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Literature summary for 1.13.11.15 extracted from

  • Vetting, M.W.; Wackett, L.P.; Que, L.Jr.; Lipscomb, J.D.; Ohlendorf, D.H.
    Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases (2004), J. Bacteriol., 186, 1945-1958.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ located in C-terminal barrel Brevibacterium fuscum
Mn2+
-
Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
-
-
Brevibacterium fuscum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde mechanism, substrate chelates the metal ion asymmetrically at sites trans to two imidazole ligands Arthrobacter globiformis
3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde mechanism, substrate chelates the metal ion asymmetrically at sites trans to two imidazole ligands Brevibacterium fuscum

Subunits

Subunits Comment Organism
homotetramer crystallization data Arthrobacter globiformis
homotetramer crystallization data Brevibacterium fuscum