Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2.

doi:10.1021/bi962362i

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Article

Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2.

Biochemistry - 25 Feb 1997

Boldt Y R, Whiting A K, Wagner M L, Sadowsky M J, Que L, Wackett L P

Abstract excerpt

Whereas all other members of the extradiol-cleaving catechol dioxygenase family are iron-dependent, the 3,4-dihydroxyphenylacetate 2,3-dioxygenase (MndD) from Arthrobacter globiformis CM-2 is dependent on manganese for catalytic activity. Recently, the endogenous iron ligands of one family member...

Topics

Amino Acid Sequence
Arthrobacter
Binding Sites
Dioxygenases
Manganese
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Oxygenases

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