DAHP synthase: Difference between revisions
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Michal Harel (talk | contribs) 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=''> | ||
== 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> | ||
