synthesized from isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) by FPP synthase. In order to increase FPP synthesis, E. coli was metabolically engineered to overexpress ispA and to utilize the foreign mevalonate (MVA) pathway for the efficient synthesis of IPP and DMAPP. Two-phase culture using a decane overlay of the culture broth was applied to reduce volatile loss of FOH produced during culture and to extract FOH from the culture broth. A FOH production of 135.5 mg/L was obtained from the recombinant E. coli harboring the pTispA and pSNA plasmids for ispA overexpression and MVA pathway utilization, respectively. It is interesting to observe that a large amount of FOH could be produced from E. coli without FOH synthase by the augmentation of FPP synthesis. Introduction of the exogenous MVA pathway enabled the dramatic production of FOH by E. coli while no detectable FOH production was observed in the endogenous MEP pathway-only control.

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“…This study describes the identification and purification of a cellular activity from both E. coli and S. enterica that synthe- (20). At physiological pH the protein exhibits suboptimal activity, potentially decreasing this catalytic efficiency further, raising the possibility that R5P could bind in the active site without dephosphorylation occurring.…”

Section: Discussionmentioning

confidence: 99%

Glutamine Phosphoribosylpyrophosphate Amidotransferase-independent Phosphoribosyl Amine Synthesis from Ribose 5-Phosphate and Glutamine or Asparagine

Koenigsknecht¹,

Ramos²,

Downs

2007

Journal of Biological Chemistry

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Phosphoribosylamine (PRA) is the first intermediate in the common pathway to purines and thiamine and is generated in bacteria by glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase (EC 2.4.2.14) from PRPP and glutamine. Genetic data have indicated that multiple, non-PRPP amidotransferase mechanisms exist to generate PRA sufficient for thiamine but not purine synthesis. Here we describe the purification and identification of an activity (present in both Escherichia coli and Salmonella enterica) that synthesizes PRA from ribose 5-phosphate and glutamine/asparagine. A purification resulting in greater than a 625-fold increase in specific activity identified 8 candidate proteins. Of the candidates, overexpression of AphA (EC 3.1.3.2), a periplasmic class B nonspecific acid phosphatase, significantly increased activity in partially purified extracts. Native purification of AphA to >95% homogeneity determined that the periplasmic L-asparaginase II, AnsB (EC 3.5.1.1), co-purified with AphA and was also necessary for PRA formation. The potential physiological relevance of AphA and AnsB in contributing to thiamine biosynthesis in vivo is discussed.

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Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655

Cited by 22 publications

References 16 publications

Accumulation of d -Glucose from Pentoses by Metabolically Engineered Escherichia coli

Accumulation of d -Glucose from Pentoses by Metabolically Engineered Escherichia coli

Farnesol production from Escherichia coli by harnessing the exogenous mevalonate pathway

Glutamine Phosphoribosylpyrophosphate Amidotransferase-independent Phosphoribosyl Amine Synthesis from Ribose 5-Phosphate and Glutamine or Asparagine

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