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DAHP synthase
From Proteopedia
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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. | + | '''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. <scene name='70/708806/Cv/2'>DAHPS is a tetramer</scene>. DAHPS exhibits feedback inhibition by aromatic amino acids like tyrosine, phenylalanine and tryptophan.<ref>PMID:1682314</ref> |
== Structural highlights == | == Structural highlights == | ||
Revision as of 08:30, 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
