PROSITE documentation PDOC00079

Intradiol ring-cleavage dioxygenases signature




Description

Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates. Cleavage of aromatic rings is one of the most important function of dioxygenases. The substrates of ring-cleavage dioxygenases can be classified into two groups according to the mode of scission of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and another adjacent nonhydroxylated carbon [1]. Intradiol dioxygenases require a nonheme ferric ion as a cofactor. The enzymes that belong to this family are:

  • Protocatechuate 3,4-dioxygenase (EC 1.13.11.3) (3,4-PCD), an oligomeric enzyme complex which consists of 12 copies each of an α and a β subunits. Both subunits are evolutionary related.
  • Catechol 1,2-dioxygenase (EC 1.13.11.1) (gene catA or clcA).
  • Chlorocatechol 1,2-dioxygenase (EC 1.13.11.1) (gene tfdC).

As a signature pattern for these enzymes we selected a region that includes a tyrosine residue which, in 3,4-PCD, has been shown [2], to be implicated in the binding of the ferric iron atom.

Expert(s) to contact by email:

Harayama S.

Last update:

December 2004 / Pattern and text revised.

Technical section

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

INTRADIOL_DIOXYGENAS, PS00083; Intradiol ring-cleavage dioxygenases signature  (PATTERN)


References

1AuthorsHarayama S., Rekik M.
TitleBacterial aromatic ring-cleavage enzymes are classified into two different gene families.
SourceJ. Biol. Chem. 264:15328-15333(1989).
PubMed ID2670937

2AuthorsOhlendorf D.H., Lipscomb J.D., Weber P.C.
TitleStructure and assembly of protocatechuate 3,4-dioxygenase.
SourceNature 336:403-405(1988).
PubMed ID3194022
DOI10.1038/336403a0



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)