Thermodynamics of the Arginine Kinase Reaction

Teague, Walter E.; Dobson, Geoffrey P.

doi:10.1074/jbc.274.32.22459

Cited by 30 publications

(32 citation statements)

References 14 publications

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“…S6), and not when the arginine residue was mutated to lysine or alanine. This observation suggests that a transfer of the phospho-group from the high-energy phosphoramidate N-P linkage (7,22) to the -OH group of the tyrosine can occur in vitro. Consistent with this hypothesis, the chemically more stable phospho-tyrosines were detected in extracts of hydrolyzed phosphorylated McsB and McsA protein preparations by TLC (9).…”

Section: Discussionmentioning

confidence: 92%

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

Elsholz

Turgay

Michalik

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

126

196

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Reversible protein phosphorylation is an important and ubiquitous protein modification in all living cells. Here we report that protein phosphorylation on arginine residues plays a physiologically significant role. We detected 121 arginine phosphorylation sites in 87 proteins in the Gram-positive model organism Bacillus subtilis in vivo. Moreover, we provide evidence that protein arginine phosphorylation has a functional role and is involved in the regulation of many critical cellular processes, such as protein degradation, motility, competence, and stringent and stress responses. Our results suggest that in B. subtilis the combined activity of a protein arginine kinase and phosphatase allows a rapid and reversible regulation of protein activity and that protein arginine phosphorylation can play a physiologically important and regulatory role in bacteria.McsB | YwlE | ClpC | HSP100/Clp | phosphagen kinase

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Section: Discussionmentioning

confidence: 92%

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

Elsholz

Turgay

Michalik

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

126

196

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“…The resting metabolite concentrations for crustacean anaerobic locomotor fibers were obtained from a combination of the data in Head and Baldwin (1986), 31 P-NMR spectra collected by Kinsey and Ellington (1996) and calculations using the AK equilibrium constant (Teague and Dobson, 1999). The resting metabolite concentrations were the same in small and large fibers (Baldwin et al, 1999).…”

Section: Mathematical Modelingmentioning

confidence: 99%

“…A K m,mito value for ADP of 20·µmol·l -1 was used, which is within the range for fast skeletal muscle (Meyer et al, 1984). AK dissociation constants were obtained from Smith and Morrison (1969), V m,AK,rev was taken from Zammitt and Newsholme (1976) and V m,AK,for was calculated from the AK Haldane relationship from Smith and Morrison (1969) using an equilibrium constant for AK of 39 (Teague and Dobson, 1999). Values for V m,myo and K m,myo were the same as in Hubley et al (1997).…”

Section: Mathematical Modelingmentioning

confidence: 99%

Does intracellular metabolite diffusion limit post-contractile recovery in burst locomotor muscle?

Kinsey

Pathi

Hardy

et al. 2005

Journal of Experimental Biology

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“…The basal ATPase maximal velocity (V m,bas ) and K m (K m,bas ) for ATP were estimated so as to maintain constant resting concentrations over time in an inactive fiber and to promote a return to the initial steady state following contraction, and these values are similar to basal ATPase rates estimated for skeletal muscle (Vicini and Kushmerick, 2000). AK dissociation constants were obtained from Smith and Morrison (Smith and Morrison, 1969), the maximal velocity for the reverse reaction (V m,AK,rev ) was taken from measurements in blue crab dark levator muscle (Holt and Kinsey, 2002), and the maximal velocity for the forward reaction (V m,AK,for ) was calculated from the AK Haldane relationship from Smith and Morrison (Smith and Morrison, 1969) using an equilibrium constant for AK of 40 (Teague and Dobson, 1999). The myosin ATPase maximal velocity (V m,myo ) and K m (K m,myo ) for ATP were the same as used for aerobic muscle by Hubley et al (Hubley et al, 1997).…”

Section: Mathematical Modelingmentioning

confidence: 99%

“…Model input parameters are detailed in Table·2. The resting metabolite concentrations for crustacean aerobic locomotor fibers were obtained from data gathered during this study and calculations using the AK equilibrium constant (Teague and Dobson, 1999). Metabolite data, expressed as mol·g -1 muscle tissue, were converted to mmol·l -1 by assuming that intracellular water accounted for 68% of the wet mass in blue crab dark levator muscle (Milligan et al, 1989).…”

Section: Mathematical Modelingmentioning

confidence: 99%

A reaction-diffusion analysis of energetics in large muscle fibers secondarily evolved for aerobic locomotor function

Hardy

Locke

Silva

et al. 2006

Journal of Experimental Biology

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SUMMARY The muscles that power swimming in the blue crab, Callinectes sapidus, grow hypertrophically, such that in juvenile crabs the cell diameters are <60 μm, whereas fibers of the adult crabs often exceed 600μm. Thus, as these animals grow, their muscle fibers greatly exceed the surface area to volume ratio and intracellular diffusion distance limits of most cells. 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. By contrast, the aerobic (dark) fibers have evolved an intricate network of intracellular subdivisions that maintain an effectively small `metabolic diameter' throughout development. In the present study, we examined the impact of intracellular metabolite diffusive flux on the rate of post-contractile AP resynthesis in the dark muscle, which has a much higher aerobic capacity than the light muscle. AP recovery was measured for 60 min in adults and 15 min in juveniles following burst contractile activity in dark fibers, and a mathematical reaction-diffusion model was used to test whether the observed aerobic rates of AP resynthesis were fast enough to be limited by intracellular metabolite diffusion. Despite the short diffusion distances and high mitochondrial density, the AP recovery rates were relatively slow and we found no evidence of diffusion limitation. However, during simulation of steady-state contraction, which is an activity more typical of the dark fibers, there were substantial intracellular metabolite gradients, indicative of diffusion limitation. This suggests that high ATP turnover rates may lead to diffusion limitation in muscle even when diffusion distances are short, as in the subdivided dark fibers.

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Thermodynamics of the Arginine Kinase Reaction

Cited by 30 publications

References 14 publications

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

Does intracellular metabolite diffusion limit post-contractile recovery in burst locomotor muscle?

A reaction-diffusion analysis of energetics in large muscle fibers secondarily evolved for aerobic locomotor function

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