Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Homogeneous diadenosine 5',5'''-P1,P4-tetraphosphate alpha, beta-phosphorylase (Ap4A-phosphorylase), the enzyme recently found in yeast (Guranowski, A., and Blanquet, S. (1985) J. Biol. Chem. 260, 3542-3547) catalyzes an exchange reaction between the beta-phosphate of nucleoside diphosphate (NDP) and orthophosphate from the medium (Pi). The common purine and pyrimidine ribonucleoside diphosphates as well as ADP analogs modified either in aglycone, sugar, or at the anhydride bond beta-position are substrates. The Km and rate values for the NDP-Pi exchange reaction were estimated at pH optima. These optima are 6.5 for UDP, 7.0 for ADP or CDP, and 8.0 for GDP. In the presence of 10 mM K2HPO4, 0.1 mM EDTA, and 100 mM Hepes/KOH (pH 7.0), the Km for ADP is 0.7 mM with a rate constant at saturating ADP of 96 s-1. The Km value for orthophosphate is 2 mM. In the NDP-Pi exchange reaction, phosphate can be substituted with arsenate and apparent arsenolysis of NDPs yields corresponding nucleoside monophosphates. The same pH optimum of 6.5 is found for arsenolysis of ADP, GDP, and CDP. Whereas the Ap4A phosphorylase sulfhydryl groups are essential for catalyzing the Ap4A phosphorolysis, the NDP-Pi exchange reactions, and the arsenolysis of NDPs, the divalent metal ions (Mg2+, Mn2+, Ca2+, Co2+, and Cd2+), which had been shown to be essential cofactors of the former reaction, are not required for the two latter ones. Used at concentrations which are optimum for Ap4A phosphorolysis, the cations (particularly Mg2+ and Cd2+) inhibit the NDP-Pi exchange and the arsenolysis of NDPs. Interestingly, the Ap4A phosphorylase exhibits higher specificity for adenosine 5'-phosphosulfate (APS) than for any other NDP tested. The V/Km ratio is almost 5-fold higher with APS than with ADP. However, in the presence of orthophosphate, the APS is irreversibly converted to ADP. Thus, the enzyme displays a property already attributed to ADP-sulfurylase (EC 2.7.7.5), (Grunberg-Manago, M., Del Campillo-Campbell, A., Dondon, L., and Michelson, A. M. (1966) Biochim. Biophys. Acta 123, 1-16; Nicholls, R. G. (1977) Biochem. J. 165, 149-155).
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PMID:Diadenosine 5',5'''-P1, P4-tetraphosphate alpha, beta-phosphorylase from yeast supports nucleoside diphosphate-phosphate exchange. 300 35

The nonequilibrium gas flow in a two-dimensional microchannel with a ratchet surface and a moving wall is investigated numerically with a kinetic method [Guo et al., Phys. Rev. E 91, 033313 (2015)]PLEEE81539-375510.1103/PhysRevE.91.033313. The presence of periodic asymmetrical ratchet structures on the bottom wall of the channel and the temperature difference between the walls of the channel result in a thermally induced flow, and hence a tangential propelling force on the wall. Such thermally induced propelling mechanism can be utilized as a model heat engine. In this article, the relations between the propelling force and the top wall moving velocity are obtained by solving the Boltzmann equation with the Shakhov model deterministically in a wide range of Knudsen numbers. The flow fields at both the static wall state and the critical state at which the thermally induced force cancels the drag force due to the active motion of the top wall are analyzed. A counterintuitive relation between the flow direction and the shear force is observed in the highly rarefied condition. The output power and thermal efficiency of the system working as a model heat engine are analyzed based on the momentum and energy transfer between the walls. The effects of Knudsen number, temperature difference, and geometric configurations are investigated. Guidance for improving the mechanical performance is discussed.
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PMID:Numerical study of nonequilibrium gas flow in a microchannel with a ratchet surface. 2829 65