Abstract:
:Putrescine N-methyltransferase (PMT) catalyses S-adenosylmethionine (SAM)-dependent methylation of putrescine in tropane alkaloid biosynthesis. PMT presumably evolved from the ubiquitous spermidine synthase (SPDS). SPDS protein structure suggested that only few amino acid exchanges in the active site were necessary to achieve PMT activity. Protein modelling, mutagenesis, and chimeric protein construction were applied to trace back evolution of PMT activity from SPDS. Ten amino acid exchanges in Datura stramonium SPDS dismissed the hypothesis of facile generation of PMT activity in existing SPDS proteins. Chimeric PMT and SPDS enzymes were active and indicated the necessity for a different putrescine binding site when PMT developed.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Biastoff S,Reinhardt N,Reva V,Brandt W,Dräger Bdoi
10.1016/j.febslet.2009.09.043subject
Has Abstractpub_date
2009-10-20 00:00:00pages
3367-74issue
20eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00743-1journal_volume
583pub_type
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