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Code : 1F1X   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : CRYSTAL STRUCTURE OF HOMOPROTOCATECHUATE 2,3-DIOXYGENASE FROM BREVIBACTERIUM FUSCUM
Release Data : 2003-06-10
Compound :
mol_id molecule chains synonym
1 HOMOPROTOCATECHUATE 2,3-DIOXYGENASE A,B,C,D 3,4-DIHYDROXYPHENYLACETATE 2,3-DIOXYGENASE
ec: 1.13.11.15
Source :
mol_id organism_scientific expression_system
1 Brevibacterium fuscum  (taxid:47914) Escherichia coli  (taxid:562)
Authors : Vetting, M.W., Lipscomb, J.D., Wackett, L.P., Que Jr., L., Ohlendorf, D.H.
Keywords : Dioxygenase, Extradiol, Iron, Biodegradation, Aromatic, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.6 Å )
Citation :

Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.

Vetting, M.W.,Wackett, L.P.,Que Jr., L.  et al.
(2004)  J.Bacteriol.  186 : 1945 - 1958

PubMed: 15028678
DOI: 10.1128/JB.186.7.1945-1958.2004

Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A Dioxygenase with Catalase Activity.

Miller, M.A.,Lipscomb, J.D.
(1996)  J.Biol.Chem.  271 : 5524 - 5535

DOI: 10.1074/jbc.271.10.5524

Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum.

Wang, Y.Z.,Lipscomb, J.D.
(1997)  Protein Expr.Purif.  10 : 1 - 9

DOI: 10.1006/prep.1996.0703

Chain : A, B, C, D
UniProt : Q45135 (Q45135_9MICO)
Reaction : -