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DAHP synthase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The bivalent metal is bound to a Cys-X-X-His motif. The DAHPS active site is located in a channel at the C-terminal of the enzyme where the substrate (PEP), inhibitor (phenylalanine) and the metal ion (Mn+2) are seen.<ref>PMID:12126632</ref> | + | The <scene name='70/708806/Cv/3'>bivalent metal is bound to a Cys-X-X-His motif</scene>. The DAHPS active site is located in a channel at the C-terminal of the enzyme where the substrate (PEP), inhibitor (phenylalanine) and the metal ion (Mn+2) are seen.<ref>PMID:12126632</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 08:44, 28 December 2015
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3D Structures of DAHP synthase
Updated on 28-December-2015
References
- ↑ Stephens CM, Bauerle R. Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. J Biol Chem. 1991 Nov 5;266(31):20810-7. PMID:1682314
- ↑ Shumilin IA, Zhao C, Bauerle R, Kretsinger RH. Allosteric inhibition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase alters the coordination of both substrates. J Mol Biol. 2002 Jul 26;320(5):1147-56. PMID:12126632
