Properties of polyphosphate: AMP phosphotransferase of Acinetobacter strain 210A

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Published inJournal of Bacteriology Vol. 173; no. 20; pp. 6484 - 6488
Main Authors BONTING, C. F. C, KORTSTEE, G. J. J, ZEHNDER, A. J. B
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.10.1991
Subjects
Acinetobacter - enzymology
Adenosine Monophosphate - metabolism
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
chromatography
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
inhibitors
Kinetics
Laboratorium voor Microbiologie
Metabolism. Enzymes
Microbiological Laboratory
Microbiologie
Microbiology
Phosphotransferases (Phosphate Group Acceptor)
Phosphotransferases - chemistry
Phosphotransferases - isolation & purification
Phosphotransferases - metabolism
polyphosphate:AMP phosphotransferase
Polyphosphates - metabolism
Characterization
Purification
Enzymatic activity
Enzyme
Neisseriaceae
Bacteria
Micrococcales
Acinetobacter
Inhibition
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Abstract Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
AbstractList Polyphosphate:AMP phosphotransferase, an enzyme which catalyzes the phosphorylation of AMP to ADP at the expense of polyphosphate, was purified more than 1500-fold from Acinetobacter strain 210A by streptomycin sulfate precipitation and by Mono-Q, Phenyl Superose, and Superose column chromatography. Streptomycin sulfate precipitation appeared to be an effective step in the purification procedure. During the following chromatographic steps, there was a 29-fold increase in specific activity but the yield was low (0.3%). Kinetic studies showed apparent K sub(m) values of 0.26 mM for AMP and 0.8 mu M for polyphosphate with an average chain length of 35 phosphate groups. The highest activities were found with polyphosphate molecules of 18 to 44 phosphate residues. The polyphosphate chain was degraded completely to ADP. The mechanism of degradation is processive. No activity was obtained with ortho-, pyro-, tri-, and tetraphosphate. The enzyme was inhibited by pyro-, tri-, and tetraphosphate.
Polyphosphate:AMP phosphotransferase, an enzyme which catalyzes the phosphorylation of AMP to ADP at the expense of polyphosphate, was purified more than 1,500-fold from Acinetobacter strain 210A by streptomycin sulfate precipitation and by Mono-Q, Phenyl Superose, and Superose column chromatography. Streptomycin sulfate precipitation appeared to be an effective step in the purification procedure. During the following chromatographic steps, there was a 29-fold increase in specific activity but the yield was low (0.3%). Kinetic studies showed apparent Km values of 0.26 mM for AMP and 0.8 microM for polyphosphate with an average chain length of 35 phosphate groups. The highest activities were found with polyphosphate molecules of 18 to 44 phosphate residues. The polyphosphate chain was degraded completely to ADP. The mechanism of degradation is processive. No activity was obtained with ortho-, pyro-, tri-, and tetraphosphate. The enzyme was inhibited by pyro-, tri-, and tetraphosphate. The inhibition by tri- and tetraphosphate was mixed with polyphosphate as a substrate. The inhibition constants for the dissociation of the enzyme-inhibitor complex and for the enzyme-inhibitor-substrate complex were 0.9 and 6.5 mM, respectively, for triphosphate and 0.7 and 1.5 mM, respectively, for tetraphosphate.
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Author C F Bonting
G J Kortstee
A J Zehnder
AuthorAffiliation Department of Microbiology, Agricultural University Wageningen, The Netherlands
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Issue 20
Keywords Characterization
Purification
Enzymatic activity
Enzyme
Neisseriaceae
Bacteria
Micrococcales
Acinetobacter
Inhibition
Language English
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SSID ssj0014452
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Polyphosphate:AMP phosphotransferase, an enzyme which catalyzes the phosphorylation of AMP to ADP at the expense of polyphosphate, was purified more than...
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SubjectTerms Acinetobacter - enzymology
Adenosine Monophosphate - metabolism
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
chromatography
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
inhibitors
Kinetics
Laboratorium voor Microbiologie
Metabolism. Enzymes
Microbiological Laboratory
Microbiologie
Microbiology
Phosphotransferases (Phosphate Group Acceptor)
Phosphotransferases - chemistry
Phosphotransferases - isolation & purification
Phosphotransferases - metabolism
polyphosphate:AMP phosphotransferase
Polyphosphates - metabolism
Title Properties of polyphosphate: AMP phosphotransferase of Acinetobacter strain 210A
URI http://jb.asm.org/content/173/20/6484.abstract
https://www.ncbi.nlm.nih.gov/pubmed/1655714
https://search.proquest.com/docview/16040766
https://search.proquest.com/docview/72139583
https://pubmed.ncbi.nlm.nih.gov/PMC208984
http://www.narcis.nl/publication/RecordID/oai:library.wur.nl:wurpubs%2F16670
Volume 173
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