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- **************************************************
- * Intradiol ring-cleavage dioxygenases signature *
- **************************************************
-
- 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 alpha and a beta
- 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.
-
- -Consensus pattern: [LIVM]-x-G-x-[LIVM]-x(4)-[GS]-x(2)-[LIVM]-x(4)-[LIVM]-
- [DE]-[LIVMFY]-x(6)-G-x-[FY]
- [Y is an iron ligand]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Expert(s) to contact by email: Harayama S.
- sharayam@ddbj.nig.ac.jp
-
- -Last update: October 1993 / Text revised.
-
- [ 1] Harayama S., Rekik M.
- J. Biol. Chem. 264:15328-15333(1989).
- [ 2] Ohlendorf D.H., Lipscomb J.D., Weber P.C.
- Nature 336:403-405(1988).
-