P1,P5-Di(adenosine-5′)pentaphosphate, a Potent Multisubstrate Inhibitor of Adenylate Kinase
Journal of Biological ChemistryPublished 1 February 1973Open access
Gustav E. Lienhard, Isaac I. Secemski
Citations522
SJR quartileQ1
SJR score1.71
SNIP1.00
Generate an AI Snapshot to get a quick, structured summary of this paper.
Study Snapshot
ObjectiveStudy objective
MethodsResearch methodology
PopulationPopulation studied
Sample sizeSample sizes
OutcomesStudy outcomes here
ResultsStudy results comes here
LimitationsResearch study limitations comes here
A concise AI-generated summary of the paper will appear here once you click Generate AI Snapshot.
TL;DR
Rabbit muscle adenylate kinase is potently inhibited by P1,P5-di(adenosine-5')pentaphosphate (Ap5A) but not by the homologs of this compound with fewer phosphoryl groups in the polyphosphate bridge and not by adenosine 5'-pentaph phosphate.
Abstract
Abstract Rabbit muscle adenylate kinase is potently inhibited by P1,P5-di(adenosine-5')pentaphosphate (Ap5A) but not by the homologs of this compound with fewer phosphoryl groups in the polyphosphate bridge and not by adenosine 5'-pentaphosphate. The inhibition by Ap5A is competitive with respect to both of the substrates, AMP and ATP. The association constant for the binding of Ap5A to adenylate kinase is about 4 x 108 m-1 at 24° and pH 8.0.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
Accounts of Chemical ResearchAnalog approaches to the structure of the transition state in enzyme reactions
597 Citations1972Richard Wolfenden
Journal of Biological ChemistryInitial Velocity and Equilibrium Kinetics of Myokinase
185 Citations1968David G. Rhoads, John M. Lowenstein
The mechanism of myokinase (ATP-AMP phosphotransferase, EC 2.7.4.3) from rabbit muscle has been investigated by studies of equilibrium isotope exchange and initial velocities and Michaelis constants for the four reactants are presented.
Annual Review of BiochemistryMitochondrial Oxidations and Energy Coupling
146 Citations1967Maynard E. Pullman, G. Schatz
Biochemical and Biophysical Research CommunicationsIsolation and characterization of dinucleoside tetra- and tri-phosphates formed in the presence of lysyl-sRNA synthetase
137 Citations1966Kurt Randerath, Claude M. Janeway +2 more
Annual Review of BiochemistryEnzymic Phosphoryl Group Transfer
93 Citations1972John F. Morrison, Elizabeth Heyde
BiochemistryStudies on Adenosine Triphosphate Transphosphorylases. IV. Enzyme-Substrate Interactions<sup>*</sup>
78 Citations1962Stephen A. Kuby, Theodore A. Mahowald +1 more
Biochimica et Biophysica Acta (BBA) - EnzymologyInhibition of rabbit skeletal muscle adenylate kinase by the transition state analogue, P1,P4-di(adenosine-5′)tetraphosphate
50 Citations1972Daniel L. Purich, Herbert J. Fromm
Inhibition studies of rabbit muscle adenylate kinase indicate that the transition state analogue, P 1, P 4 -di(adenosine-5′)-tetraphosphate, is a competitive inhibitor relative to ATP and AMP.
The Journal of Organic ChemistryDismutation Reactions of Nucleoside Polyphosphates. III. The Synthesis of α,ι-Dinucleoside 5'-Polyphosphates<sup>1</sup>
43 Citations1965Jürgen Reiß, J. G. Moffatt
Annual reports in medicinal chemistryChapter 23. Transition State Analogs as Enzyme Inhibitors
40 Citations1972Gustav E. Lienhard
A general approach is described for the design of specific, potent reversible enzyme inhibitors that are called transition state analogs, a compound that resembles in structure the substrate portion of the transition state of the enzymatic reaction.
Journal of Chromatography ASeparation of polyphosphates by anion exchange thin layer chromatography
24 Citations1968J.M. Tanzer, Micah I. Krichevsky +1 more
The method allows separation of several linear and cyclical phosphates by one-dimensional development of thin layer plates and also permits estimation of the approximate chain lengths of the components of polyphosphates glasses.
Methods in enzymology on CD-ROM/Methods in enzymology[27] Myokinase, ATP-AMP transphosphorylase
18 Citations1963Lafayette Noda, Stephen A. Kuby
The enzyme is phenomenally stable as a crystalline suspension with essentially no loss in activity over more than a six-month period.
Biochemical JournalAmino acid sequences aroung the thiol groups of myokinase
14 Citations1968Alan G. Weeds, Lafayette Noda
Digested with trypsin in acetatetrypsin/substrate weight digest concentrated evaporation and then submitted to ionophoresis at A strip ionophoretogram submitted to further ionophoreogram pH2 at right angles first five first spot pH.