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  1. Article ; Online: Insoluble Protein Applications: The Use of Bacterial Inclusion Bodies as Biocatalysts.

    Köszagová, Romana / Hrabárová, Eva / Achbergerová, Lucia / Nahálka, Jozef

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2406, Page(s) 501–515

    Abstract: Biocatalysis and biotransformations have a broad application in industrial synthetic chemistry. In addition to the whole cell catalysis, purified recombinant enzymes are successfully used for biocatalysis of specific chemical reactions. In this ... ...

    Abstract Biocatalysis and biotransformations have a broad application in industrial synthetic chemistry. In addition to the whole cell catalysis, purified recombinant enzymes are successfully used for biocatalysis of specific chemical reactions. In this contribution, we report characterization, immobilization, and application of several model target enzymes (D-amino acid oxidase, sialic acid aldolase, maltodextrin phosphorylase, polyphosphate kinase, UDP-glucose pyrophosphorylase) physiologically aggregated within inclusion bodies retaining their biological activity as immobilized biocatalysts.
    MeSH term(s) Bacteria/chemistry ; Bacteria/metabolism ; Biocatalysis ; Biotransformation ; Enzymes, Immobilized/chemistry ; Inclusion Bodies
    Chemical Substances Enzymes, Immobilized
    Language English
    Publishing date 2022-01-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1859-2_30
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  2. Article ; Online: Degradation of polyphosphates by polyphosphate kinases from Ruegeria pomeroyi.

    Achbergerová, Lucia / Nahálka, Jozef

    Biotechnology letters

    2014  Volume 36, Issue 10, Page(s) 2029–2035

    Abstract: Polyphosphate kinases 2 (PPK2) are key enzymes for polyphosphate utilisation in bacteria. The genome of Ruegeria pomeroyi, a marine α-proteobacterium, includes three Pseudomonas aeruginosa PPK2 homologs. We expressed these homologs in Escherichia coli as ...

    Abstract Polyphosphate kinases 2 (PPK2) are key enzymes for polyphosphate utilisation in bacteria. The genome of Ruegeria pomeroyi, a marine α-proteobacterium, includes three Pseudomonas aeruginosa PPK2 homologs. We expressed these homologs in Escherichia coli as soluble proteins, purified the protein products and compared their metal, pH and nucleotide preferences. The optimal pH was 8.0 for SPO1727 and 9.0 for SPO1256. The SPO0224 gene product had two pH optima at eight and ten. The SPO0224 protein showed little dependence on metal presence, while SPO1256 required Mg(2+). SPO1727 required Mg(2+) but accepted other ions as well.
    MeSH term(s) Alphaproteobacteria/enzymology ; Alphaproteobacteria/metabolism ; Bacterial Proteins/biosynthesis ; Bacterial Proteins/isolation & purification ; Bacterial Proteins/metabolism ; Escherichia coli/metabolism ; Hydrogen-Ion Concentration ; Magnesium/chemistry ; Phosphates/metabolism ; Phosphotransferases (Phosphate Group Acceptor)/biosynthesis ; Phosphotransferases (Phosphate Group Acceptor)/isolation & purification ; Phosphotransferases (Phosphate Group Acceptor)/metabolism
    Chemical Substances Bacterial Proteins ; Phosphates ; Phosphotransferases (Phosphate Group Acceptor) (EC 2.7.4.-) ; polyphosphate kinase (EC 2.7.4.1) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2014-10
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 423853-9
    ISSN 1573-6776 ; 0141-5492
    ISSN (online) 1573-6776
    ISSN 0141-5492
    DOI 10.1007/s10529-014-1566-6
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4564: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  3. Article: Degradation of polyphosphates by polyphosphate kinases from Ruegeria pomeroyi

    Achbergerová, Lucia / Nahálka, Jozef

    Biotechnology letters. 2014 Oct., v. 36, no. 10

    2014  

    Abstract: Polyphosphate kinases 2 (PPK2) are key enzymes for polyphosphate utilisation in bacteria. The genome of Ruegeria pomeroyi, a marine α-proteobacterium, includes three Pseudomonas aeruginosa PPK2 homologs. We expressed these homologs in Escherichia coli as ...

    Abstract Polyphosphate kinases 2 (PPK2) are key enzymes for polyphosphate utilisation in bacteria. The genome of Ruegeria pomeroyi, a marine α-proteobacterium, includes three Pseudomonas aeruginosa PPK2 homologs. We expressed these homologs in Escherichia coli as soluble proteins, purified the protein products and compared their metal, pH and nucleotide preferences. The optimal pH was 8.0 for SPO1727 and 9.0 for SPO1256. The SPO0224 gene product had two pH optima at eight and ten. The SPO0224 protein showed little dependence on metal presence, while SPO1256 required Mg²⁺. SPO1727 required Mg²⁺ but accepted other ions as well.
    Keywords Escherichia coli ; Pseudomonas aeruginosa ; Ruegeria ; bacteria ; genes ; ions ; kinases ; magnesium ; pH ; polyphosphates ; protein products
    Language English
    Dates of publication 2014-10
    Size p. 2029-2035.
    Publishing place Springer-Verlag
    Document type Article
    ZDB-ID 423853-9
    ISSN 1573-6776 ; 0141-5492
    ISSN (online) 1573-6776
    ISSN 0141-5492
    DOI 10.1007/s10529-014-1566-6
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4564: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article: PPK1 and PPK2 — which polyphosphate kinase is older?

    Achbergerová, Lucia / Nahálka, Jozef

    Biológia. 2014 Mar., v. 69, no. 3

    2014  

    Abstract: Polyphosphate kinases (PPKs) catalyse the polymerisation and degradation of polyphosphate chains. As a result of this process, PPK produces or consumes energy in the form of ATP. Polyphosphate is a linear molecule that contains tens to hundreds of ... ...

    Abstract Polyphosphate kinases (PPKs) catalyse the polymerisation and degradation of polyphosphate chains. As a result of this process, PPK produces or consumes energy in the form of ATP. Polyphosphate is a linear molecule that contains tens to hundreds of phosphate residues connected by macroergic bonds, and it appears to be an easily obtainable and rich source of energy from prebiotic times to the present. Notably, polyphosphate is present in the cells of all three domains of life, but PPKs are widely distributed only in Bacteria, as Archaea and Eucarya use various unrelated or “nonhomologous” proteins for energy and metabolic balance. The present study focuses on PPK1 and PPK2 homologues, which have been described to some extent in Bacteria, and the aim was to determine which homologue group, PPK1 or PPK2, is older. Phylogenetic analyses of 109 sequence homologues of Escherichia coli PPK1 and 109 sequence homologues of Pseudomonas aeruginosa PPK2 from 109 bacterial genomes imply that polyphosphate consumption (PPK2) evolved first and that phosphate polymerisation (PPK1) evolved later. Independently, a theory of the trends in amino acid loss and gain also confirms that PPK2 is older than PPK1. According to the results of this study, we propose 68 hypothetical proteins to mark as PPK2 homologues and 3 hypothetical proteins to mark as PPK1 homologues.
    Keywords Archaea ; Escherichia coli ; Pseudomonas aeruginosa ; amino acids ; bacteria ; energy ; genome ; kinases ; phylogeny ; polymerization ; prebiotics ; proteins
    Language English
    Dates of publication 2014-03
    Size p. 263-269.
    Publishing place Springer-Verlag
    Document type Article
    ZDB-ID 419136-5
    ISSN 1336-9563 ; 0006-3088 ; 1335-6372 ; 1335-6380
    ISSN (online) 1336-9563
    ISSN 0006-3088 ; 1335-6372 ; 1335-6380
    DOI 10.2478/s11756-013-0324-x
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    In stock of ZB MED Cologne/Königswinter

    Zs.B 791: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Insoluble protein applications: the use of bacterial inclusion bodies as biocatalysts.

    Hrabárová, Eva / Achbergerová, Lucia / Nahálka, Jozef

    Methods in molecular biology (Clifton, N.J.)

    2015  Volume 1258, Page(s) 411–422

    Abstract: Biocatalysis and biotransformations have a broad application in industrial synthetic chemistry. In addition to the whole cell catalysis, purified recombinant enzymes are successfully used for biocatalysis of specific chemical reactions. In this ... ...

    Abstract Biocatalysis and biotransformations have a broad application in industrial synthetic chemistry. In addition to the whole cell catalysis, purified recombinant enzymes are successfully used for biocatalysis of specific chemical reactions. In this contribution, we report characterization, immobilization, and application of several model target enzymes (D-amino acid oxidase, sialic acid aldolase, maltodextrin phosphorylase, polyphosphate kinase) physiologically aggregated within inclusion bodies (IBs) retaining their biological activity as immobilized biocatalysts.
    MeSH term(s) Bacteria/metabolism ; Biocatalysis ; Catalysis ; Inclusion Bodies/metabolism
    Language English
    Publishing date 2015
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-2205-5_24
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  6. Article ; Online: Polyphosphate--an ancient energy source and active metabolic regulator.

    Achbergerová, Lucia / Nahálka, Jozef

    Microbial cell factories

    2011  Volume 10, Page(s) 63

    Abstract: There are a several molecules on Earth that effectively store energy within their covalent bonds, and one of these energy-rich molecules is polyphosphate. In microbial cells, polyphosphate granules are synthesised for both energy and phosphate storage ... ...

    Abstract There are a several molecules on Earth that effectively store energy within their covalent bonds, and one of these energy-rich molecules is polyphosphate. In microbial cells, polyphosphate granules are synthesised for both energy and phosphate storage and are degraded to produce nucleotide triphosphate or phosphate. Energy released from these energetic carriers is used by the cell for production of all vital molecules such as amino acids, nucleobases, sugars and lipids. Polyphosphate chains directly regulate some processes in the cell and are used as phosphate donors in gene regulation. These two processes, energetic metabolism and regulation, are orchestrated by polyphosphate kinases. Polyphosphate kinases (PPKs) can currently be categorized into three groups (PPK1, PPK2 and PPK3) according their functionality; they can also be divided into three groups according their homology (EcPPK1, PaPPK2 and ScVTC). This review discusses historical information, similarities and differences, biochemical characteristics, roles in stress response regulation and possible applications in the biotechnology industry of these enzymes. At the end of the review, a hypothesis is discussed in view of synthetic biology applications that states polyphosphate and calcium-rich organelles have endosymbiotic origins from ancient protocells that metabolized polyphosphate.
    MeSH term(s) Bacteria/metabolism ; Bacterial Proteins/metabolism ; Bacterial Proteins/physiology ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Phosphotransferases (Phosphate Group Acceptor)/physiology ; Polyphosphates/chemistry ; Polyphosphates/metabolism ; Protein Structure, Tertiary
    Chemical Substances Bacterial Proteins ; Polyphosphates ; Phosphotransferases (Phosphate Group Acceptor) (EC 2.7.4.-) ; polyphosphate kinase (EC 2.7.4.1)
    Language English
    Publishing date 2011-08-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 1475-2859
    ISSN (online) 1475-2859
    DOI 10.1186/1475-2859-10-63
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  7. Article ; Online: Polyphosphate - an ancient energy source and active metabolic regulator

    Achbergerová Lucia / Nahálka Jozef

    Microbial Cell Factories, Vol 10, Iss 1, p

    2011  Volume 63

    Abstract: Abstract There are a several molecules on Earth that effectively store energy within their covalent bonds, and one of these energy-rich molecules is polyphosphate. In microbial cells, polyphosphate granules are synthesised for both energy and phosphate ... ...

    Abstract Abstract There are a several molecules on Earth that effectively store energy within their covalent bonds, and one of these energy-rich molecules is polyphosphate. In microbial cells, polyphosphate granules are synthesised for both energy and phosphate storage and are degraded to produce nucleotide triphosphate or phosphate. Energy released from these energetic carriers is used by the cell for production of all vital molecules such as amino acids, nucleobases, sugars and lipids. Polyphosphate chains directly regulate some processes in the cell and are used as phosphate donors in gene regulation. These two processes, energetic metabolism and regulation, are orchestrated by polyphosphate kinases. Polyphosphate kinases (PPKs) can currently be categorized into three groups (PPK1, PPK2 and PPK3) according their functionality; they can also be divided into three groups according their homology ( Ec PPK1, Pa PPK2 and Sc VTC). This review discusses historical information, similarities and differences, biochemical characteristics, roles in stress response regulation and possible applications in the biotechnology industry of these enzymes. At the end of the review, a hypothesis is discussed in view of synthetic biology applications that states polyphosphate and calcium-rich organelles have endosymbiotic origins from ancient protocells that metabolized polyphosphate.
    Keywords Microbiology ; QR1-502 ; Science ; Q ; DOAJ:Microbiology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
    Subject code 571
    Language English
    Publishing date 2011-08-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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