Abstract
Vibrio cholerae O1, biotype El Tor, accumulates inorganic polyphosphate (poly P) principally as large clusters of granules. Poly P kinase (PPK), the enzyme that synthesizes poly P from ATP, is encoded by the ppk gene, which has been cloned from V. cholerae, overexpressed, and knocked out by insertion-deletion mutagenesis. The predicted amino acid sequence of PPK is 701 residues (81.6 kDa), with 64% identity to that of Escherichia coli, which it resembles biochemically. As in E. coli, ppk is part of an operon with ppx, the gene that encodes exopolyphosphatase (PPX). However, unlike in E. coli, PPX activity was not detected in cell extracts of wild-type V. cholerae. The ppk null mutant of V. cholerae has diminished adaptation to high concentrations of calcium in the medium as well as motility and abiotic surface attachment.
MeSH Terms
Amino Acid Sequence
Base Sequence
DNA, Bacterial
Diphosphotransferases/genetics,metabolism,physiology
Genes, Bacterial
Molecular Sequence Data
Mutagenesis
Phosphates/metabolism
Phosphoprotein Phosphatases
Polymers
Vibrio cholerae/enzymology,genetics,metabolism
Chemicals
DNA, Bacterial
Phosphates
Polymers
Diphosphotransferases
nucleotide 3'-pyrophosphokinase-2',3'-cyclic monophosphokinase
Phosphoprotein Phosphatases
protein phosphatase 4
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ogawa N
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA.
Tzeng C M
Fraley C D
Kornberg A
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