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1.13.11.54: acireductone dioxygenase [iron(II)-requiring]

This is an abbreviated version!
For detailed information about acireductone dioxygenase [iron(II)-requiring], go to the full flat file.

Word Map on EC 1.13.11.54

Reaction

1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one
+
O2
=
4-(methylsulfanyl)-2-oxobutanoate
 +
formate

Synonyms

1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, aci-reductone dioxygenase, acireductone dioxygenase, acireductone dioxygenase 1, ADI1, ARD, ARD', ARD1, ARD4, ARDp, Fe(II)-bound acireductone dioxygenase, Fe-ARD, MTCBP-1, MtnD, OsARD1, Ymr009p

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.54 acireductone dioxygenase [iron(II)-requiring]

Metals Ions

Metals Ions on EC 1.13.11.54 - acireductone dioxygenase [iron(II)-requiring]

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
enzyme contains 1 atom of Fe
Iron
ligands are H96, H98, E102 and H140, the same as in the isoform requiring Ni2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions
Mn2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Ni2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
additional information
the identity of bound metal ion does not affect the oligomeric state of ARD