2 edition of Interaction of ATP analogs with myosin found in the catalog.
Interaction of ATP analogs with myosin
Written in English
|Other titles||Interaction of adenosine triphosphate analogs with myosin.|
|Statement||by Donald Wang.|
|The Physical Object|
|Pagination||xi, 97 leaves, bound :|
|Number of Pages||97|
Biochemistry ,31, Synthesis and Properties of a Conformationally Restricted Spin-Labeled Analog of ATP and Its Interaction with Myosin and Skeletal Muscle? Dario R. Alessi: John E. T. Corrie,g Piotr G. Fajer,llJ Michael A. Ferenczi,f David D. Thomas,// Ian P. Trayer,'J and David R. Trenthaml School of Biochemistry, The University of Birmingham, . rived from ATP hydrolysis which occurs on the myosin activated by F-actin (2). The control of this mechanism in vertebrate skeletal muscle involves reversible inhibition of the interaction between actin and myosin, which can be biochemically monitored by measuring the 1Llg2+ATPase activity of actomyosin at low.
Thermogenesis by resting muscle varies with conditions and plays an active role in homeostasis of body weight. The low metabolic rate of living resting muscles requires that ATP turnover by myosin be inhibited relative to the purified protein in vitro. This inhibition has not been previously seen in in vitro systems. We used quantitative epifluorescence microscopy of . Myosin binds to actin at a binding site on the globular actin protein. Myosin has another binding site for ATP at which enzymatic activity hydrolyzes ATP to ADP, releasing an inorganic phosphate molecule and energy. ATP binding causes myosin to release actin, allowing actin and myosin to detach from each other.
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Interactions between these synthetic ATP analogues and actomyosin systems, as indicated by the decrease in light scattering of myosin I3 solution, the hydrolysis by myosin A under various * Present address: Institute for Enzyme Research, University of Wisconsin, Madison, Wis.
(U,S.A.).Cited by: 6. Structural states of the skeletal muscle actin-myosin complex detected by TR-FRET. (A) Fluorescence decay of 1 µM AF actin (D, black) with 5 µM AF labeled S1A1 and 10 µM S1A2 respectively, in the absence (D + A, green) and presence of saturating ATP (D + A + ATP, red), acquired during the steady decay in the presence of acceptor Cited by: 8.
Two such analogues, 3'-O-(N-methylanthraniloyl)azido-ATP (MantN3-ATP) and 8-Br-ATP, were synthesized and used to probe the conformation of the ATP-binding site of myosin. In the presence of these analogues, actomyosin was rapidly dissociated; Mg2+-dependent ATP hydrolysis was significantly activated by actin; and Pi bursting was by: ATP has long been known to play a central role in the energetics of cells both in transduction mechanisms and in metabolic pathways, and is involved in regulation of enzyme, channel and receptor activities.
Numerous ATP analogues have been synthesised to probe the role of ATP in biosystems ([Yount,Cited by: The following compounds were synthesized as analogues of ATPmorpho 5′-triphosphate (III) and 2,6-dimethlymercaptoβ-d-ribofuranosylpurine 5′-triphosphate (V).The interactions of these analogues with actomyosin system were investigated, together with those of 3′-deoxythymidine 5′-triphosphate (I), thymidine 5′-triphosphate (II)and 2′,3′-O-isopropylidene adenosine 5 Cited by: Various 8-substituted ATP analogs were synthesized, and their reactions with myosin and actomyosin were studied.
The nucleoside triphosphates (NTPs) with an amino group at the 6 position and hydrogen at the 8 position, and formycin 5'-triphosphate (FTP) were hydrolyzed by myosin very slowly in the presence of Mg2+ and rapidly in the presence of EDTA and K+.
Firstly, we consider purine-based nucleotides. Fig. 2 shows the interaction of GTP with myosin predicted by the MD simulations. An overlay of the myosinGTP MD simulation structure and the myosinATP MD structure via a least-squares distance minimization on the P-loops places the GTP 6-position carbonyl oxygen only Å from the 6-position amine nitrogen of ATP.
Some of these analogs (e.g., ITP, GTP, and aza-ATP) bind more slowly to myosin, support less force and shortening velocity, and have slower steady-state hydrolysis rates than when MgATP is the substrate for contraction (Pate et. Muscle - Muscle - Actin-myosin interaction and its regulation: Mixtures of myosin and actin in test tubes are used to study the relationship between the ATP breakdown reaction and the interaction of myosin and actin.
The ATPase reaction can be followed by measuring the change in the amount of phosphate present in the solution. The myosin-actin interaction also. A wide variety of purine- and pyrimidine-based nucleotides can serve as a substrate for actomyosin mechanics, but with varying effectiveness.
To understand the myosin-ATP interaction and in particular, the interactions with the base, we have used molecular dynamics simulations to model the interactions of myosin with ATP, CTP, UTP, aza-ATP. The force and displacement caused by the myosin head were determined by measuring the displacement of the bead with nanometer accuracy (Finer et al.
).Individual ATPase reactions of single one-headed myosin molecules were measured by directly observing association-dissociation events of a fluorescent ATP analog labeled with Cy3 (Funatsu et al.
Abstract. Various 8-substituted ATP analogs were synthesized, and their reactions with myosin and actomyosin were studied. The nucleoside triphosphates (NTPs) with an amino group at the 6 position and hydrogen at the 8 position, and formycin 5'-triphosphate (FTP) were hydrolyzed by myosin very slowly in the presence of Mg2+ and rapidly in the presence of EDTA and K+.
ATP can then attach to myosin, which allows the cross-bridge cycle to start again and further muscle contraction can occur (Figure 1). The movement of the myosin head back to its original position is called the recovery stroke.
Resting muscles store energy from ATP in the myosin heads while they wait for another contraction. of these analogs (e.g., ITP, GTP, and aza-ATP) bind more slowly to myosin, support less force and shortening veloc-ity, and have slower steady-state hydrolysis rates than when MgATP is the substrate for contraction (Pate et al.,; White et al., ).
Two notable exceptions to this are 2-[(4-azidonitrophenyl)amino]ethyltriphosphate. Two such analogues, 3'-O-(N-methylanthraniloyl)azido-ATP (MantN3-ATP) and 8-Br-ATP, were synthesized and used to probe the conformation of the ATP-binding site of myosin.
In the presence of these analogues, actomyosin was rapidly dissociated; Mg2+-dependent ATP hydrolysis was significantly activated by actin; and P(i) bursting was observed.
Interaction of vanadate with uridine and adenosine monophosphate. Formation of ADP and ATP analogs. Journal of the American Chemical Society(17), ATP analogues and the guinea-pig taenia coli: a comparison of the structure-activity relationships of ectonucleotidases with those of the P2-purinoceptor.
European Journal of Pharmacology(3), Synthesis and properties of a conformationally restricted spin-labeled analog of ATP and its interaction with myosin and skeletal muscle. Dario R. Alessi, John E. Corrie, Piotr G. Fajer, Michael A. Ferenczi, David D. Thomas, Ian P.
Trayer, and ; David R. Trentham. Kinetics of the interaction of 2'(3')-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two complexes. Biochemistry30 (2), Interaction between actomyosin and 8-substituted ATP analogs. Takenaka H, Ikehara M, Tonomura Y.
Various 8-substituted ATP analogs were synthesized, and their reactions with myosin and actomyosin were studied. The nucleoside triphosphates (NTPs) with an amino group at the 6 position and hydrogen at the 8 position, and formycin 5'-triphosphate.
myosin (Fig. 4), suggesting that under these conditions skeletal myosin has relatively fewer crossbridges in a ‘strong-binding’ state compared to smooth muscle myosin.
Another way of observing the effect of ‘weak-binding’ bridges on movement is to use the well-characterized chemically modified analog, pPDM-skeletal myosin. The intrinsic chemical reaction of adenosine triphosphate (ATP) hydrolysis catalyzed by myosin is modeled by using a combined quantum mechanics and molecular mechanics (QM/MM) methodology that achieves a near ab initio representation of the entire model.
Starting with coordinates derived from the heavy atoms of the crystal structure (Protein Data Bank ID code [1VOM]) in which myosin .2-[(2-Nitrophenyl)amino]ethyl triphosphate (NPhAETP) is the smallest ATP analogue that serves as a substrate for the actin-activated ATPase of myosin subfragment 1 (S1) and supports the development of active tension in skinned fibers.
2-(Phenylamino)ethyl triphosphate (PhAETP), in which the nitro group on the phenyl ring of NPhAETP is substituted by a H atom, is also a .