Several Polyphosphate Kinase 2 Enzymes Catalyse the Production of Adenosine 5′‐Polyphosphates
Polyphosphate kinases (PPKs) are involved in many metabolic processes; enzymes of the second family (PPK2) are responsible for nucleotide synthesis fuelled by the consumption of inorganic polyphosphate. They catalyse the phosphorylation of nucleotides with various numbers of phosphate residues, such...
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Published in | Chembiochem : a European journal of chemical biology Vol. 20; no. 8; pp. 1019 - 1022 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Germany
Wiley Subscription Services, Inc
15.04.2019
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Subjects | |
Online Access | Get full text |
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Summary: | Polyphosphate kinases (PPKs) are involved in many metabolic processes; enzymes of the second family (PPK2) are responsible for nucleotide synthesis fuelled by the consumption of inorganic polyphosphate. They catalyse the phosphorylation of nucleotides with various numbers of phosphate residues, such as monophosphates or diphosphates. Hence, these enzymes are promising candidates for cofactor regeneration systems. Besides adenosine 5′‐triphosphate, PPK2s also catalyse the synthesis of highly phosphorylated nucleotides in vitro, as shown here for adenosine 5′‐tetraphosphate and adenosine 5′‐pentaphosphate. These unusually phosphorylated adenosine 5′‐polyphosphates add up to 50 % of the whole adenosine nucleotides in the assay. The two new products were chemically synthesised to serve as standards and compared with the two enzymatically produced compounds by high‐performance ion chromatography and 31P NMR analysis. This study shows that PPK2s are highly suitable for biocatalytic synthesis of different phosphorylated nucleotides.
ATP and beyond… Polyphosphate kinases of family 2 (PPK2) catalyse the phosphorylation of nucleotides further than just to the corresponding 5′‐triphosphates. This might make them useful catalysts for the production of cofactor and substrate analogues and help with the elucidation of the natural role of nucleoside polyphosphates. |
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Bibliography: | These authors contributed equally to this work. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1439-4227 1439-7633 |
DOI: | 10.1002/cbic.201800704 |