Class III Polyphosphate Kinase 2 Enzymes Catalyze the Pyrophosphorylation of Adenosine-5'-Monophosphate.
Adenosine Diphosphate
/ chemistry
Adenosine Monophosphate
/ chemistry
Amino Acid Sequence
Biocatalysis
Deinococcus
/ enzymology
Delftia
/ enzymology
Diphosphates
/ chemistry
Kinetics
Phosphates
/ chemistry
Phosphorylation
Phosphotransferases (Phosphate Group Acceptor)
/ chemistry
Substrate Specificity
enzymes
kinetics
phosphorylation
polyphosphate kinase 2
reaction mechanisms
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
02 12 2019
02 12 2019
Historique:
received:
08
05
2019
pubmed:
18
6
2019
medline:
14
8
2020
entrez:
18
6
2019
Statut:
ppublish
Résumé
Polyphosphate kinase 2 (PPK2) transfer phosphate from inorganic polyphosphate to nucleotides. According to their activity, PPK2 enzymes are classified into three groups. Among them, class III enzymes catalyze both the phosphorylation of nucleotide mono- to diphosphates and di- to triphosphates by using polyphosphate, which is a very inexpensive substrate. Therefore, class III enzymes are very attractive for use in biotechnological applications. Despite several studies on class III enzymes, a detailed mechanism of how phosphate is transferred from the polyphosphate to the nucleotide remains to be elucidated. Herein, it is reported that PPK2 class III enzymes from two different bacterial species catalyze the phosphorylation of adenosine mono- (AMP) into triphosphate (ATP) not only through step-by-step phosphorylation, but also by pyrophosphorylation. These are the first PPK2 enzymes that have been shown to possess polyphosphate-dependent pyrophosphorylation activity.
Identifiants
pubmed: 31206993
doi: 10.1002/cbic.201900303
doi:
Substances chimiques
Diphosphates
0
Phosphates
0
Adenosine Monophosphate
415SHH325A
diphosphoric acid
4E862E7GRQ
Adenosine Diphosphate
61D2G4IYVH
Phosphotransferases (Phosphate Group Acceptor)
EC 2.7.4.-
polyphosphate kinase
EC 2.7.4.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2961-2967Subventions
Organisme : Japan society for the promotion of Science
ID : 17H00888
Pays : International
Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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