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- **************************************************
- * Extradiol 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. Extradiol dioxygenases are
- usually multimeric and bind one atom of ferrous ion per subunit. It has been
- shown [1] that the known extradiol dioxygenases are evolutionary related. The
- enzymes that belong to this family are:
-
- - Catechol 2,3-dioxygenase (EC 1.13.11.2) (metapyrocatechase) (genes nahH,
- xylE, dmpB, mcpII, and pheB).
- - 3-methylcatechol 2,3-dioxygenase (EC 1.13.11.-) (gene todE).
- - Biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) (gene bphC).
- - 1,2-dihydroxynaphthalene dioxygenase (EC 1.13.11.-) (gene nahC).
-
- As a signature pattern for these enzymes we selected a region that includes
- four conserved residues. Among them are an histidine and a tyrosine which
- could be implicated in the binding of the ferrous iron atom.
-
- -Consensus pattern: [GNT]-x-H-x(7)-[LIVMF]-Y-x(2)-[DENT]-P-x-[GP]-x(2,3)-E
- -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 / Pattern and text revised.
-
- [ 1] Harayama S., Rekik M.
- J. Biol. Chem. 264:15328-15333(1989).
-