DAHP synthase: Difference between revisions
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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. <scene name='70/708806/Cv/ | '''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/6'>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 == | ||
The DAHPS active site is located in a channel at the C-terminal of the enzyme where the <scene name='70/708806/Cv/ | The DAHPS active site is located in a channel at the C-terminal of the enzyme where the <scene name='70/708806/Cv/7'>substrate (PEP)</scene>, <scene name='70/708806/Cv/8'>inhibitor (phenylalanine)</scene> and <scene name='70/708806/Cv/9'>metal ion (Mn+2)</scene> are seen. The bivalent metal is bound to a Cys-X-X-His motif.<ref>PMID:12126632</ref> | ||
</StructureSection> | </StructureSection> | ||
