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DAHP synthase
From Proteopedia
(Difference between revisions)
(New page: <StructureSection load='1oab' size='340' side='right' caption='Yeast DAHP synthase complex with Mn+2 ion and PEP (PDB code 1oab)' scene=''> '''DAHP synthase''' or '''3-deoxy-D-arabino...) |
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<StructureSection load='1oab' size='340' side='right' caption='Yeast DAHP synthase complex with Mn+2 ion and PEP (PDB code [[1oab]])' scene=''> | <StructureSection load='1oab' size='340' side='right' caption='Yeast DAHP synthase complex with Mn+2 ion and PEP (PDB code [[1oab]])' scene=''> | ||
| - | '''DAHP synthase''' or '''3-deoxy-D-arabino-heptulosonate 7-phosphate synthase''' (DAHPS) catalyzes the conversion of phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate to 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) and phosphate. DAHPS is part of the shikimate pathway. DAHPS requires a bivalent metal ion cofactor for normal activity. DAHPS is a tetramer. DAHPS exhibits feedback inhibition by aromatic amino acids like tyrosine, phenylalanine and tryptophan. | ||
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== Function == | == Function == | ||
| - | + | '''DAHP synthase''' or '''3-deoxy-D-arabino-heptulosonate 7-phosphate synthase''' (DAHPS) catalyzes the conversion of phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate to 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) and phosphate. DAHPS is part of the shikimate pathway. DAHPS requires a bivalent metal ion cofactor for normal activity. DAHPS is a tetramer. DAHPS exhibits feedback inhibition by aromatic amino acids like tyrosine, phenylalanine and tryptophan.<ref>PMID:1682314</ref> | |
| - | == | + | == 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> | |
</StructureSection> | </StructureSection> | ||
Revision as of 10:54, 21 December 2015
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3D Structures of DAHP synthase
Updated on 21-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
