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

被引：16

作者：

Biastoff, Stefan ^{[1
]}

Reinhardt, Nicole ^{[1
]}

Reva, Veaceslav ^{[2
]}

Brandt, Wolfgang ^{[3
]}

Draeger, Birgit ^{[1
]}

机构：

[1] Univ Halle Wittenberg, Fac Sci 1, Inst Pharm, D-06120 Halle, Germany

[2] State Univ Moldova, Fac Biol & Soil Sci, MD-2009 Kishinev, Moldova

[3] Leibniz Inst Plant Biochem, Dept Bioorgan Chem, D-06120 Halle, Germany

来源：

FEBS LETTERS | 2009年 / 583卷 / 20期

关键词：

Putrescine N-methyltransferase; S-Adenosylmethionine; Spermidine synthase; Alkaloid biosynthesis; Protein evolution; QUALITY ASSESSMENT; S-ADENOSYLMETHIONINE; CRYSTAL-STRUCTURE; CALYSTEGINES; MODEL; SERVER;

D O I：

10.1016/j.febslet.2009.09.043

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：3367 / 3374

页数：8

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