Research article
Conservation of structure and activity in Plasmodium purine nucleoside phosphorylases
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* Corresponding author: R Leo Brady L.Brady@bris.ac.uk
1 Department of Biochemistry, University of Bristol, Bristol, BS8 1TD, UK
2 Current address: Oxford Structural Genomics Consortium, Oxford, UK
BMC Structural Biology 2009, 9:42 doi:10.1186/1472-6807-9-42
Published: 3 July 2009Additional files
Additional file 1:
Steady-state kinetic data for five purine nucleoside substrates for recombinant PNP enzymes. Table lists enzymatic constants derived in the current study, together with previously published data. Values for kcat assume one catalytic site per subunit; values for KM1, KM2, kcat1 and kcat2 for 2'-Deoxyinosine refer to Equation 2 in Methods.; Other values from a [8], b [21], c [22], d [23], e [24], andf [25].
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