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| == Function == | | == Function == |
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| '''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> | | '''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> |
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| == Structural highlights == | | == Structural highlights == |
Revision as of 08:30, 28 December 2015
| 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.[1]
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.[2]
- ↑ 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
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3D Structures of DAHP synthase
Updated on 28-December-2015
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- DAHP synthase
- 1vr6 - TmDAHPS – Thermotoga maritima
- 3pg8 - TmDAHPS catalytic domain
- 1ofp - yDAHPS – yeast
- 1ofb, 1ofq - yDAHPS + Mn
- 4uma, 4umb, 4umc - NmDAHPS + Mn – Nisseria meningitidis
- 4ixx - NmDAHPS (mutant) + Mn
- 3tqk - DAHPS + Mn – Francisella tularensis
- DAHP synthase binary complex
- 4hsn - NmDAHPS + Mn + PEP
- 4c1k - PfDAHPS + Cd + PEP – Pyrococcus furiosus
- 1zco - PfDAHPS + Mn + PEP
- 1of6 - yDAHPS + Mn + tyrosine
- 1hfb - yDAHPS + PEP
- 1oab - yDAHPS + Mn + PEP
- 1ofa - yDAHPS + Co + PEP
- 1ofr - yDAHPS + Mn + phenylalanine
- 1og0 - yDAHPS (mutant) + Mn + phenylalanine
- 2b7o - MtDAHPS + Mn + PEP – Mycobacterium tuberculosis
- 3nud - MtDAHPS + phenylalanine
- 2ypo - MtDAHPS + Mn + phenylalanine
- 3nue - MtDAHPS + Mn + tryptophan
- 2ypp - MtDAHPS + Mn + tyrosine
- 3nv8 - MtDAHPS + Mn + PEP
- 3pfp - MtDAHPS + Mn + inhibitor
- 1qr7 - EcDAHPS + Pb + PEP – Escherichia coli
- 1gg1 - EcDAHPS + Mn + phosphoglycolate
- 1n8f – EcDAHPS (mutant) + Mn + PEP
- 1ofo - yDAHPS + phosphoglycolate
- 1vs1 - DAHPS + Mn + PEP – Aeropyrum pernix
- 2w19 - MtDAHPS + chorismate mutase
- DAHP synthase ternary complex
- 1of8 - yDAHPS + Co + PEP + glycerol-3-phosphate
- 1rzm - TmDAHPS + Cd + PEP + erythrose-4-phosphate
- 3pg9 – TmDAHPS + tyrosine + inhibitor
- 1kfl - EcDAHPS + Mn + PEP + phenylalanine
- 4hso - MnDAHPS (mutant) + Mn + PEP + tyrosine
- 2w1a - MtDAHPS + Mn + TSA + chorismate mutase
- 3kgf, 3rzi - MtDAHPS + Mn + phenylalanine + tryptophan
- 2ypq - MtDAHPS + Mn + tyrosine + tryptophan
References
