Remote Control by Inter-Enzyme Allostery: A Novel Paradigm for Regulation of the Shikimate Pathway
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- 作者：Steffi Munack1 ; 4 ; &dagger ; ; Kathrin Roderer2 ; &dagger ; ; Mats Ö ; kvist1 ; 3 ; 4 ; Jurate Kamarauskaite2 ; Severin Sasso2 ; 4 ; André ; van Eerde1 ; 4 ; Peter Kast2 ; kast@org.chem.ethz.ch" class="auth_mail" title="E-mail the corresponding author ; Ute Krengel1 ; ute.krengel@kjemi.uio.no" class="auth_mail" title="E-mail the corresponding author
- 关键词：AS ; anthranilate synthase ; CM ; chorismate mutase ; BTP ; (1 ; 3-bis[tris(hydroxymethyl)methylamino]propane) ; DAHP ; 3-deoxy-d-arabino-heptulosonate-7-phosphate or 3 ; DS ; DAHP synthase ; EcCM ; Escherichia coli chorismate mutase domain of the bifunctional CM-PDT (PheA) protein ; E4P ; d-erythrose-4-phosphate (2) ; MALS ; multi-angle light scattering ; MtCM ; Mycobacterium tuberculosis chorismate mutase encoded by Rv0948c ; MtDS ; M. tuberculosis DAHP synthase encoded by Rv2178c ; PDH ; prephenate dehydrogenase ; P
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：27 March 2016
- 年：2016
- 卷：428
- 期：6
- 页码：1237-1255
- 全文大小：2914 K
文摘
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In Mycobacterium tuberculosis, the shikimate pathway shows unusual features.
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The key branch point enzyme chorismate mutase has no own regulatory sites.
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Activation and feedback inhibition need reversible interaction with DAHP synthase.
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Crystal structures show how allosteric sites on DAHP synthase regulate both enzymes.
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'Inter-enzyme allostery' may be a general principle for efficient metabolic control.