ATP:AMP phosphotransferase

Ctrnacta V, Ault JG, Stejskal F, Keithly JS (2006) Localization of pyruvate NADP(+) oxido-reductase in sporozoites of Cryptosporidiumparvum. J Eukaryot Microbiol 53 225-231 Dederck PJ, Muller M (1987) Hydrogenosomal ATP AMP phosphotransferase of Trichomonas vaginalis. Comp Biochem Physiol 88 575-580 Docampo R, Moreno SN, Mason RP (1987) Free radical intermediates in the reaction of pyruvate ferredoxin oxidoreductase in Tritrichomonas foetus hydrogenosomes. J Biol Chem 262 12417-12420... 

Thuma, E. Schirmer, R.H. Schirmer, I. Preparation and characterization of a crystalline human ATP AMP phosphotransferase. Biochim. Biophys. Acta, 268, 81-91 (1972)... 

Dinbergs, I.D. Lindmark, D.G. Tritrichomonas foetus purification and characterization of hydrogenosomal ATP AMP phosphotransferase (adenylate kinase). Exp. Parasitol., 69, 150-156 (1989)... 

Batra, P.P. Burnette, B. Takeda, K. Purification and characterization of ATP AMP phosphotransferase from Mycobacterium marinum. Biochim. Biophys. Acta, 869, 350-357 (1986)... 

The following method has been described for the assay of cyclic AMP [144, 145]. Cyclic AMP is converted to 5 -AMP with the aid of phosphodiesterase and then to ATP with myokinase (EC 2.V.4.3 ATP AMP phosphotransferase adenylate kinase) and pyruvate kinase (EC 2.7.1.40 ATP pyruvate phosphotransferase). ATP is measured by determining the orthophosphate which accumulates during incubation of ATP with a cycling system containing myosin, pyruvate kinase, and phosphoenol pyruvate. Alternately, the ATP is determined by its luminescent reaction with firefly luciferin and luciferase [145-147]. With a sensitivity to about 1 pmol/tube of cyclic AMP, this assay is almost as sensitive as the phosphorylase method, but with a linearity over three orders of magnitude, it is linear over a much wider range than the phosphorylase method. 

Tomasselli AG, Noda LH (1980) Mitochondrial ATP AMP phosphotransferase from beef heart Purifications and properties. Eur. J. Biochem. 103, 481-491. 

Adenylate kinase (AK) is a ubiquitous monomeric enzyme that catalyzes the interconversion of AMP, ADP, and ATP. This interconversion of the adenine nucleotides seems to be of particular importance in regulating the equilibrium of adenine nucleotides in tissues, especially in red blood cells. AK has three isozymes (AK 1,2, and 3). AK 1 is present in the cytosol of skeletal muscle, brain, and red blood cells, and AK 2 is found in the intermembrane space of mitochondria of liver, kidney, spleen, and heart. AK 3, also called GTP AMP phosphotransferase, exists in the mitochondrial matrix of liver and heart. 

Kameda, A. Shiba, T. Kawazoe, Y. Satoh, Y. Ihara, Y. Munekata, M. Ishige, K. Noguchi, T. A novel ATP regeneration system using polyphos-phate-AMP phosphotransferase and polyphosphate kinase. J. Biosci. Bioeng., 91, 557-563 (2001)... 

S. M. Resnick and A. J. Zehnder (2000). In vitro ATP regeneration from polyphosphate and AMP by polyphosphate AMP phosphotransferase and adenylate kinase from Acinetobacter johnsonii 210A. Appl. Environ. Microbiol., 6, 2045-2051. 

Polyphosphate can replace ATP in the phosphorylation of glucose in numerous microorganisms [23,24]. Since the equilibrium of Reaction (1) is on the side of polyphosphate synthesis, this enzyme is not employed in polyphosphate degradation. Instead, a poly-P AMP phosphotransferase activity was found in cell-free extracts of the phosphate-accumulating bacterium Acinetobacter johnsonii which catalyzes Reaction (2)... 

A number of reactions which consume ATP generate AMP rather than ADP as a product, only few produce adenosine [534]. ATP may be recycled from AMP using polyphosphate-AMP phosphotransferase and polyphosphate kinase in a tandem-process at the expense of inorganic polyphosphate as phosphate donor for both steps. Alternatively, the combination of adenosine kinase and adenylate kinase were used (Scheme 2.80) [535]. 

The transport of each COg requires the expenditure of two high-energy phosphate bonds. The energy of these bonds is expended in the phosphorylation of pyruvate to PEP (phosphoenolpyruvate) by the plant enzyme pyruvate-Pj dikinase the products are PEP, AMP, and pyrophosphate (PPi). This represents a unique phosphotransferase reaction in that both the /3- and y-phosphates of a single ATP are used to phosphorylate the two substrates, pyruvate and Pj. The reaction mechanism involves an enzyme phosphohistidine intermediate. The y-phosphate of ATP is transferred to Pj, whereas formation of E-His-P occurs by addition of the /3-phosphate from ATP ... 

A cyclic AMP independent protein kinase which catalyzes the phosphorylation of histidine in histones has been found in nuclei from rat tissue and in Walker-256 carcinosarcoma cell nuclei (96). Two histone kinases (ATP histone N-phosphotransferase) have been partially purified from the nuclei of the carcinosarcoma cells (78a). One of these enzymes preferentially phosphorylates histone H4 (IV, F2al) at an optimum pH of 9.5, while the other preferentially phosphorylates histone I (FI) at an optimum pH of 6.5. Both enzymes had an absolute requirement for Mg2+, required similar levels of ATP, and were not stimulated by added cyclic AMP or cyclic GMP. The pH 9.5 kinase was strongly inhibited by relatively low concentrations of GTP and CTP, but the pH 6.5 kinase was not affected. The pH 9.5 kinase phosphorylates the only two histidines (His-18 and His-75) in histone H4 to form 3-phosphohistidine. The pH 6.5 kinase phosphorylates the c-amino group of a lysine residue in histone I. Location of this lysine is not known. The phospho groups of both these derivatives are acid labile. 

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