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Chemical Compound Review

CHEBI:18412     (2S)-2-amino-5-[[amino...

Synonyms: AC1L3NIV, FT-0673858, AK142567, C05945, 1189-11-3, ...
 
 
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Disease relevance of N-Phospho-L-arginine

  • AK activity was demonstrated in vivo by monitoring the decreases in PArg and ATP resonances during prolonged ischemia [1].
  • Anoxia produced an expected decrease in peak intensities of ATP and arginine phosphate while the peak of intracellular Pi was enhanced and shifted to indicate intracellular acidification during anoxia [2].
  • The extent of changes in arginine phosphate and inorganic phosphate was directly proportional to the magnitude of the imposed acidosis [3].
 

High impact information on N-Phospho-L-arginine

  • The product of the AK enzyme, phosphoarginine (PArg), served as an MRS-visible reporter of AK expression [1].
  • Differential up-regulation of Na+-Ca2+ exchange by phosphoarginine and ATP in dialysed squid axons [4].
  • Arginine kinase catalyzes the reversible transphosphorylation between adenosine diphosphate (ADP) and phosphoarginine, which is involved in temporal and spatial adenosine triphosphate (ATP) buffering [5].
  • Subjecting animals to acute thermal change at an average rate of 1 deg. h-1 led to significant Pi accumulation (equivalent to PLA breakdown) and decrements in the free energy of ATP hydrolysis (dG/dzeta) at both ends of the temperature window, starting at mean critical temperatures (Tc) of 7.0 and 26.8 degrees C, respectively [6].
  • Previous studies have shown that arginine phosphate (AP) recovery in the anaerobic (light) fibers, which demonstrate a fiber size dependence on anaerobic processes following contraction, is too slow to be restricted by intracellular metabolite diffusive flux, in spite of the fiber's large size [7].
 

Chemical compound and disease context of N-Phospho-L-arginine

  • Hypoxia alone induced no change in the adenylate energy charge (AEC), total adenylate (TAN), ATP/ADP ratio or in the equilibrium constant for adenylate kinase K'(ADEN), apparently due to protection of ATP levels by arginine phosphate [8].
 

Biological context of N-Phospho-L-arginine

  • Muscular fatigue corresponds to a 60% breakdown of phosphoarginine, and a 45% increase of sugar phosphates [9].
  • We have demonstrated that phosphoarginine supplies energy as a 'phosphagen' for ciliary beating in Paramecium caudatum, suggesting that phosphoarginine functions not only as a reservoir of energy but also as a transporter of energy in these continuously energy-consuming circumstances. http://www.biologists.com/JEB/movies/jeb3123.html[10]
  • This non-invasive technique is ideal for examining cellular respiration since critical metabolite concentrations, including phosphoarginine ([PA]), inorganic phosphate ([P(i)]) and [ATP], and the arginine kinase (AK) rate constant, can be monitored in real time [11].
  • Arginine kinase (AK) catalyzes the reversible phosphorylation of arginine by MgATP to form a high-energy compound phosphoarginine (Parg) and MgADP in forward reaction in invertebrates [12].
  • Neither acclimation salinity nor salinity change had a significant effect on the concentrations of arginine phosphate, inorganic phosphate or ATP [13].
 

Anatomical context of N-Phospho-L-arginine

 

Associations of N-Phospho-L-arginine with other chemical compounds

 

Gene context of N-Phospho-L-arginine

  • 1. Further addition of protamine molecules leads to a precipitation of the protamine-DNA complexes for arginine-phosphate ratio > or = 1 [23].
  • Arginine kinase, the enzyme responsible for phosphoarginine and ATP synthesis, also shows a differential activity in epimastigote and trypomastigote parasite stages [24].
  • Muscle AEC did not change with molt stage, but levels of ATP (F = 8.050) and ADP (F = 4.130) were significantly higher in premolt (D3 pleopod stage 5.0-5.5) animals; while levels of arginine phosphate (F = 6.981) were significantly higher in post-molt animals [22].
  • 2. Both forms were monomeric (mol. wt. approximately 42,000) and showed the same pH optimum (7.5-8.0) in the direction of phosphoarginine synthesis [25].
 

Analytical, diagnostic and therapeutic context of N-Phospho-L-arginine

References

  1. Noninvasive measurement of gene expression in skeletal muscle. Walter, G., Barton, E.R., Sweeney, H.L. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  2. 31P-NMR studies of the freeze-tolerant larvae of the gall fly, Eurosta solidaginis. Storey, K.B., Miceli, M., Butler, K.W., Smith, I.C., Deslauriers, R. Eur. J. Biochem. (1984) [Pubmed]
  3. Graded intracellular acidosis produces extensive and reversible reductions in the effective free energy change of ATP hydrolysis in a molluscan muscle. Combs, C.A., Ellington, W.R. J. Comp. Physiol. B, Biochem. Syst. Environ. Physiol. (1995) [Pubmed]
  4. Differential up-regulation of Na+-Ca2+ exchange by phosphoarginine and ATP in dialysed squid axons. DiPolo, R., Beaugé, L. J. Physiol. (Lond.) (1998) [Pubmed]
  5. Arginine kinase overexpression improves Trypanosoma cruzi survival capability. Pereira, C.A., Alonso, G.D., Ivaldi, S., Silber, A.M., Alves, M.J., Torres, H.N., Flawiá, M.M. FEBS Lett. (2003) [Pubmed]
  6. Critical temperatures in the cephalopod Sepia officinalis investigated using in vivo 31P NMR spectroscopy. Melzner, F., Bock, C., Pörtner, H.O. J. Exp. Biol. (2006) [Pubmed]
  7. A reaction-diffusion analysis of energetics in large muscle fibers secondarily evolved for aerobic locomotor function. Hardy, K.M., Locke, B.R., Da Silva, M., Kinsey, S.T. J. Exp. Biol. (2006) [Pubmed]
  8. The effect of lead on the metabolic and energetic status of the Yabby, Cherax destructor, during environmental hypoxia. Morris, S., van Aardt, W.J., Ahern, M.D. Aquat. Toxicol. (2005) [Pubmed]
  9. In vivo 31P NMR in crustacean muscles: fatigue and recovery in the tail musculature from the prawn Palaemon elegans. Thébault, M.T., Raffin, J.P., Le Gall, J.Y. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
  10. ATP-regenerating system in the cilia of Paramecium caudatum. Noguchi, M., Sawada, T., Akazawa, T. J. Exp. Biol. (2001) [Pubmed]
  11. Sublethal actions of copper in abalone (Haliotis rufescens) as characterized by in vivo 31P NMR. Viant, M.R., Walton, J.H., TenBrook, P.L., Tjeerdema, R.S. Aquat. Toxicol. (2002) [Pubmed]
  12. The roles of C-terminal loop residues of dimeric arginine kinase from sea cucumber Stichopus japonicus in catalysis, specificity and structure. Zhang, J.W., Zhao, T.J., Wang, S.L., Guo, Q., Liu, T.T., Zhao, F., Wang, X.C. Int. J. Biol. Macromol. (2006) [Pubmed]
  13. The effects of rapid salinity change on in vivo arginine kinase flux in the juvenile blue crab, Callinectes sapidus. Kinsey, S.T., Lee, B.C. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2003) [Pubmed]
  14. Participation of calcium ions in the molecular mechanism of cardioprotective action of exogenous phosphocreatine. Konorev, E.A., Medvedeva, N.V., Jaliashvili, I.V., Lakomkin, V.L., Saks, V.A. Basic Res. Cardiol. (1991) [Pubmed]
  15. Synthesis of phosphocreatine and phosphoarginine by mitochondria from various sources. Hird, F.J., McLean, R.M. Comp. Biochem. Physiol., B (1983) [Pubmed]
  16. Nutritional status and energy metabolism of crayfish (Procambarus clarkii, Girard) muscle and hepatopancreas. Schirf, V.R., Turner, P., Selby, L., Hannapel, C., de la Cruz, P., Dehn, P.F. Comparative biochemistry and physiology. A, Comparative physiology. (1987) [Pubmed]
  17. The collagen content of selected animals. Cianciosi, S.C., Hird, F.J. Comp. Biochem. Physiol., B (1986) [Pubmed]
  18. Purification and properties of adductor muscle phosphofructokinase from the oyster, Crassostrea virginica. The aerobic/anaerobic transition: role of arginine phosphate in enzyme control. Storey, K.B. Eur. J. Biochem. (1976) [Pubmed]
  19. 31P-nuclear-magnetic-resonance study of muscles from Mytilus edulis. Schanck, A., Verbaert, B., Van Meersche, M., Baguet, F., Devroede, J. Eur. J. Biochem. (1986) [Pubmed]
  20. Differential effects of arginine, glutamate and phosphoarginine on Ca(2+)-activation properties of muscle fibres from crayfish and rat. Jame, D.W., West, J.M., Dooley, P.C., Stephenson, D.G. J. Muscle Res. Cell. Motil. (2004) [Pubmed]
  21. Studies on the apparent inhibition of the type-M pyruvate kinase from Carcinus maenas (the common shore crab) by phospho-L-arginine [proceedings]. Giles, I.G., Poat, P.C., Munday, K.A. Biochem. Soc. Trans. (1980) [Pubmed]
  22. Adenylate energy charge, arginine phosphate and ATPase activity in juvenile Homarus americanus during the molt cycle. Dehn, P.F., Haya, K., Aiken, D.E. Comp. Biochem. Physiol., B (1985) [Pubmed]
  23. Interaction of human P1 and P2 protamines with DNA. Bianchi, F., Rousseaux-Prevost, R., Bailly, C., Rousseaux, J. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  24. Arginine metabolism in Trypanosoma cruzi is coupled to parasite stage and replication. Pereira, C.A., Alonso, G.D., Ivaldi, S., Silber, A., Alves, M.J., Bouvier, L.A., Flawiá, M.M., Torres, H.N. FEBS Lett. (2002) [Pubmed]
  25. Purification and properties of two molecular forms of arginine kinase from the adductor muscle of the scallop, Pecten maximus. Reddy, S.R., Roustan, C., Benyamin, Y. Comp. Biochem. Physiol., B (1991) [Pubmed]
  26. Optimized method for the determination of phosphoarginine in abalone tissue by high-performance liquid chromatography. Viant, M.R., Rosenblum, E.S., Tjeerdema, R.S. J. Chromatogr. B Biomed. Sci. Appl. (2001) [Pubmed]
  27. An investigation into the apparent inhibition by arginine phosphate of the activity of Carcinus maenas type-M pyruvate kinase. Poat, P.C., Giles, I.G., Munday, K.A. Biochim. Biophys. Acta (1980) [Pubmed]
 
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