Amino acid biosynthesis : new architectures in allosteric enzymes
This review focuses on the allosteric controls in the Aspartate-derived and the branched-chain amino acid biosynthetic pathways examined both from kinetic and structural points of view. The objective is to show the differences that exist among the plant and microbial worlds concerning the allosteric...
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 46(2008), 3 vom: 01. März, Seite 325-39 |
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| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2008
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| Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
| Schlagworte: | Journal Article Review Amino Acids Bacterial Proteins Enzymes Plant Proteins Carbon-Oxygen Lyases EC 4.2.- threonine synthase EC 4.2.3.1 |
| Zusammenfassung: | This review focuses on the allosteric controls in the Aspartate-derived and the branched-chain amino acid biosynthetic pathways examined both from kinetic and structural points of view. The objective is to show the differences that exist among the plant and microbial worlds concerning the allosteric regulation of these pathways and to unveil the structural bases of this diversity. Indeed, crystallographic structures of enzymes from these pathways have been determined in bacteria, fungi and plants, providing a wonderful opportunity to obtain insight into the acquisition and modulation of allosteric controls in the course of evolution. This will be examined using two enzymes, threonine synthase and the ACT domain containing enzyme aspartate kinase. In a last part, as many enzymes in these pathways display regulatory domains containing the conserved ACT module, the organization of ACT domains in this kind of allosteric enzymes will be reviewed, providing explanations for the variety of allosteric effectors and type of controls observed |
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| Beschreibung: | Date Completed 21.07.2008 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 0981-9428 |
| DOI: | 10.1016/j.plaphy.2007.12.006 |