Words similar to catalytic
Example sentences for: catalytic
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AC Activated carbon ACI Activated carbon injection CAAA Clean Air Act Amendments DCS Distributed control system ESP Electrostatic precipitator FF Fabric filter FGD Flue gas desulfurization GWe Gigawatt (electric) IPM Integrated Planning Model LSD Lime spray dryer LSFO Limestone forced oxidation MEL Magnesium enhanced lime MWe Megawatt (electric) NAAQS National Ambient Air Quality Standards PJFF Pulsejet fabric filter PLC Programmable logic controller SCR Selective catalytic reduction SIP State Implementation Plan TVA Tennessee Valley Authority
NTPDases do not form phosphorylated intermediates during catalysis, a conclusion also supported by lack of vanadate sensitivity and Pi product inhibition [ 3 4 5 6 ] . The catalytic reaction appears to be irreversible and no partial reactions have been observed [ 7 8 ] . Divalent cations like Ca 2+or Mg 2+are required for activity, and maximal activity is reached when the concentrations of substrates and divalent cations are equal [ 1 ] . The specific activities of NTPDases vary over a broad range from ten thousand units for potato apyrase to less than one hundred units for chicken gizzard ecto-ATPase [ 9 10 ] . Sequence comparisons indicate that most of NTPDases contain five highly conserved regions, apyrase conserved region, ACR1 - ACR5 [ 9 11 ] . However, the catalytic sites have not been identified, although ACR1 and ACR4 have been implicated in β- and γ-phosphate binding, respectively [ 9 ] .
Of these, four subunits, which correspond to the bacterial α, β, β' and ω, are universally present in all cellular DDRPs and constitute the conserved DDRP core [ 7 ] . Orthologs of the β and β' subunits are also encoded in the genomes of several families of large eukaryotic DNA viruses [ 33 34 35 ] . Biochemical studies have shown that the catalytic site of DDRP resides in the β' subunit and contains three invariant aspartates that coordinate a Mg 2+cation [ 22 23 24 36 ] . Recent structural analyses demonstrated that the core of DDRP is assembled around the β and β' subunits, which interact with each other to form a positively charged nucleic-acid-binding cleft.
Along with the LRAT proteins, these proteins contain a second conserved cysteine (red letters in Figure 1), carboxy-terminal to the catalytic cysteine.
The details of the catalytic mechanism of these enzymes have been revealed by determination of the crystal structures of isopenicillin N synthase (IPNS), deacetoxycephalosporin C synthase (DAOCS) and clavaminic acid synthase (CAS) [ 8, 9, 10, 11].
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