Conservation of structure and activity in Plasmodium purine nucleoside phosphorylases

doi:10.1186/1472-6807-9-42

BMC Structural Biology

Volume 9

Viewing options:

Abstract
Full text
PDF (1.7MB)
Additional files

Associated material:

Related literature:

Articles citing this article
on Google Scholar
on ISI Web of Science
on PubMed Central
Other articles by authors
on Google Scholar

Chaikuad A
Brady RL

on PubMed

Chaikuad A
Brady RL
Related articles/pages
on Google

on Google Scholar

on PubMed

Tools:

Nominate for award

Post to:

Research article

Conservation of structure and activity in Plasmodium purine nucleoside phosphorylases

Apirat Chaikuad¹^,2 and R Leo Brady¹

¹Department of Biochemistry, University of Bristol, Bristol, BS8 1TD, UK

²Current address: Oxford Structural Genomics Consortium, Oxford, UK

author email corresponding author email

BMC Structural Biology 2009, 9:42doi:10.1186/1472-6807-9-42


Published:	3 July 2009

Additional 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 k_catassume one catalytic site per subunit; values for K_M1, K_M2, k_cat1and k_cat2for 2'-Deoxyinosine refer to Equation 2 in Methods.; Other values from ^a[8], ^b[21], ^c[22], ^d[23], ^e[24], and^f[25].

Format: DOC Size: 108KB Download file

This file can be viewed with: Microsoft Word Viewer