3-dehydroquinate synthase

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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
3-dehydroquinate synthase
3-Dehydroquinate synthase homodimer, Aspergillus nidulans
Identifiers
SymbolDHQ_synthase
PfamPF01761
InterProIPR002658
SCOP21dqs / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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+).

The reaction catalyzed by 3-dehydroquinate synthase
  1. ^ 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
  2. ^ 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.
  3. ^ 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.