Evolution of putrescine N-methyltransferase from spermidine synthase demanded alterations in substrate binding.

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 Lett

journal_title

FEBS letters

authors

Biastoff S,Reinhardt N,Reva V,Brandt W,Dräger B

doi

10.1016/j.febslet.2009.09.043

subject

Has Abstract

pub_date

2009-10-20 00:00:00

pages

3367-74

issue

20

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00743-1

journal_volume

583

pub_type

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