Abstract:
:The function of Lys-59, Arg-141, and Arg-277 in PAPS binding and catalysis of the flavonol 3-sulfotransferase was investigated. Affinity chromatography of conservative mutants with PAPS analogues allowed us to determine that Lys-59 interacts with the 5' portion of the nucleotide, while Arg-141 interacts with the 3' portion, confirming assignments deduced from the crystal structure of mouse estrogen sulfotransferase [Kakuta, Y., Pedersen, L. G., Carter, C. W. , Negishi, M., and Pedersen, L. C. (1997) Nat. Struct. Biol. 4, 904-908]. The affinity chromatography method could be used to characterize site-directed mutants for other types of enzymes that bind nucleoside 3',5'- or 2',5'-diphosphates. 31P NMR spectra of enzyme-PAP complexes were recorded for the wild-type enzyme and K59R and K59A mutants. The results of these experiments suggest that Lys-59 is involved in the determination of the proper orientation of the phosphosulfate group for catalysis.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Marsolais F,Laviolette M,Kakuta Y,Negishi M,Pedersen LC,Auger M,Varin Ldoi
10.1021/bi982239msubject
Has Abstractpub_date
1999-03-30 00:00:00pages
4066-71issue
13eissn
0006-2960issn
1520-4995pii
bi982239mjournal_volume
38pub_type
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