The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Alternative substrates for calf intestinal adenosine deaminase. A pre-steady-state kinetic analysis.

The protein fluorescence of adenosine deaminase ( ADA) was perturbed during the deamination of adenosine and four analogues of adenosine. The kinetics for the approach to the steady-state during turnover were monitored by fluorescence changes associated with formation of enzymatic intermediates. These kinetic data and the steady-state kinetic data were analyzed in terms of the kinetic scheme as follows. [formula: see text] The steady-state turnover number was assigned to k2, which was 244 s-1 for adenosine and 1.1 x 10(-3) s-1 for 6-methylamino-2-aminopurine arabinoside (aMDAP). Values for the association rate constants, k1, and the dissociation rate constants, k-1, were calculated from the kinetics for the approach to the steady state. k1 varied from 31 x 10(6) M-1 s-1 for adenosine to 2.8 x 10(6) M-1 s-1 for N-6-methyladenine arabinoside. k-1 varied from 500 s-1 for adenosine to 31 s-1 for aMDAP. The latter value was confirmed (22 s-1) by spectrofluorometrically monitoring the trapping of ADA by excess erythro-9-(2-hydroxy-3-nonyl) adenine as aMDAP.ADA dissociated. The ratio of k2 to k-1, which determines the commitment to catalysis, decreased from 0.49 for adenosine to 3.5 x 10(-5) for aMDAP. The Km values calculated from k1, k-1, and k2 were similar to the values determined from steady-state kinetic data. The spectrum of enzyme-bound aMDAP resembled protonated aMDAP.[1]


WikiGenes - Universities