Back 3-Dehydrochinat-Synthase German 3-Déshydroquinate synthase French 3-deidrochinato sintasi Italian 3-Dehidrohinatna sintaza Serbo-Croatian 3-Dehidrohinatna sintaza Serbian
| 3-dehydroquinate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Ribbon representation of the Helicobacter pylori 3-dehydroquinate synthase.[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 4.2.3.4 | ||||||||
| CAS no. | 37211-77-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| 3-dehydroquinate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3-Dehydroquinate synthase homodimer, Aspergillus nidulans | |||||||||
| Identifiers | |||||||||
| Symbol | DHQ_synthase | ||||||||
| Pfam | PF01761 | ||||||||
| InterPro | IPR002658 | ||||||||
| SCOP2 | 1dqs / SCOPe / SUPFAM | ||||||||
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The enzyme 3-dehydroquinate synthase (EC 4.2.3.4) catalyzes the chemical reaction
- [[3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate]] 3-dehydroquinate + phosphate
The protein uses NAD+ to catalyze the reaction.[2][3] This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
3-Dehydroquinate synthase belongs to the family of lyases, to be specific those carbon-oxygen lyases acting on phosphates. This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis. It employs one cofactor, cobalt (Co2+).
- ^ PDB: 3CLH; Liu JS, Cheng WC, Wang HJ, Chen YC, Wang WC (August 2008). "Structure-based inhibitor discovery of Helicobacter pylori dehydroquinate synthase". Biochemical and Biophysical Research Communications. 373 (1): 1–7. doi:10.1016/j.bbrc.2008.05.070. PMID 18503755.; rendered with MacPyMOL
- ^ Hawkins AR, Lamb HK (August 1995). "The molecular biology of multidomain proteins. Selected examples". European Journal of Biochemistry. 232 (1): 7–18. doi:10.1111/j.1432-1033.1995.tb20775.x. PMID 7556173.
- ^ Barten R, Meyer TF (April 1998). "Cloning and characterisation of the Neisseria gonorrhoeae aroB gene". Molecular & General Genetics. 258 (1–2): 34–44. doi:10.1007/s004380050704. PMID 9613570. S2CID 26380973.