Thermal Bifunctionality of Bacterial Phenylalanine Aminomutase and Ammonia Lyase Enzymes

被引：35

作者：

Chesters, Christopher ^{[1
,2
]}

Wilding, Matthew ^{[1
,2
]}

Goodall, Mark ^{[1
,2
]}

Micklefield, Jason ^{[1
,2
]}

机构：

[1] Univ Manchester, Sch Chem, Manchester M1 7DN, Lancs, England

[2] Univ Manchester, Manchester Interdisciplinary Bioctr, Manchester M1 7DN, Lancs, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2012年 / 51卷 / 18期

基金：

英国生物技术与生命科学研究理事会;

关键词：

aminomutases; ammonia lyases; enzymes; enzyme catalysis; ss-amino acids; 4-METHYLIDENEIMIDAZOLE-5-ONE-CONTAINING TYROSINE AMINOMUTASE; VISCOSITY DEPENDENCE; CRYSTAL-STRUCTURE; ACTIVE-SITE; MECHANISM; PROMISCUITY; IMPROVEMENT; SUBSTRATE;

D O I：

10.1002/anie.201200669

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Enzymatic thermal switch: The bacterial 4-methylideneimidazol-5-one (MIO) dependent enzymes AdmH and EncP are shown to display remarkable thermal bifunctionality: they act as mutases (blue graph) at lower temperatures but with lyase (red graph) activity predominant at higher temperatures. This temperature-dependent switch in enzyme class also explains how these two similar enzymes can fulfill different catalytic functions in secondary metabolisms. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

收藏

页码：4344 / 4348

页数：5

相关论文

共 32 条

[1] Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase [J].

Arnett, Samantha O. ;

Gerratana, Barbara ;

Townsend, Craig A. .

BIOCHEMISTRY, 2007, 46 (32) :9337-9345

[2]

Bartsch S., 2009, ANGEW CHEM, V121, P3412

[3] A Single Residue Influences the Reaction Mechanism of Ammonia Lyases and Mutases [J].

Bartsch, Sebastian ;

Bornscheuer, Uwe T. .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2009, 48 (18) :3362-3365

[4] Solvent effects on stereoselectivity: more than just an environment [J].

Cainelli, Gianfranco ;

Galletti, Paola ;

Giacomini, Daria .

CHEMICAL SOCIETY REVIEWS, 2009, 38 (04) :990-1001

[5] Crystal structure of phenylalanine ammonia lyase: Multiple helix dipoles implicated in catalysis [J].

Calabrese, JC ;

Jordan, DB ;

Boodhoo, A ;

Sariaslani, S ;

Vannelli, T .

BIOCHEMISTRY, 2004, 43 (36) :11403-11416

[6] Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis [J].

Christenson, SD ;

Wu, WM ;

Spies, MA ;

Shen, B ;

Toney, MD .

BIOCHEMISTRY, 2003, 42 (43) :12708-12718

[7] A novel 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis [J].

Christenson, SD ;

Liu, W ;

Toney, MD ;

Shen, B .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (20) :6062-6063

[8] The mechanism of MIO-based aminomutases in β-amino acid biosynthesis [J].

Christianson, Carl V. ;

Montavon, Timothy J. ;

Festin, Grace M. ;

Cooke, Heather A. ;

Shen, Ben ;

Bruner, Steven D. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2007, 129 (51) :15744-+

[9] The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway [J].

Christianson, Carl V. ;

Montavon, Timothy J. ;

Van Lanen, Steven G. ;

Shen, Ben ;

Bruner, Steven D. .

BIOCHEMISTRY, 2007, 46 (24) :7205-7214

[10] Probing the Active Site of MIO-Dependent Aminomutases, Key Catalysts in the Biosynthesis of β-Amino Acids Incorporated in Secondary Metabolites [J].

Cooke, Heather A. ;

Bruner, Steven D. .

BIOPOLYMERS, 2010, 93 (09) :802-810

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