Synthesis of phosphocreatine and phosphoarginine by mitochondria from various sources

Hird, FJ; McLean, R.M.

doi:10.1016/0305-0491(83)90168-2

Cited by 4 publications

(2 citation statements)

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“…Phosphorylation of compounds containing a guanidino group was evaluated using an indirect assay that detects the conversion of ATP to ADP by an enzyme‐coupled system (Hird and McLean 1983). Different compounds, including L‐arginine (Km 0.33 mM, determined using the direct isotopic assay), were tested at 10 mM concentration.…”

Section: Resultsmentioning

confidence: 99%

“…of 1 ml. Arginine kinase activity was calculated from the consumption of NADH, measured as a decrease in absorbance at 340 nm, during 10‐min reactions (Hird and McLean 1983). To determine whether the compounds tested for inhibition of arginine kinase activity in the indirect competition assay inhibited the coupling enzymes, all the drugs were tested in the presence of 1.5 mM ADP to bypass the arginine kinase reaction.…”

Section: Methodsmentioning

confidence: 99%

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Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi

Pereira

Alonso

Ivaldi

et al. 2003

J Eukaryotic Microbiology

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Arginine kinase catalyzes the transphosphorylation between phosphoarginine and ADP. Phosphoarginine is involved in temporal ATP buffering and inorganic phosphate regulation. Trypanosoma cruzi arginine kinase phosphorylates only L-arginine (specific activity 398.9 x mUE-min(-1) x mg(-1)), and is inhibited by the arginine analogs, agmatine, canavanine, nitroarginine, and homoarginine. Canavanine and homoarginine also produce a significant inhibition of the epimastigote culture growth (79.7% and 55.8%, respectively). Inhibition constants were calculated for canavanine and homoarginine (7.55 and 6.02 mM, respectively). In addition, two novel guanidino kinase activities were detected in the epimastigote soluble extract. The development of the arginine kinase inhibitors of T. cruzi could be an important feature because the phosphagens biosynthetic pathway in trypanosomatids is different from the one in their mammalian hosts.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%