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PROSITE documentation PDOC00788

Dehydroquinase class I active site

Description:

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.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

DEHYDROQUINASE_I, PS01028Dehydroquinase class I active site  (PATTERN)
Consensus pattern: D - [LIVM] - [DE] - [LIVMN] - x(18,20) - [LIVM](2) - x - [SC] - [NHY] - H - [DN]
H is the active site residue
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE
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Matching PDB structures: 1GQN 1L9W 1QFE 2EGZ ... [ALL]

Reference:

1 AuthorsDeka R.K., Kleanthous C., Coggins J.R.
TitleIdentification of the essential histidine residue at the active site of Escherichia coli dehydroquinase.
SourceJ. Biol. Chem. 267:22237-22242(1992).
PubMed ID1429576

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