PROSITE documentation PDOC00788Dehydroquinase class I active site
3-dehydroquinate dehydratase (EC 4.2.1.10), or dehydroquinase, catalyzes the conversion of 3-dehydroquinate into 3-dehydroshikimate. It is the third step in the shikimate pathway for the biosynthesis of aromatic amino acids from chorismate. Two classes of dehydroquinases exist, known as types I and II. The best studied type I enzyme is from Escherichia coli (gene aroD) and related bacteria where it is a homodimeric protein of a chain of about 250 residues. In fungi, dehydroquinase is part of a multifunctional enzyme which catalyzes five consecutive steps in the shikimate pathway. In aroD, it has been shown [1] that a histidine is involved in the catalytic mechanism; we used the region around this residue as a signature pattern.
Last update:December 2001 / Pattern and text revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Deka R.K. Kleanthous C. Coggins J.R. |
Title | Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase. | |
Source | J. Biol. Chem. 267:22237-22242(1992). | |
PubMed ID | 1429576 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)