Properties of polyphosphatase ofAcinetobacter johnsonii 210A
- 1 January 1993
- journal article
- Published by Springer Nature in Antonie van Leeuwenhoek
- Vol. 64 (1) , 75-81
- https://doi.org/10.1007/bf00870924
Abstract
Polyphosphatase, an enzyme which hydrolyses highly polymeric polyphosphates to Pi, was purified 77-fold fromAcinetobacter johnsonii 210A by Q-Sepharose, hydroxylapatite and Mono-Q column chromatography. The native molecular mass estimated by gel filtration and native gel electrophoresis was 55 kDa. SDS-polyacrylamide gel electrophoresis indicated that polyphosphatase ofAcinetobacter johnsonii 210A is a monomer. The enzyme was specific for highly polymeric polyphosphates and showed no activity towards pyrophosphate and organic phosphate esters. The enzyme was inhibited by iodoacetamide and in the presence of 10 mM Mg2+ by pyro- and triphosphate. The apparent Km-value for polyphosphate with an average chain length of 64 residues was 5.9 µM and for tetraphosphate 1.2 mM. Polyphosphate chains were degraded to short chain polymers by a processive mechanism. Polyphosphatase activity was maximal in the presence of Mg2+ and K+.Keywords
This publication has 21 references indexed in Scilit:
- The Physiological Role of Inorganic Polyphosphates in Microorganisms: Some Evolutionary AspectsPublished by Springer Nature ,1990
- ATP production from polyphosphate in Acinetobacter strain 210AArchiv für Mikrobiologie, 1987
- Preparation of standards and determination of sizes of long-chain polyphosphates by gel electrophoresisAnalytical Biochemistry, 1987
- Quantitative detection of orthophosphate in polyacrylamide gelsAnalytical Biochemistry, 1985
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Polyphosphate phosphohydrolase from Endomyces magnushBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresisArchives of Biochemistry and Biophysics, 1968
- Purification and Properties of a Polymetaphosphatase from Corynebacterium xerosisJournal of General Microbiology, 1959