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PMID: 10660553 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The multiple activities of polyphosphate kinase of Escherichia coli and their subunit structure determined by radiation target analysis.

The Journal of biological chemistry ·Vol. 275 ·No. 6 ·2000-02-11 ·Pages 3977-83

Tzeng CM, Kornberg A

Abstract

Polyphosphate kinase (PPK), the principal enzyme required for the synthesis of inorganic polyphosphate (polyP) from ATP, also exhibits other enzymatic activities, which differ significantly in their biochemical optima and responses to chemical agents. These several activities include: polyP synthesis (forward reaction), nATP --> polyP(n) + nADP (Equation 1); ATP synthesis from polyP (reverse reaction), ADP + polyP(n) --> ATP + polyP(n - 1) (Equation 2); general nucleoside-diphosphate kinase, GDP + polyP(n) --> GTP + polyP(n - 1) (Equation 3); linear guanosine 5'-tetraphosphate (ppppG) synthesis, GDP + polyP(n) --> ppppG + polyP(n - 2) (Equation 4); and autophosphorylation, PPK + ATP --> PPK-P + ADP (Equation 5). The Mg(2+) optima are 5, 2, 1, and 0.2 mM, respectively, for the activities in Equations 1, 2, 3, and 4. Inorganic pyrophosphate inhibits the activities in Equations 1 and 3 but stimulates that in Equation 4. The kinetics of the activities in Equations 1, 2, and 3 are highly processive, whereas the transfer of a pyrophosphoryl group from polyP to GDP (Equation 4) is distributive and demonstrates a rapid equilibrium, random Bi-Bi catalytic mechanism. Radiation target analysis revealed that the principal functional unit of the homotetrameric PPK is a dimer. Exceptions are a trimer for the synthesis of ppppG (Equation 4) and a tetrameric state for the autophosphorylation of PPK (Equation 5) at low ATP concentrations. Thus, the diverse functions of this enzyme involve different subunit organizations and conformations. The highly conserved homology of PPK among 18 microorganisms was used to determine important residues and conserved regions by alanine substitution, by site-directed mutagenesis, and by deletion mutagenesis. Of 46 single-site mutants, seven exhibit none of the five enzymatic activities; in one mutant, ATP synthesis from polyP is reduced relative to GTP synthesis. Among deletion mutants, some lost all five PPK activities, but others retained partial activity for some reactions but not for others.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/chemistry Diphosphates/pharmacology Enzyme Inhibitors/pharmacology Escherichia coli/enzymology Gamma Rays Guanidine/pharmacology Guanosine Tetraphosphate/biosynthesis Kinetics Magnesium/pharmacology Molecular Sequence Data Mutation Nucleotides/metabolism Phosphorylation/radiation effects Phosphotransferases (Phosphate Group Acceptor)/chemistry,metabolism,radiation effects Polyphosphates/metabolism Protein Conformation Sequence Alignment
Chemicals
Bacterial Proteins Diphosphates Enzyme Inhibitors Nucleotides Polyphosphates Guanosine Tetraphosphate Phosphotransferases (Phosphate Group Acceptor) polyphosphate kinase Magnesium Guanidine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tzeng C M
Department of Biochemistry, Stanford University, Stanford, California 94305-5307, USA.
Kornberg A
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2000-02-11
Pages
3977-83
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM07581-38 · United States
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