Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii

Kim, Young‐Ok; Kim, Han-Woo; Park, In-Suk; Lee, Jehee; Lee, Sang-Jun; Kim, Kyung-Kil

doi:10.2323/jgam.55.345

Cited by 5 publications

(2 citation statements)

References 20 publications

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“…With the current bioinformatics methodology, it is not possible to infer the catalytic ability of transphosphorylation from a phosphatase protein structure alone, necessitating the dedicated biochemical characterization. However, there is evidence from the literature (37,(72)(73)(74) that phosphatases related to Agp by common membership in the high-molecular-weight histidine acid phosphatase family also possess transphosphorylation activity, albeit on donor and acceptor substrates different from the ones identified here for Agp. Acceptor substrate selectivity and phosphorylation site selectivity of transphosphorylation will be fine-tuned by positioning of the sugar acceptor substrate in the binding pocket on the phosphoenzyme intermediate.…”

Section: Discussionmentioning

confidence: 75%

Phosphoryl Transfer from α-d-Glucose 1-Phosphate Catalyzed by Escherichia coli Sugar-Phosphate Phosphatases of Two Protein Superfamily Types

Wildberger

Pfeiffer

Brecker

et al. 2015

Appl Environ Microbiol

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The Cori ester ␣-D-glucose 1-phosphate (␣Glc 1-P) is a high-energy intermediate of cellular carbohydrate metabolism. Its glycosidic phosphomonoester moiety primes ␣Glc 1-P for flexible exploitation in glucosyl and phosphoryl transfer reactions. Two structurally and mechanistically distinct sugar-phosphate phosphatases from Escherichia coli were characterized in this study for utilization of ␣Glc 1-P as a phosphoryl donor substrate. The agp gene encodes a periplasmic ␣Glc 1-P phosphatase (Agp) belonging to the histidine acid phosphatase family. Had13 is from the haloacid dehydrogenase-like phosphatase family. Cytoplasmic expression of Agp (in E. coli Origami B) gave a functional enzyme preparation (k cat for phosphoryl transfer from ␣Glc 1-P to water, 40 s ؊1 ) that was shown by mass spectrometry to exhibit no free cysteines and the native intramolecular disulfide bond between Cys 189 and Cys 195 . Enzymatic phosphoryl transfer from ␣Glc 1-P to water in H 2 18 O solvent proceeded with complete 18 O label incorporation into the phosphate released, consistent with catalytic reaction through O-1-P, but not C-1-O, bond cleavage. Hydrolase activity of both enzymes was not restricted to a glycosidic phosphomonoester substrate, and D-glucose 6-phosphate was converted with a k cat similar to that of ␣Glc 1-P. By examining phosphoryl transfer from ␣Glc 1-P to an acceptor substrate other than water (D-fructose or D-glucose), we discovered that Agp exhibited pronounced synthetic activity, unlike Had13, which utilized ␣Glc 1-P mainly for phosphoryl transfer to water. By applying D-fructose in 10-fold molar excess over ␣Glc 1-P (20 mM), enzymatic conversion furnished D-fructose 1-phosphate as the main product in a 55% overall yield. Agp is a promising biocatalyst for use in transphosphorylation from ␣Glc 1-P. Phosphorylation of sugar substrates is a common biochemical transformation of central importance to cellular metabolism (1-3). It usually involves phosphoryl transfer from a phosphoactivated donor substrate, such as ATP, to an acceptor group, typically a hydroxyl, on the sugar backbone (4-7). Various phosphotransferases (EC 2.7) catalyze sugar phosphorylation (8-12). In an alternative reaction catalyzed by glycoside phosphorylases (EC 2.4), where phosphorylation occurs exclusively at the sugar's anomeric position, a glycosyl residue is transferred from a sugar donor substrate to phosphate (Fig. 1A) (13, 14). The phosphomonoester moiety attached to sugars is a key element of biological recognition, across all steps of glycolysis, for example, and it serves to prime sugars for further conversion in different biochemical pathways (15-18). It is known from intracellular-metabolite-profiling studies that changes in concentrations of common sugar phosphates (e.g., D-glucose 6-phosphate [Glc 6-P] and D-fructose 6-phosphate [Fru 6-P]) are often linked to major alterations in cellular physiology (19)(20)(21)(22). Due to the requirement for authentic reference material in different biological investigations, there is considerable ...

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Section: Discussionmentioning

confidence: 75%

Phosphoryl Transfer from α-d-Glucose 1-Phosphate Catalyzed by Escherichia coli Sugar-Phosphate Phosphatases of Two Protein Superfamily Types

Wildberger

Pfeiffer

Brecker

et al. 2015

Appl Environ Microbiol

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“…Thirdly, some bacteria, particularly Citrobacter sp., Acinetobacter sp., Pseudomonas sp., discovered in wastewater have the ability of producing EEs, such as lipase, protease, amylase, urease and so on . Catalyzed by the EEs, some solid organics can be degraded to digestible organics that can be absorbed and utilized algal cells.…”

Section: Resultsmentioning

confidence: 99%

Contribution of glycerol addition and algal–bacterial cooperation to nutrients recovery: a study on the mechanisms of microalgae‐based wastewater remediation

Zeng

et al. 2020

J of Chemical Tech & Biotech

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BACKGROUND: Microalgae biotechnology is considered as a promising way to recover nutrients from centrate wastewater for value-added biomass production, but it is rarely adopted in a real-world application. Current study confirmed that carbon deficiency and suspended solids are two problems jeopardizing the microalgae-based wastewater remediation. In this regard, glycerol was added into centrate wastewater as exogenous carbon source and algal-bacterial cooperation for nutrients recovery assessment. RESULTS:The results showed that glycerol addition increased the biomass yield of algae from 1.54 to 2.58 g L −1 in 5-day culture and, at the same time, improved the removal efficiency of nitrogen and phosphorus, which were further assessed by pilot-scale experiments. Bacterial community analysis indicated that algal-bacterial cooperation involves carbon dioxide and oxygen exchange, phosphorus absorption, and solid organics degradation, forming a complementary nexus beneficial for wastewater treatment.CONCLUSION: Glycerol is proven to be a good carbon source for microalgae growth in the centrate wastewater. Additionally, the cooperation between microalgae and bacteria plays a key role in the nutrients removal during centrate wastewater. It is expected the technology and knowledge provided by current work can further promote the industrialization of microalgaebased wastewater remediation. Figure 6. Scheme for microalgae-based centrate wastewater treatment and mechanism of nutrients recovery. www.soci.org M Xu et al.wileyonlinelibrary.com/jctb

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Multi-enzyme systems and recombinant cells for synthesis of valuable saccharides: Advances and perspectives

Yang

Zhang

Tian

et al. 2019

Biotechnology Advances

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Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii

Cited by 5 publications

References 20 publications

Phosphoryl Transfer from α-d-Glucose 1-Phosphate Catalyzed by Escherichia coli Sugar-Phosphate Phosphatases of Two Protein Superfamily Types

Phosphoryl Transfer from α-d-Glucose 1-Phosphate Catalyzed by Escherichia coli Sugar-Phosphate Phosphatases of Two Protein Superfamily Types

Contribution of glycerol addition and algal–bacterial cooperation to nutrients recovery: a study on the mechanisms of microalgae‐based wastewater remediation

Multi-enzyme systems and recombinant cells for synthesis of valuable saccharides: Advances and perspectives

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