DAHP synthase

From Proteopedia

Jump to: navigation, search

Function

DAHP synthase or 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase or phospho-2-dehydro-3-deoxyheptonate aldolase (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.[1]

Structural highlights

The DAHPS active site is located in a channel at the C-terminal of the enzyme where the substrate (PEP), inhibitor (phenylalanine) and metal ion (Mn+2) are seen. The bivalent metal is bound to a Cys-X-X-His motif.[2]

3D Structures of DAHP synthase

DAHP synthase 3D structures


E. coli DAHP synthase complex with PEP, phenylalanine, sulfate and Mn+2 ion (PDB code 1kfl)

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/DAHP_synthase"
Personal tools